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Pulse Proteins: From Processing to Structure-Function Relationships
By Ashish Singhal, Asli Can Karaca, Robert Tyler and Michael Nickerson
Submitted: September 29th 2015Reviewed: April 29th 2016Published: October 19th 2016
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Interest in alternative protein sources to those derived from animal, soy and wheat is on the rise, as consumers are searching for lower cost, healthier alternatives without compromising product quality and safety. Pulses are rich in protein, carbohydrates, vitamins and minerals and are low in fat. Although pea proteins experience greater integration into the plant protein ingredient market than others, lentil, chickpea, bean and faba beans are not far behind. This review discusses approaches used for extracting pulse proteins used to produce protein products (concentrates/isolates), mechanism driving structure-function relationships as well as potential applications.
Pulse proteins
structure-function and applications
Legumin: Vicilin
Ashish Singhal
Department of Food and Bioproduct Sciences, University of Saskatchewan, Canada
Asli Can Karaca
Aromsa A.S. GOSB 700, Gebze, Kocaeli, Turkey
Robert Tyler
Michael Nickerson*
*Address all correspondence to: michael.nickerson@usask.ca
Grain LegumesEdited by Aakash Goyal
Grain Legumes
Edited by Aakash Kumar Goyal
Pulses such as beans, peas and lentils have been consumed for thousands of years and represent one of the most extensively consumed food in the world [1]. Pulses play crucial roles in fulfilling the nutritional requirements of the growing population in a cost effective manner, especially for developing or underdeveloped countries where animal protein consumption is either limited or expensive [2]. Pulses are widely used for food purposes because of their high protein content, high nutritional and health beneficial properties, appropriate functional attributes, and associated low production cost and abundance [3]. The health benefits associated with pulse consumption include lowering of cholesterol levels, reducing the risks of various cardiovascular diseases and cancers, and decreasing the risk of type-2 diabetes [4]. Along with protein, pulses provides dietary fiber and vitamins and minerals such as iron, zinc, folate, and magnesium [1]. Pulses also have an antioxidant and anti-carcinogenic effect because of the presence of phytochemicals, saponins and tannins in them [1].
For many years, pulses have been used in the preparation of wholesome nutritional meals in combination with other food sources or ingredients. Pulse crops such as pea, chickpea and common bean (Phaseolus vulgaris L.), when blended with regionally grown cereal grains, could be of immense value in helping to fulfill the nutritional requirements of people relying just on mono-carbohydrate diets [5]. However, the nutritional quality of pulses is limited because of the presence of heat labile and heat stable anti-nutritional factors (ANFs) [2]. The ANFs include proteins such as lectins and protease inhibitors, and other compounds such as phytate, tannins, saponins, and alkaloids [2]. The negative impact of these ANFs on consumption of pulses in human and animal diets has been extensively reported [6]. However, the processed forms of legumes (flours, concentrates or isolates) are reported to have lower levels of ANFs than their corresponding raw material (seeds) [7]. For instance, during the germination process, legumes were found to have a higher digestibility, soluble protein [8] and dietary fiber [9, 10], and reduced levels of ANFs [11]. Furthermore, protein isolates prepared by extraction or precipitation methods were also found to have reduced anti-nutritional factors such as trypsin inhibitors, glycosides (such as convicine and vicine) and hemagglutinins which would otherwise impair protein digestion and could be toxic for human consumption [5, 12–14]. The exploitation of protein isolates or concentrates in new food formulations is of great importance because of their high nutrition and functionality [15]. The utilization of right individual functional properties might be useful in producing different food products such as cakes, biscuits, beverages and breads.
2. Protein structure and legumin/vicilin (L/V) ratio
The majority of pulse proteins are albumin and globulin fractions, where globulins represent ∼70% and albumins constitute 10–20% of the total pulse protein [5, 16]. In addition, other proteins are present in minor proportions such as prolamins and glutelins [17, 18]. These four proteins can be classified according to their solubility in various solvents based on the Osborne classification scheme [19]. For example, globulin proteins are soluble in dilute salt solution, albumins in water, prolamins in 70% ethanol solution, and glutelins are solubilized in dilute alkali solutions [19, 20].
Albumins encompass structural and enzymatic proteins, lectins and protease inhibitors, with their overall molecular mass (MM) ranging between 5 and 80 kDa [5]. In contrast, the salt soluble globulins include legumin (11S, S = Svedberg Unit) and vicilin (7S) proteins. The 11S fraction is a hexamer (MM of ∼340–360 kDa) comprised of six subunits (MM of ∼60 kDa) linked by non-covalent interactions. Each subunit pair is comprised of an acidic (MM of ∼40 kDa) and basic (MM of ∼20 kDa) chain joined by a disulfide bond [16, 21]. In contrast, the 7S fraction is a trimer with a MM of ∼175–180 kDa, and lacks disulfide bridging [5]. Vicilin protein molecules also have been reported to have various subunits of 75, 43, 33, 56, 12 and 25 kDa [16, 21]. A third type of globulin is also present, although in lesser amounts as compared to other globulins, and is known as convicilin [22]. It is a 7S globulin, and a single convicilin molecule has an overall MM of 220–290 kDa, and consists of 3 or 4 subunits each with a MW of 70 kDa. This protein has a different amino acid profile than vicilin as it contains sulfur-containing amino acids, is immunologically similar to 7S vicilin, and contains very little carbohydrate [5]. Various pulse species have been reported to contain convicilin-type proteins. For example, Saenz de Miera et al. [23] investigated 29 different legume species from 4 genera (Pisum, Lens, Vicia and Lathyrus spp.), and reported the presence of 34 new convicilin gene sequences. All of the above studies considered convicilin as a third class of globulin molecules. However, O'Kane et al. [24] deny the consideration of convicilin as a third pea globulin based on their findings and reported that convicilin (a polypeptide) should be denoted as the R-subunit of pea vicilin molecules (salt extracted).
The ratio of legumin:vicilin (L/V) is not fixed and may vary among different pulse varieties and species. The ratio of L/V for pea, soybean and faba bean varies in the range of 0.2–8.0, 1.3–3.4 and 1.7–3.7, respectively [25–35]. Various studies reported that L/V ratio for wrinkled pea seeds (0.2–0.6) represents a smaller ratio compared to the smooth pea seeds (0.3–2.0) [28, 30, 35, 36]. Various factors including the methods used in the preparation of protein materials (concentrates or isolates), processing parameters like pH and temperature and environmental or agronomic factors may account for the variation in these ratios, which in turn could also have influential effects on the physiochemical properties of pulse protein materials [16, 21, 37, 38]. As a part of their studies, Barac et al. [38] extracted the proteins from six varieties (genotypes) of pea (Calvedon, L1, L2, L3, Maja and M.A) and indicated that genotypes with high 7S protein levels or low 11S protein levels yielded higher amounts of protein (protein extractability) compared to the other genotypes. Moreover, pure vicilin solutions were observed to have better functional properties (such as emulsification and gelation) than the pure legumin solutions [38]. It was indicated that a low L/V ratio for preparation of protein isolates could be desirable. In the Mertens et al. [35] study on smooth pea seeds, it was reported that agronomic factors, including variety, cultivar type and location, affected the protein content and L/V ratio with high significance. However, some varieties were less sensitive to the prevailing climatic conditions than others. This approach could be beneficial from an industrial point of view as it could manifest in picking stable and less sensitive L/V ratio lines for specific product quality characteristics [35].
Various groups have researched relationships between L/V ratios and their functional attributes. A number of studies noted that pea vicilin showed higher emulsifying properties than corresponding pea legumin [39–41], which was attributed due to higher solubility [42] and surface hydrophobicity [5] of vicilin proteins. Furthermore, Shen and Tang [43] reported that emulsifying properties of vicilins were found to be dependent on both the legume source (Kidney bean, red bean and mung bean) and their protein concentration (0.25–2.5% w/v). The differences in the emulsion properties of vicilins at different concentrations were majorly related to the variation in zeta potential and interfacial characteristics, and were also found to be dependent on other factors such as protein folding, penetration and structural rearrangement at the interface [43]. Bora et al. [44] studied the heat induced gelation of mixed pea globulins and found that 7S globulin had the capacity to undergo heat gelation while 11S globulin did not although used the same optimal conditions of gelation with 15% globulin solutions, pH 7.1 and heating at 87°C for 20 min. However, Nakamura et al. [45] observed that the gels formed by 7S globulins of soybean are less strong and transparent as compared to those formed by 11S globulins, which were much harder and turbid in nature. The study suggested that the extent of interaction in gel formation of a mixed system of 7S and 11S globulins is affected by factors such as the 11S/7S ratio and the composition of their subunits. Cserhalmi et al. [39] reported that mixed globulins and 7S fractions of pea proteins had increased surface hydrophobicity and emulsifying properties compared to the albumins and 11S fractions. Moreover, for all the pea varieties tested, the emulsifying and surface hydrophobicity properties were different from each other. Thus, varying the L/V ratio could be used in obtaining the desired functional attribute in new food formulations.
The quantification of 7S and 11S fractions present in isolates or concentrates is an essential step for calculation of L/V ratio which can be achieved using various methods described in literature. Methods include ammonium sulfate salt extraction [46], isoelectric precipitation [47], sodium dodecyl sulfate-polyacrylamide-gel electrophoresis (SDS-PAGE), gel chromatography [48], selective thermal denaturation [49], sucrose gradient centrifugation [50] and zonal isoelectric precipitation [51, 52]. The effective separation and the choice of technique should be dependent on factors such as nature of sample (isolates, concentrates, seed), extraction technique employed and the level of purification required. For testing of functional and physicochemical properties of 7S and 11S fractions, it is required that enough quantity of these samples is obtained whichever technique is used without compromising the purity.
3. Protein extraction
Protein extraction is dependent on many factors such as pH, temperature, particle size, ionic strength, type of salt used, and solvent to flour ratio [53, 54]. Various extraction methods are being studied so as to maximize the protein yield without compromising the protein functionality of the concentrate or isolate product. The protein extraction processes which are being exploited in the preparation of protein-rich materials (such as isolates and concentrates) can be classified into dry and wet methods [55–57].
3.1. Dry processing
Dry processing of pulses is typically done by air classification, which involves the separation of flours on the basis of particle size and density using an air stream into protein and starch rich fractions [21, 58]. Air classification has been found to be suitable for legume crops low in fat, such as field pea and common bean. Flours are first fractionated into starch (SI) and protein (PI) rich concentrates using an air classification method. SI is then remilled and fractionated to give SII and PII concentrates [55]. Protein separation efficiency (PSE) is defined as the percentage of total flour protein recovered in the PI and PII fractions, and measured as the subtraction of % total flour protein recovered in SII fraction from 100% [55]. For legume crops high in fat such as soybean and chickpea, particle agglomeration is detected which interferes with PSE [59–61]. Dry processing has major advantage over wet extraction methods as the native functionality of proteins is retained and a lower amount of energy and no water is required [62]. Moreover, in contrast to wet extraction methods where both protein concentrates and isolates can be produced, dry processes are suitable only for preparing protein concentrates with protein content from 40–75% [63] probably because of the presence of higher amount of other compounds such as oil and fibers, and protein loss in coarse fractions [64].
Tyler et al. [55] studied the fractionation of eight legumes (cowpea, great northern bean, lima bean, mung bean, navy bean, lentil, faba bean and field pea) using flours produced by pin milling followed by air classification and found faba bean (63.8–75.1%) and lima bean (43.4–49.6%) to have the highest and lowest protein concentrations in the protein-rich fractions. According to the authors, the suitability of pin milling followed by air classification is strongly correlated with the PSE of the legumes. Mung bean, lentil and great northern bean were found to have the highest mean PSE values of 88.9, 87.2 and 87.0%, respectively, whereas lima bean, cowpea and navy bean showed the lowest at 80.2, 78.2 and 80.3%, respectively. The other two legumes, faba bean and field pea, had PSE values of 84.1 and 82.8%, respectively. Overall, the authors indicated that except for lima bean and cowpea, the legumes were found to be suitable for separation of protein and starch fractions by the pin milling and air classification method.
3.2. Wet processing
In general, wet extraction methods can be exploited for preparing both protein concentrates and isolates at levels of 70% and 90% protein (or higher), respectively. However, it should be noted that currently there is no universal classification scheme which separates concentrate from an isolate for all the legumes. The various wet extraction processes include acid/alkaline extraction-isoelectric precipitation, ultrafiltration and salt extraction. Legume flours dispersed in aqueous solutions typically show high solubility when subjected to alkaline or acidic extraction conditions at pH 8–10 and below 4 respectively [63].
3.2.1. Acid/alkaline extraction-isoelectric precipitation (IEP)
Briefly, proteins are first dissolved under alkaline (alkaline extraction) or acidic (acid extraction) conditions, followed by a clarification step and then precipitation by adjusting the pH to the isoelectric point (pI) of the protein [65]. In solutions with the pH < pI, proteins assume a net positive charge, whereas at pHs > pI proteins assume a net negative charge. Under solvent conditions where proteins carry a net positive or negative charge, repulsive forces between proteins repel neighboring molecules, and also promote protein-water interactions for improved dispersion and solubility. Near the pI value, proteins tend to carry a neutral net charge, allowing neighboring proteins to aggregate via attractive van der Waals forces and hydrophobic interactions. Under these conditions, protein-protein interactions are favored over protein-water interactions, and thus protein is precipitated out of the solution.
According to Han and Hamaker [65], alkaline extraction followed by isoelectric precipitation is the most widely used method for obtaining extracts with protein purity greater than 70%. During alkaline extraction, legume proteins become solubilized at high pH values. The solution can then be clarified by centrifugation to remove insoluble material such as insoluble fiber, carbohydrates and insoluble proteins (e.g., prolamins). Protein concentrates or isolates can be formed by reducing the pH of the supernatant to near the pI of the protein using an acid such as HCl [63, 66]. The study of Can Karaca et al. [16] showed that isolates prepared from legumes (faba bean, chickpea, lentil, pea and soybean) by an alkaline extraction/IEP method had higher overall protein content (85.6%) as compared to those prepared by a salt extraction method (78.4%). Moreover, it was reported that both legume source and protein extraction method along with their interaction had significant effects on protein levels of the isolates, and also on physicochemical and emulsifying properties. The overall surface charge, solubility, hydrophobicity and creaming stability for IEP produced isolates was higher as compared to isolates produced by salt extraction [16]. The effect of processing or extraction conditions on the protein content of isolates can also be well observed from the studies of Flink and Christiansen [67] and McCurdy and Knipfel [68]. In the former study, faba bean isolates with protein contents of 80.0–90.0% were obtained when the bean:solvent ratio was 1:5 (w/v) with pH 8 to 10 at 23°C for 10 min, and the precipitation of protein was carried out at pH 3–5. While in the latter study, the protein content of faba bean isolates was 76.4–94.0% using a bean:solvent ratio of 1:5 w/v with pH 7–10, for 30 min, temperatures of 10°C and 20°C, and precipitation at pH 4–5.3.
Acid extraction (in principle similar to alkaline extraction) involves the preliminary extraction of proteins under acidic conditions. This process could result in high solubilization of proteins prior to protein recovery (IEP, Ultrafiltration (UF)), as proteins tend to be more soluble under acidic conditions (pH below 4) [5]. In a study by Vose [69] for preparation of faba bean (Vicia faba equina L. cv. Diana) and pea (Pisum sativum L. cv. Trapper) IEP isolates, the cyclone discharge obtained from pin milling these two legumes was acidified directly using 2 N HCl to a isoelectric point of 4.4–4.6. This process resulted in pea and faba bean protein isolates with 91.9% and 91.2% protein, respectively [5].
3.2.2. Ultrafiltration/diafiltration
In the literature, membrane separation methods were shown to produce protein isolates with higher functionality [70, 71] and were effective in reducing levels of anti-nutritional components which include protease and amylase inhibitors, lectins and polyphenols [72–74]. UF and microfiltration are membrane-based fractionation methods using pressure as the driving force for separation. Microfiltration can be used to separate particles or macromolecules larger than 0.1 μm, whereas ultrafiltration removes similar particles in the range of 0.001–0.02 μm [75]. For preparation of protein materials using ultrafiltration, the supernatant after alkaline or acidic extraction is processed using either UF or diafiltration (DF) together to isolate the protein material. UF is often combined with DF to improve protein recovery, where water is added to the retentate for dilution purposes, followed by re-ultrafiltration.
Vose [69] used the UF procedure to produce faba bean and pea protein isolates which protein levels of 94.1% and 89.5%, respectively. Boye et al. [66] evaluated the protein content of isolates obtained from different pulses (pea, chickpea and lentil) using alkaline extraction-IEP and UF/DF extraction methods. The protein content in concentrates obtained by the UF/DF method was found to be higher than in those obtained by IEP. For instance, for yellow pea, green lentil, red lentil, and desi and kabuli chickpea, UF/DF gave protein levels of 83.9%, 88.6%, 82.7%, 76.5% and 68.5%, respectively. In contrast, for IEP extraction, protein levels were 81.7%, 79.1%, 78.2%, 73.6% and 63.9% respectively for the same legume crops. Moreover, it was reported that UF was different from IEP in terms of protein composition as the isolates prepared by UF comprised both globulins and albumins, whereas the isolates prepared by IEP were observed to contain only globulins [63, 76, 77].
3.2.3. Salt extraction
Salt extraction is a process where globulin proteins are separated from albumins on the basis of solubility [5], as described previously in the Osborne classification scheme [19]. Proteins contain both hydrophobic and hydrophilic amino acids. The majority of hydrophobic moieties are buried inside the quaternary or tertiary structure due to a hydrophobic effect, and the majority of hydrophilic moieties are on the surface, free to participate in protein-water interactions. 'Salting-in' of proteins typically occurs at low salt levels, where the ions act to increase order of the protein's hydration layers and promote protein-water interactions [78–83]. However, at high levels of salt, hydration layers can be disrupted as ion-water interactions become favored over protein-water interactions in a 'salting-out' process [78–83]. As the ions attract water molecules away from the surface of the proteins, protein-protein aggregation is favored due to hydrophobic interactions. Aggregates continue to grow in size and number until they fall out of solution as a precipitate. The ability of ions to 'salt-in' or 'salt-out' proteins depends on both the ionic strength and type of cations and/or anions present, as described according to the Hofmeister series [Anions: SO42− > HPO42−> acetate− > Cl− > NO3−; Cations: N(CH3)4+> NH4+> Na+ = K+ > Li+ > Mg2+] [84].
Salts formed between cations and anions with higher precipitation ability in the series decrease the solubility of non-polar amino acids, favoring hydrophobic interactions to 'salt-out' proteins. On the contrary, salts formed between cations and anions with lower precipitation ability in the series weaken the hydrophobic interactions and result in increasing solubility of non-polar amino acids, thus favoring the 'salting-in' process [85]. Broadly speaking, ammonium sulfate (NH4)2SO4 and sodium chloride (NaCl) are the most commonly used salts for research purposes [16, 86–88]. Typically in the salt extraction procedure, proteins are initially dissolved in an aqueous NaCl solution (0.3–0.5 M) [86, 88] at neutral pH, followed by a clarification procedure to remove insoluble material. Precipitation of the protein can be triggered by either diluting the supernatant with water to lower the ionic strength or by dialysis to remove the salts, resulting in the formation of protein micelles which grow in size and number until precipitation ensues. Alsohaimy et al. [87] prepared protein isolates from chickpea, lupin and lentil using IEP and ammonium sulfate precipitation. For all of these legumes, the latter method resulted in higher protein content (chickpea − 90.6%, lupin − 92.6% and lentil − 93.0%) in comparison to the former method (chickpea − 81.4%, lupin − 87.3% and lentil − 80.0%). On the contrary, Can Karaca et al. [16] produced isolates from chickpea, faba bean, pea and lentil using IEP and a salt extraction method and found that the protein levels obtained using the IEP method (chickpea − 85.4%, faba − 84.1%, pea − 88.8%, and lentil − 81.9%) were found to be higher than the ones produced by the salt extraction method (chickpea − 81.6%, faba − 82.0%, pea − 81.1%, and lentil- − 74.7%) [16].
4. Functional properties of pulse proteins
Protein flours, concentrates and isolates can be incorporated into various foods to increase their nutritional value and/or to provide specific and desirable functional attributes [5]. These functional attributes may include solubility, gelation, emulsifying ability, oil and water absorption capacity, and foaming. Moreover, functional properties of legume proteins contribute an important aspect in determining the competitiveness of the protein ingredient or the product in the market, as they can impact the sensory, physical and chemical properties of a food, which includes texture and organoleptic characteristics. In the literature, the functional attributes of legume proteins vary considerably due to differences in the raw material, processing, extraction methods and environmental conditions used during testing.
4.1. Solubility
Protein solubility plays a major role in various food applications as a number of functional properties such as foaming, gelation or thickening, and emulsification are closely related and often dependent on protein solubility. High protein solubility may be helpful in producing food products such as beverages, infant milk powder, imitation milk and other products which require instant solubility with no residues left. For instance, imitation milk produced using lentil protein isolate was reported to have the same quality as compared to milk prepared from soy protein isolate, however had a lower quality than when pea protein isolate was used [21]. The solubility of protein depends on various attributes including hydrophobic/hydrophilic balance of the protein molecule (mainly the surface composition: polar/non polar amino acids), pI, pH, temperature, ionic strength and the type of ions present in the solution [63]. Proteins exhibit minimum solubility at their pI because of a zero net surface charge, resulting in aggregation of protein molecules into larger structures, followed by precipitation. On the contrary, when the pH values are greater or less than the protein's pI, proteins exert a positive or negative net charge into solution, repelling one another to maximize solubility.
The solubility profiles of concentrates and isolates from various pulses obtained by IEP or UF were found to be lowest between pH 4 and 6, and significantly increased with pH shifting to either more acidic or alkaline conditions [63]. Boye et al. [66] reported that the solubility of pea, chickpea and lentil protein concentrates, which were processed using IEP and UF/DF techniques, were highest at pHs 1–3 and pHs 7–10. Moreover, the solubility profile varied with different varieties where, UF-yellow pea and UF-red lentil concentrates had the highest solubility at neutral pH, while at pH 3 and 8–10 solubility was highest for only UF-red lentil. In both cases, the lowest solubility was found for UF-chickpea (desi). The study by Can Karaca et al. [16] on five different legumes (pea, chickpea, faba bean, lentil and soybean) showed higher overall solubility (determined at neutral pH) of these legume isolates prepared by the IEP method (85.9%) as compared to ones prepared by a salt extraction method (61.5%). For the IEP method, the pea protein isolate had the lowest solubility (61.4%); soybean isolates had the highest solubility (96.5%); and pea, lentil and chickpea isolates exhibited intermediate solubility (>90.0%). However, highly variable results were obtained for the solubility of salt-extracted isolates with values of 30.1% and 96.6% for chickpea and soybean respectively, while intermediate solubility was observed for lentil (89.8%), pea (38.1%), and faba bean (52.5%). Solubility profile of isolates produced from kabuli (PBG-1, PDG-4, PDG-3, GL769 and GPF-2) and desi chickpea cultivars (L550) were found to be non-significant as a function of genotype (p>0.05) [89]. However, in the study of Barac et al. [38], the solubility profile of six pea genotypes (Maja, Calvedon, Miracle, L1, L2 and L3) were found to be significantly different from each other except L2 and Maja (p<0.05).
4.2. Oil holding and water hydration capacities (OHC, WHC)
OHC and WHC refer to the extent to which oil and water, respectively, can be bound per gram of the protein material or legume flour [5, 63]. These properties are essential with respect to maintaining the quality of a product, its shelf life and consumer acceptability (texture and mouth feel). The ability of a protein to bind oil and water is important in preventing cook loss or leakage from the product during processing or storage [63]. Failure of a protein to bind water could lead to brittle and dry characteristics of the product [5]. WHC values for pulse protein concentrates, such as pea, faba bean, lentil and chickpea, have been determined by various groups [66, 89, 90] and fall in the range of 0.6–4.9 g/g, suggesting that both pulse genotype and manner of processing could impact values. For instance, Kaur and Singh [89] found that protein isolates prepared by kabuli chickpea cultivars (PBG-1, PDG-4, PDG-3, GL769 and GPF-2) produced significantly lower WHC than desi chickpea (L550) (p<0.05) which clearly indicates the impact of different cultivars in assessing functionality. Boye et al. [66] reported that for all the legumes studied (red and green lentil, desi and kabuli chickpea, yellow pea), IEP protein concentrates had higher WHCs than did ones prepared by UF (with the exception of red lentil protein concentrates) although no substantial differences were observed between WHC values between the processing treatments. The yellow pea concentrate (IEP) had the highest WHC value which was much higher than those of the kabuli and desi chickpea concentrates (IEP and UF) indicating the more significant effect of pulse type compared to extraction method on WHC.
OHC values reported by various authors [86, 89, 90] for different pulses range from 1.0–3.96 g/g, and seem to depend again on the type and variety of pulse used, and the method of preparation of the protein product. Boye et al. [66] studied the UF and IEP concentrates produced from red and green lentil, yellow pea and kabuli and desi chickpea. They reported that pulse variety and processing conditions had a larger impact on the OHC of yellow pea, kabuli chickpea and red lentil concentrates as compared to those made from desi chickpea and green lentil. Moreover, UF concentrates made from yellow pea, red lentil and kabuli chickpea had significantly higher OHC than their corresponding IEP concentrates. Red lentil and yellow pea concentrates produced by UF had the highest OHC of 2.26 g/g and 1.17 g/g respectively. However, no significant differences in OHC were observed between the IEP produced concentrates (p>0.05) [66]. In the study of Kaur and Singh [89], chickpea protein isolates were reported to have higher OHC than the corresponding flour samples. Moreover, in contrast to WHC, the OHC of kabuli chickpea was reported to be significantly higher than desi cultivars (p<0.05).
The water and oil holding properties of legume proteins may be essential in formulation of food products such as meat, pasta, cookies, etc. In producing low fat meat products, water is added to substitute the fat loss. And, water holding compounds are added to prevent cooking losses and meat shrinkage which includes proteins (whey, soy and collagen), lipids (soy lecithin) and carbohydrates (flours, starches and gums) [91]. For instance, soy proteins added to ground beef improves the tenderness, moisture retention, decreases cooking losses, and inhibits rancidity [92]. Deliza et al. [93] replaced meat in ground beef mixture with hydrated textured soybean protein (15 or 30%) and found that beef patties were more tender as compared to controls, although the overall flavor quality was reduced with having less beefy flavor. However, legumes (navy beans, chickpeas, mung beans and, red kidney beans) when substituted at a level of 15% in beef mince resulted in acceptable products, with chickpea preferred over other legumes [94].
4.3. Emulsification
An emulsion is a mixture of two or more immiscible liquids (usually oil and water), where one of the liquids (the dispersed phase) is mixed in to the other (the continuous phase) in the form of small spherical droplets [95]. Emulsions are generally classified into two types: oil-in-water (O/W), in which oil droplets are dispersed within an aqueous phase (e.g., milk, mayonnaise, cream and soups); or water-in-oil (W/O), in which water droplets are dispersed within an oil phase (e.g., butter and margarine). Emulsions are thermodynamically unstable and with time separate into oil and liquid layers due to collision and coalescence of droplets [95]. Stabilizers such as emulsifiers can be used to produce stable emulsions. For instance, protein as an emulsifier acts by adsorbing onto the oil-water interface to form a viscoelastic film surrounding the oil droplets. Stability is enhanced through electrostatic charge repulsion (depending on the pH), steric hindrance or increases to the continuous phase viscosity [95].
Protein emulsifiers are used worldwide because of their ability to adsorb at the droplet surface in an O/W emulsion during the process of homogenization, thereby reducing interfacial tension. The adsorbed protein molecules present at the surface act as a separating membrane preventing coalescence with the neighboring droplets [63]. To be an effective emulsifier, protein must exhibit the following properties: fast adsorption at the oil-water interface, ability to form a protective and cohesive layer around the oil droplets, and ability to unfold at the interface [96]. Various studies reported that the emulsifying ability of legume protein concentrates or isolates are dependent on the type of legume or the method (IEP/UF/salt extraction) used in their preparation. For instance, Fuhrmeister and Meuser [71] reported that a pea protein isolate prepared by an IEP method was found to have lower emulsifying ability as compared to one prepared using UF.
Emulsion activity index (EAI) refers to the area of emulsion stabilized per gram of emulsifier or protein material and expressed as m2/g whereas emulsion stability index (ESI) refers to the measure of stability of this emulsion as a function of the time. Emulsion capacity (EC) is the amount of oil homogenized per gram of protein material and expressed as g oil/g protein whereas creaming stability (CS) is the ability of an emulsion to resist creaming and the formation of a serum layer as time passes, and measured as %. The study conducted by Can Karaca et al. [16] on different legumes (pea, chickpea, faba bean, soybean and lentil) showed that both legume source and extraction method (IEP or UF) had significant effects on emulsifying and physicochemical properties. Both EAI and ESI were significantly affected by legume source and extraction method, whereas EC was dependent on the legume source only. However, Boye et al. [66], studying the functional properties of chickpea, lentil and pea protein concentrates, concluded that IEP and UF preparation methods had little impact on emulsifying properties. Barac et al. [38] studying functional properties of six pea genotypes reported significant differences in emulsifying properties (EAI and ESI) as a function of Genotype and pH. The EAI of pea genotypes tested in this study was significantly higher than the commercial pea protein isolates tested.
Emulsifying and other functional properties of proteins can also be improved with protein modifications such as limited enzymatic hydrolysis using proteases (e.g. trypsin). The hydrolysis reaction results in partial unraveling of protein molecules thus exposing more ionic and hydrophobic groups for interaction with oil droplets [97]. For instance, trypsin treated oat bran protein with a ∼4–8% degree of hydrolysis (DH) had improved solubility, water holding, foaming and emulsifying properties as compared to those of native proteins [98]. On the contrary, Avramenko et al. [99] reported detrimental effects of trypsin mediated hydrolysis (DH∼4–20%) of lentil protein isolates. Here, except zeta potential, all the physicochemical properties (surface hydrophobicity and interfacial tension) and emulsifying properties (emulsion activity and stability indices) were found to have lower values as compared to the unhydrolyzed lentil protein isolate. This suggests that processing conditions might have specific effects dependent on protein source.
Legume proteins play a vital role in the formulation of a number of novel foods (such as sausages, bologna, meat analogues, cakes and soups) by formation and stabilization of emulsions. Meat analogues are foods which are made from nonmeat ingredients, structurally similar to meat and may have the same texture, flavor, appearance, and chemical characteristics [100]. Some of the traditional foods such as wheat gluten, rice, mushrooms, tofu and legumes when added with flavors mimic the finished a meat products such as chicken, beef, sausage etc. [100]. Soybean protein is an important meat analogue since it has meat like texture and provides a similar amino acid profile to meat proteins [100]. Tofu is a widely consumed meat analogue made from soy, which provides a good source of protein, calcium and, iron. In general, the market for meat analogues is large and includes vegetarians, vegans, and people who do not eat meat products because of religious or cultural practices.
4.4. Foaming
Similar to emulsions, foams also have two immiscible phases (aqueous and gas), and require an energy input to facilitate their formation. Foams are comprised of a dispersed gas phase within a continuous aqueous phase [96]. Proteins in solution adsorb to the gas-liquid interface in a similar manner as in emulsions to form a viscoelastic film surrounding the gas bubbles that helps resist rupturing and bubble fusion [63]. In contrast to emulsions, the major driving mechanism associated with foam instability is associated with Oswald ripening, which involves the diffusion of small gas bubbles through the continuous phase in order to become absorbed into a larger gas bubble [96]. Rupture of the viscoelastic film leads to drainage of the continuous liquid phase through the film matrix. Various food products are available which use protein as a stabilizer including meringues, whipped desserts, mousses and leavened bakery products [101]. Vose [69] reported that the foaming properties of faba bean and yellow pea isolates, prepared using UF, were higher than that of skim milk powder, wheat flour and soy protein isolates. A faba bean isolate was observed to have better foaming properties than pea protein isolate.
Foaming capacity (FC) refers to the volume of foam generated after homogenization of a certain amount of protein solution whereas foam stability (FS) refers to the ability to retain foam structure and resistance in the formation of serum layer as a function of time. In the study of Sathe and Salunkhe [102] on great northern bean (Phaseolus vulgaris L.) protein materials, the FCs were in the following decreasing order: albumins (180%) > protein concentrate (164%) > globulins (140%) ∼ egg albumin (140%) > flour (132%) > isolate (106%), where egg albumin was the standard for measuring foaming capacity. These results indicated that all great northern bean protein materials except the isolate, had FCs that were comparable to or higher than that of egg albumin. However, the foaming stabilities were as good as egg albumin, and hence the overall foaming ability was given only a fair mark [5, 102]. Boye et al. [66] studied and compared the functional properties of yellow pea, green and red lentil, and kabuli and desi chickpea protein concentrates prepared using IEP and UF techniques. In their studies, they found that foaming capacity (which ranged from 98% to 106%) was similar for pea and lentil protein concentrates irrespective of extraction method used. However, the desi and kabuli chickpea concentrates prepared by the IEP method showed higher foaming capacity than the others. In general, it was observed that chickpea showed higher foaming capacity and expansion but lower foam stability as compared to the other sources. Furthermore, variability was observed in foaming stability with kabuli and desi chickpea and green lentil concentrates prepared by the IEP method having higher foam stability values compared to concentrates prepared by the UF method. Barac et al. [38], studying the functional properties of isolates produced from six pea genotypes using the IEP method, reported significant differences in their foaming properties as a function of genotype and regardless of changes in pH. Generally, a low foam stability was observed probably because of the low concentration of protein used in the formation of the protein solution. However, foaming capacity was highest for Maja cultivar, which was significantly higher than the commercial pea protein isolate.
Nowadays, there has been a growing interest by the food industry towards utilizing pulse proteins in novel products due to their nutritional value, availability, low cost, desired functional properties and beneficial health effects [3]. Pulse protein concentrates and isolates are being applied in many food products such as beverages, imitation milk, baby foods, bakery products, meat analogs, cereals, snack foods, bars, and nutrition supplements. Examples of some of the food applications of pulse proteins from literature offering opportunities for novel product development are presented in Table 1. Pulse proteins are also used in non-food applications such as microencapsulation of bioactive ingredients. Pulse proteins can serve as good encapsulating agents due to their amphiphilic nature, ability to stabilize oil-in-water emulsions and film forming abilities. Some of the current examples of pulse protein-based microcapsules include: alpha-tocopherol [103], polyunsaturated fatty acids-rich oil [104] and conjugated linoleic acid [105] encapsulated with pea protein, flaxseed oil encapsulated with chickpea or lentil protein [106], Bifidobacterium adolescentis [107] and folate [108] encapsulated with chickpea protein.
Pulse protein
Protein Conc'n (%)
Chickpea Pasta 5–15 Quality characteristics of the cooked pasta were not affected by increasing protein content. [109]
Chickpea, faba
bean, lentil, mung
bean, smooth pea, pea, and winged bean Bean curd 2.3–3 Chickpea and faba beans had comparable textural properties to soybean. [110]
Lentil and
white bean Cake 3 Lentil and white bean protein extracts tested were found to be suitable to replace soy and pea in bakery products. [111]
Pea protein Gluten-free
bread 1–6 Pea protein addition improved rheological and structural properties of the dough. [112]
Lupin Bread 5–10 Lupin protein addition increased the dough development time, stability and the resistance to deformation and the extensibility of the dough. [113]
Lupin Fermented sausage 2 Products containing lupin protein showed no difference in firmness, appearance and color compared to control. [114]
Pea and sweet lupin (cross-linked) Sausage-like vegetarian substitute 9 Sensory profile and textural properties were overall accepted. [115]
Some examples of food applications of pulse proteins.
6. Challenges for pulse protein ingredients
Application of pulse protein ingredients in food products is limited due to the formation of a green or beany off-flavor during storage [116]. The most potent odor-active volatiles have been identified in soy protein. One of the key off-flavors in soy protein is reported to be n-hexanal, which is a degradation product of linoleic acid. Fermentation with Lactobacillus or Streptococci strains was suggested to overcome this hurdle [117]. In the case of pulse proteins, Murat et al. [118] showed that the flavor profile is evolving during the extraction process from pea flour to pea protein extract. The odor active compounds were found to be different between pea flour and pea protein powder. Schindler et al. [116] identified 23 highly odor-active compounds in pea protein extracts including n-hexanal, 1-pyrroline, dimethyl trisulfide, 1-octen-3-one, 2,5-dimethyl pyrazine, 3-octen-2-one, β-damascenone, and guaiacol. The authors suggested that lactic acid fermentation improved the aroma of pea protein extracts by decreasing the n-hexanal content and reducing or masking off-flavors.
Financial support for this work was provided by the Saskatchewan Ministry of Agriculture, the Western Grains Research Foundation, and the Saskatchewan Pulse Growers.
2.Protein structure and legumin/vicilin (L/V) ratio
3.Protein extraction
4.Functional properties of pulse proteins
5.Applications
6.Challenges for pulse protein ingredients
Ashish Singhal, Asli Can Karaca, Robert Tyler and Michael Nickerson (October 19th 2016). Pulse Proteins: From Processing to Structure-Function Relationships, Grain Legumes, Aakash Kumar Goyal, IntechOpen, DOI: 10.5772/64020. Available from:
Edited by Aakash Goyal
Genetic Control of Cadmium Concentration in Soybean Seeds
By Souframanien Jegadeesan, Richard Ying Yu and Kangfu Yu
Crop PlantEdited by Aakash Goyal
Crop Plant
Progression of DNA Marker and the Next Generation of Crop Development
By Herry S. Utomo, Ida Wenefrida and Steve D. Linscombe


Hello Kitty is dressed for the USA in six fresh, new Jerry Leigh-original collections! Choose from Tropical Beach, Nautical, Desert Cowboy, Southern, Florida and Texas in Junior, Youth and Toddler. These styles are exclusive to Jerry Leigh and not available anywhere else!


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static int keyCounter=0;

@implementation TestSqlite3{
    LEConfigurableList *list;
}
-(void) leAdditionalInits{
    [[LEUICommon sharedInstance] leSetViewBGColor:LEColorBG9];
    LEView *view=[LEView new].leSuperViewcontroller(self);
    [LENavigation new].leSuperView(view).leTitle(@"测试TestSqlite3");
    view.leSubViewContainer.leBgColor(LEColorText9);
    list=[LEConfigurableListWithRefresh new].leSuperView(view.leSubViewContainer).leDelegate(self).leDataSource(self);
    list.backgroundColor=[LEUICommon sharedInstance].leViewBGColor;
    //
    NSMutableArray *curData=[NSMutableArray new];
    [curData addObject:@{LEConfigurableCellKey_Type:[NSNumber numberWithInt:L_Title_R_Arrow],
                         LEConfigurableCellKey_Title:@"leReloadWithNewPath",
                         LEConfigurableCellKey_Function:@"leReloadWithNewPath"}];
    [curData addObject:@{LEConfigurableCellKey_Type:[NSNumber numberWithInt:L_Title_R_Arrow],
                         LEConfigurableCellKey_Title:@"leCreateTable",
                         LEConfigurableCellKey_Function:@"leCreateTable"}];
    [curData addObject:@{LEConfigurableCellKey_Type:[NSNumber numberWithInt:L_Title_R_Arrow],
                         LEConfigurableCellKey_Title:@"leInsertRecordToTable",
                         LEConfigurableCellKey_Function:@"leInsertRecordToTable"}];
    [curData addObject:@{LEConfigurableCellKey_Type:[NSNumber numberWithInt:L_Title_R_Arrow],
                         LEConfigurableCellKey_Title:@"leSelectRecordsFromTable",
                         LEConfigurableCellKey_Function:@"leSelectRecordsFromTable"}];
    [curData addObject:@{LEConfigurableCellKey_Type:[NSNumber numberWithInt:L_Title_R_Arrow],
                         LEConfigurableCellKey_Title:@"leBatchImportToTable",
                         LEConfigurableCellKey_Function:@"leBatchImportToTable"}];
    [curData addObject:@{LEConfigurableCellKey_Type:[NSNumber numberWithInt:L_Title_R_Arrow],
                         LEConfigurableCellKey_Title:@"leClearTable",
                         LEConfigurableCellKey_Function:@"leClearTable"}];
    [curData addObject:@{LEConfigurableCellKey_Type:[NSNumber numberWithInt:L_Title_R_Arrow],
                         LEConfigurableCellKey_Title:@"leRemoveTable",
                         LEConfigurableCellKey_Function:@"leRemoveTable"}];

    [list leOnRefreshedWithData:curData];
//    [LEDataManager sharedInstance];
}
//
-(void) leReloadWithNewPath{
    NSString *docsPath = NSSearchPathForDirectoriesInDomains(NSDocumentDirectory, NSUserDomainMask, YES)[0];
    NSString *dbPath   = [docsPath stringByAppendingPathComponent:[NSString stringWithFormat:@"%zd.db",LEIntToString(rand()%100)]];
    [LEHUD leShowHud:dbPath];
    LELogObject(dbPath)
    [[LEDataManager sharedInstance] leReloadWithNewPath:dbPath];
}
-(void) leCreateTable{
    [[LEDataManager sharedInstance] leCreateTable:TableName];
}
-(void) leInsertRecordToTable{
    NSString *value=LEIntToString(rand()%1000);
    LELogObject(value)
    [LEHUD leShowHud:value];
    [[LEDataManager sharedInstance] leInsertRecordToTable:TableName WithKey:LEIntToString(keyCounter++) Value:value];
}
-(void) leSelectRecordsFromTable{
    NSArray *result=[[LEDataManager sharedInstance] leSelectRecordsFromTable:TableName];
    LELogObject(result)
    [LEHUD leShowHud:[NSString stringWithFormat:@"%@", result]];
}
-(void) leBatchImportToTable{
    [[LEDataManager sharedInstance] leClearTable:TableName];
    NSMutableArray *muta=[NSMutableArray new];
    for (NSInteger i=0,j=1+rand()%5; i<j; i++) {
        [muta addObject:[NSString stringWithFormat:@"insert into %@ (key,value) values ('%@', '%@')",TableName,LEIntToString(keyCounter++),LEIntegerToString(i)]];
    }
    LELogObject(muta)
    [[LEDataManager sharedInstance] leBatchImportToTable:TableName WithData:muta];
}
-(void) leClearTable{
    [[LEDataManager sharedInstance] leClearTable:TableName];
}
-(void) leRemoveTable{
    [[LEDataManager sharedInstance] leRemoveTable:TableName];
}
-(void) leOnCellEventWithInfo:(NSDictionary *)info{
}
//
@end

redpajama_set_name: RedPajamaGithub


Moe's Crosstown Tavern is hosting a benefit for Allan Park as local residents and members of the Hampton Park Terrace Neighborhood Association work with the Charleston Parks Conservancy to raise money to renovate the park.
A gift certificate to Ted's Butcherblock, and more.
Moe's also will host Allan Park Night at 5 p.m. May 23rd with a special plated dinner and craft beer from Sweetwater Brewing Co. Proceeds from the food sales will be donated to Allan Park. The winners of the prize drawing will be announced at 9 p.m.


Minecraft: Pi Edition, a free version of Mojang's block-based world builder created for the diminutive Raspberry Pi computer, is available for download today, according to a post on Mojang's website.
Already downloaded and installed.. Runs pretty nicely on the Pi..


text:
Home | Israel News
Israeli Soldier Who Was Attacked During West Bank Raid Dies of Injuries
Ronen Lubarsky, 20, sustained critical head injuries when a heavy stone slab was dropped on him from a building ■ Netanyahu vows to 'catch the terrorist, bring him to justice'
Yaniv Kubovich
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Clashes between Palestinians and Israeli security forces in the al-Am'ari refugee camp, West Bank, May 21, 2018.Credit: Screenshot / Israel Television News Company
An Israeli soldier from the elite unit Duvdevan died on Saturday from critical injuries he sustained during a military raid on a West Bank refugee camp near Ramallah, the Israel Defense Forces' Spokesperson's Office said.
Ronen Lubarsky, 21, died of his wounds, May 26, 2018.Credit: Screenshot from Lubarsky's Facebook page.
Ronen Lubarsky, 20, from the central Israeli city of Rehovot, was critically injured when a heavy stone slab was thrown from the third floor of a building during arrests at the al-Am'ari refugee camp. The army unit was unable to pursue the attacker as they could not identify who had thrown the slab.
Lubarsky was evacuated to Hadassah University Hospital in Ein Karem in Jerusalem, where he was sedated and hooked up to a respirator. Though he was wearing full protective gear at the time of the incident, the impact of the slab shattered his helmet and caused a severe blow to his head.
PTSD plagues the Israeli special forces that inspired Fauda
Israeli soldier critically injured during raid on Palestinian refugee camp
Two years on the job, Israel's defense minister lacks knowledge, training and influence
Prime Minister Benjamin Netanyahu expressed sorrow over the news of Lubarsky's death. "I send heartfelt condolences to his family," Netanyahu said Saturday evening. "The security forces will catch the terrorist and the State of Israel will bring him to justice."
The military said the raid targeted members of a cell involved in recent shooting attacks against Israelis. Three Palestinian suspects were taken to the Shin Bet security service for questioning.
The first set of Israeli forces that arrived at the site for the raid was undercover and surrounded the building where the wanted men were located. A larger force of the Duvdevan unit equipped with full protective gear arrived afterwards, including Lubarsky.
Lubarsky's death brings the amount of fallen Duvdevan soldiers to 18 since the unit was established in 1986. Most of the fallen soldiers were killed in training accidents or as a result of friendly fire during an operation – none of them were killed by enemy fire.
"We will learn and draw lessons from this event," the IDF spokesperson, Ronen Manlis, said after the incident. "During the Ramadan period there has been an increase in the number of attacks, and attempts to carry them out. This falls within the framework of the operation in the refugee camp," he concluded.
Israel Weighs Nixing COVID Isolation for Schoolchildren
Where the Streets Have No Arabic Names, a Group of Women Remind Us of History Where the Streets Have No Arabic Names, a Group of Women Remind Us of Palestinian History

redpajama_set_name: RedPajamaCommonCrawl


text:
When Bob Dylan Refused to Let Aggressive Hecklers Ruin His Show
Bob Dylan's pianist Alan Pasqua recalled a moment when hecklers tried to ruin a show, but Dylan refused to let the rest of his audience down. The incident took place around 1978 on the tour ...
Ultimate Classic Rock2d
Bob Dylan almost died in 1997. Months later, 'Time Out of Mind' revived his career
A quarter of a century ago, Bob Dylan found vital new life in an album about death's inexorable approach. "I'm walking through streets that are dead," the rock 'n' roll legend sang ...
Los Angeles Times4d
Inside The Making of Bob Dylan's Luminous Late-'90s Masterpiece
Mark Seliger"Creative ability is about pulling old elements together and making something new," Bob Dylan told me last month.
From Odessa to Duluth: The journey of Bob Dylan's grandparents
DULUTH — "My grandmother's voice possessed a haunting accent, face always set in a half-despairing expression," Bob Dylan wrote in his 2004 memoir. "Life for her hadn't been easy. She'd come to ...
Duluth News Tribune5d
A Beginner's Guide to Bob Dylan's Sprawling, 17-Volume Bootleg Series
The Bootleg Series Volumes 1–3 (Rare & Unreleased) 1961–1991. The project was Dylanology physically incarnated, featuring 58 rare and unreleased demos, live recordings, and session outtakes from Dylan ...
David Crosby died today at the age of 81, but the singer-songwriter's humor, charm, insights and obstreperousness were on full display in David Crosby: Remember My Name, the 2019 bio-doc which was ...
Bob Dylan loves a bit of Eminem and Wu-Tang Clan and we bet you didn't see that coming
In the bingo card combination we bet you weren't expecting this year, Bob Dylan has shared his admiration ... He signed the letter with his 'deepest regrets'. Got a story?
Review: 'Modern Song' selected and explained by Bob Dylan
Bob Dylan's wacky joyride of a book — titled "The Philosophy of Modern Song" — is more riff than philosophy. Anecdotal, ...
Songs of a weary heart: A box set revisits Bob Dylan's luminous 'Time Out of Mind'
Bob Dylan's career has been nothing if not a ... the hard truths of age and regret — and scrutinized them with a poetic yet unsparing edge. The album's emotional center, "Not Dark Yet, ...
The Boston Globe5d
New Bootleg Series Installment Maps The Long Road To Dylan's Resurrection
Most editions of Bob Dylan's three-decades-and-running Bootleg Series focus on a particular phase of his career, but a few have zoomed in on the making of an especially hallowed record.
Rolling Stone6d
Daisy Jones & the Six announce debut album with first single "Regret Me" and share teaser for Amazon series of the same name
Atlantic Records has announced Aurora, the debut album from a fictional '70s band called Daisy Jones & the Six, and the ...
thelineofbestfit.com6d


I think the lyrics from All Sons and Daughter's Higher struck a cord in me because it was me! For a long time I let fear dictate my life. I listened to fear's speech filled with the "what if's" of rejection, failure, and the obscure and dreaded unknown. I agreed with fear's overly cautious advice until I realized what fear promised never actually happened! In fact it was fear that often hedged me into my little comfortable radius keeping me from the life God called abundant.
The first step to freedom and abundant life happened about two years ago when I gave my life over to Christ. Although God did a major work in my life with fear, I had to daily choose to live differently and live in the reality that I no longer had to fear.
One day while I was having some quiet time, Jesus gave me gentle and loving promise and proposition through Isaiah 41:13 saying, "I, the Lord your God, will hold you by your right hand saying to you, 'fear not, I will help you." He would lovingly take me by the hand and help me through my fears. However, the promise was predicated on one thing – was I willing to take His hand? Was I willing to do deeper with Him?
Jesus asks us all this question.
Are we willing to take God's hand? Are we willing to change? To leave behind what we know? What we think is right or good? To leave our old lifestyle patterns and habits? To go outside our comfort zone? To trust God and not ourselves? To completely let fear go?
Jesus will never force us. His proposition is gentle and full of grace and compassion. It comes from a heart that wants relationship with us and to grow in intimacy with us. He is calling us higher. Calling us deeper.
That day, I answered. At first it was hard and uncomfortable. It was different. It was change. It was hard. It was scary. But I was assured I didn't have to fear anymore and I had God to help me through it. Step by step old habits, unbelief, insecurity, and fear began to dissipate. God was patient with my struggles. Gracious when I fell and dusted me off to take His hand and continue with Him.
As I started living the abundant life Jesus intended me to have, I grew closer to Jesus. I discovered more of who He was and enjoyed dialoguing with Him about life. I discovered a relationship with Him.
Out of my anxieties, I learned that Jesus never called us to live the mediocre life, He called us to something greater, something "higher" and "deeper." In fact Jesus said, "I have come that they might have life and that more abundantly," (John 10:10).
uncovered the beauty of the various shades of God's nature and character.
That's the abundant life -- the higher, deeper call God is giving us.
Isn't it time to stop settling for less?


What about the maximum supply of portable toilet manufacturers by WELLCAMP per month?
WELLCAMP has our own factory, which is equipped with advanced machine and state-of-art technology, to supply enough monthly production amount of portable toilet manufacturers. In our factory, we introduced a complete set of production machines and advanced technology to perform the bulk production. During the peak season, there would be mountains of orders which the company can deal with efficiently in order.
WELLCAMP, WELLCAMP prefab house, WELLCAMP container house takes dominant position in market. The series has many styles to meet the diversified needs of customers. Our offer of Wellcamp folding container is very popular in Saudi Arabia, Qatar Oman and other Middle East countries for various applications. . To satisfy different product function requirements, are available. Durability is a feature of WELLCAMP prefab house. . Thanks to the efforts of our experienced team, , we manufacture is of .
Constant excellence and constant quality assurance are of great importance to WELLCAMP, WELLCAMP prefab house, WELLCAMP container house. Inquiry!


Google and Huawei are working on a fix, but in the mean time there's a work around that might work. Go to Settings > Applications > Google Play Services and choose remove the updates. Reboot your smart phone and reinstall the Google Play Services from the Play store.
We've noticed an issue with our Snowfox application run on some of the Huawei's Android devices. Due to this problem, the application won't start. Recent updates to Google's map service is affecting not only Snowfox application, but many other applications which use Google maps. It seems that only Huawei devices are affected.


At BaneCare, we are driven to create an environment built on compassion, dignity, and respect — for our residents and their extended families, for our community, and for our fellow staff members.
We strive to achieve the highest possible quality of life for each resident by providing quality skilled nursing and post-acute rehabilitative care, delivered with sensitivity, deep respect, and genuine hospitality.
We are focused every day on caring for our residents just as we would want to be cared for ourselves. When families are no longer able to care for their loved ones, we will be there for them, understanding how difficult it is to make the decision to utilize a skilled nursing facility.


text:
28 Oct 2022 Author
Adult Primary Training
Abe Impact Report
NurseJournal.orgis a comprehensive on-line resource for present and future nursing college students, in addition to current graduates looking for licensure and full-time employment. Close More than eleven million doses of COVID vaccine have been administered in PA. In How to Build for the Future, you may find out about setting targets, planning for the quick and long term, utilizing cash and credit, and tips on how to help shield your cash. In Managing Your Money, you may find out about bank account options, the way to create a price range, and the way to manage money circulate and financial savings. The ABE program is a part of the School of Adult & General Education at CNM.
Visual Fundamental
Students excited about the program should attend a digital orientation via Zoom. Once orientation is full, you'll be despatched a link to use for admissions and a link to fill out the required documents. HSE Programprovides lessons and tutoring to college students getting ready to take theGED or HiSET exams.
Education provides youngsters a ladder out of poverty and a path to a promising future. But, within the Democratic Republic of Congo almost 7 million kids aged 5 to 17 are out of faculty. The Universal Basic Education, UBE, got here as a alternative of the Universal Primary Education and supposed to boost the success of the primary nine years of education The UBE involves 6 years of Primary School.
Throughout, help has been delivered even during times of conflict and disaster. We are increasing our reach and adapting our programmes quickly to assist children caught up in the nation's rapidly evolving humanitarian challenges. UNICEF delivers help nationwide however with particular concentrate on Chin, Kachin, Kayah, Kayin, Mon, Rakhine and Shan States and Yangon Region, where the challenges are most acute. Even earlier than the COVID-19 and the current disaster started after February 2021, kids in Myanmar already confronted huge barriers to studying. When her college was closed due to the coronavirus, Nelvy continued to review due to the radio and elevated her motivation to learn.
Well Family


How Can Proper Nutrition Help Prevent Pet Intolerance?
Pet Intolerance is a type of allergy caused due to an exposure to pet hair, dander etc, and a person who is susceptible to such a condition starts exhibiting symptoms soon after being exposed to such pet allergens or upon direct contact with pets. Just like testing and medications, proper nutrition is important for avoiding or managing this problem as much as possible. It is a truth that foods are not a real cure. Vegetables and fruits are perfect for the entire body as these are filled with nutrients. There are other foods, which can be part of a good diet and can ensure good health and save the body from pet allergies.
Omega-3 fatty acids are able to reduce inflammation, which is a common symptom arising after pet exposure. These fatty acids are present in seafood such as mackerel, salmon, tuna and more. Each week, you should opt for 2 – 3 servings of fish. A Japanese study proved that women who consumed more fish suffer from less hay fever also referred to as allergic rhinitis, a common symptom of pet intolerance.
There is a mixed result from research about local honey and its effectiveness in curing allergies. Taking a small amount of honey early on can help you to develop tolerance to pet dander, birch pollen and other minute particles. Studies have revealed that people who consume honey regularly develop better immunity, which helps their body to fight off diseases better.
This is a yogurt drink which is rich in probiotics – a type of bacteria that is beneficial and generally lives within the gut. Studies show that increasing the level of probiotics can help the body to prevent pet intolerance allergies and get alleviated from the same. Probiotics are present in fermented foods. These can be found in rich amounts in Kimchi and Sauerkraut. You should choose packaged yogurts with the label reading "live active cultures".
Make sure you deal with your pet intolerance by keeping all hair off the furniture and off your bed. Wash your pet regularly if you have a pet intolerance, and if you suspect it may be an allergy to pets that is causing your symptoms, please do consult a doctor.
To order your intolerance test today, click here.


Due to health care privacy laws (HIPPA), Middlebury College deans and Residential Life staff normally will not have up-to-date information about current health situations or treatment recommendations. If you want them to know, you must tell them.
What should I do when taken to the hospital?
Inform your family of your condition as soon as possible if you have not already done so. The hospital staff can help you.
If you need additional support, contact your Commons Office or the Department of Public Safety.
What should I do when returning to campus from the hospital?
Carefully follow the discharge instructions given to you by the hospital staff.
Call Parton or the hospital if you need help understanding the instructions.
What are my resources for self-care?
Enlist the help of your friends or residence staff if you need support taking care of yourself, such as getting food, drinks or necessary medications.
Immediately contact Parton if your condition worsens (or return to the Emergency Room if Parton is closed).
Unable to reach your Commons Office or the Health Center?


In e4 (like in the other projects under the Eclipse top-level project), we produce regular builds. One important kind of build is called integration build - usually run once a week to produce a version that is good enough to for purposes of integrating with other teams' work, and for self-hosting. Integration builds simply take what's in master, tag it, and generate a report of changes since the last build.
Our current stable build, e4 0.15, has all of our plugins marked as (Incubation) and new plugins should have a version 0.15.0.qualifier.
Checking in code: The checkin comment should at a minimum include "bug #", and preferably be of the form "bug # summary"
Tool: we don't need to use the releng tool to submit for builds, that happens automatically.
We run our builds on build.eclipse.org (an x86_64 linux machine) with a local userid, e4Build.
The main build project is in e4/releng/org.eclipse.e4.builder. It contains the masterBuild.sh script that can be modified to run a test build or a real build (tagged and uploaded to download.eclipse.org). Our build is now controlled by maven/tycho and the pom.xml.
It also contains the old PDE build directory, e4/releng/org.eclipse.e4.builder/builder/general, that used to build our master feature.
We have a set of variables that are needed in order to make the system go.
The base directory that contains all build related files except the JREs.
The branch to check out the releng project (this contains subprojects that contain all our repository to branch mapping). Default is master.
Build architecture, currently x86 or ppc.
The ID of the eclipse build we use as a target platform. With the changes to use a zipped repo for the eclipse SDK, this ID is only used to generate URLs on the download page. It should potentially be used to collect the correct p2 repo for the eclipse/equinox SDK.
The java that is used to launch JVMs from the masterBuild.sh script.


Getting Started in Currency Trading, Fourth Edition is both an introduction and a reference manual for beginning and intermediate traders. Starting with a description of the Foreign Exchange (FOREX) market and a brief history, the book includes an invaluable section made up of relevant FOREX terms clearly defined using examples. The FOREX market has grown substantially and evolved dramatically in recent years, and this new edition is designed to help the reader to adapt and take advantage of these changes.
This new edition of Getting Started in Currency Trading contains significant new information, including a chapter on computers and FOREX, managed FOREX, and new information about regulation, alongside the author's successful trading plan, designed to help the reader put it all together.


Perform innovative data analyses on neuroimaging and related data. Develop and implement computer algorithms for analyzing that data. Assume major responsibility for software and hardware development and implementation in a neuroimaging-focused, neuroscience lab.� Primary responsibilities will include collaboratively performing data analyses on neuroimaging and related data, with a major emphasis on fMRI data processing and computer programming.� Secondary responsibilities include software and hardware development, implementation for neuroimaging data and associated coordination of essential experimental procedures and files and potential contributions to collecting neuroimaging data.
Computer programming, which includes design and development of data analysis tools.
Design, develop, and implement computer algorithms and software for analyzing functional and structural MRI data of the brain and maintain data analysis programs developed over time for those data for neuroimaging-related neuroscience research purposes.
Implement and support data analysis tools; evaluate and resolve software problems for both existing and developing analysis streams for the purpose of processing and analyzing neuroimaging data and assume responsibilities for software development and effective implementation of the software for the purpose of processing and analyzing neuroimaging data.
Train research technicians on data entry methods and develop and maintain operational documentation of analysis methods.
BA/BS required with concentration in Cognitive Neuroscience, Biomedical Engineering, Computer Science, or related field.
Proficiency with standard computer programming languages (MATLAB, Python, C/C++, csh, bash) and familiarity with statistical packages (SPSS, SAS, R), psychological testing tools (Eprime, psychtoolbox) and neuroimaging software packages (FSL, SPM, FreeSurfer, AFNI and 3D Slicer).
Previous experience with functional magnetic resonance imaging or other cognitive neuroscience method.
Experience (>1 year) working in a cognitive neuroscience research laboratory, or equivalent combination of relevant experience strongly recommended.
Processing and analysis of fMRI data.
Strong programming, quantitative, and computational skills.
Ability to interact with others respectfully, supportively, and compassionately.
The Research Programmer Analyst should be able to solve day to day problems independently but know when input from a supervisor is warranted and seek such input without hesitation. When unusual conditions or situations arise, the research assistant should consult with the supervisor regarding the best course of action.
Takes direction from laboratory principal investigator and works in conjunction with data analyst.
The position will have minimal supervisory responsibilities. However, s/he will be expected to assist in training/overseeing the work of research assistants who contribute to assessment and data entry.
The work areas will be in offices in the Department of Psychological and Brain Sciences and the Department of Radiology. Work hours are somewhat flexible and will necessitate some early evening and weekend hours.
This position is in the Department of Psychological & Brain Sciences. This position is for the Danforth Campus.
The hiring range for this position is $43,856 - $59,222 annually.


text:
Q: Showing that all quadratic regular forms are isometric to the sum of one-dimensional and two-dimensional forms I was given the following problem:

Show that, in characteristic 2, every regular quadratic form is isometric to the sum of one-dimensional and two-dimensional forms

Since the question asks about $char(F)=2$, I'm unsure as to how to approach this problem: do I look for a specific isometry for all regular forms, or is there any theorem that I can utilize in order to solve this?

redpajama_set_name: RedPajamaStackExchange


text:
Q: Is there any faster ways to make DataFrame with .describe() values? I have DataFrame with 20000 rows and 1600 columns. Each row represent an observed object and each column is a date. Example:
df2 = pd.DataFrame(np.array([[1, 2, 3, 4, 5], [6, np.NaN, np.NaN, np.NaN, 10], [np.NaN, np.NaN, 14, 13, 15], [16, 17, 18, 19, 20], [21, 22, 23, 24, 25]]),
                   columns=['2016-01-01', '2016-01-02', '2016-01-03', '2016-01-04', '2016-01-05'],
                   index=[1, 2, 3, 4, 5])

I want to get new DataFrame, which should include elements of .describe() function and couple more (first value, last value and number of observations / number of dates since first observation
I've made this:
for i in df2.index:
    df[i] = df2.T[i].describe()

But it is very slow, so I am looking for some faster solutions and help with other columns
Expected result is
    count   mean  std         min   max   first_v  last_v  density
1   5       3     1.581139    1     5     1        5       1
2   2       8     2.828427    6     10    6        10      0.4
3   3       14    1.000000    13    15    14       15      1
4   5       18    1.581139    16    20    16       20      1
5   5       23    1.581139    21    25    21       25      1

A: Instead of your loop just use:
df = df2.T.describe()


text:
using System;
using dng.ResumableUpload.Log;

namespace dng.ResumableUpload.EventHandlers
{
    public delegate void UploadLoggingHandler(LogLevel logLevel, string message, ChunkUploadParameter chunkUploadParameter, Exception exception);
}


Note 1 map; colour; 37 x 43 cm., on sheet 51 x 66 cm.
Note GSGS series 4229. Second Edition (Coloured)-AMS 1. Copied from an Italian Istituto Geografico Militare map dated 1896 with principal communications revised up to 1939 from smaller scale maps. Photolithographed by the British Ordnance Survey in 1943 and revised from Air Photos. Road classification is NOT based on reconnaissance, reliability is uncertain. The meridians are based on the meridian of Rome, which is 12 degrees, 27 minutes and 7.1 seconds east of Greenwich. Contours at 10 metres (V.I.). South Italy Grid (Blue).


text:
Title: The Last Roman Emperor Topos in the Byzantine Apocalyptic Tradition
Author(s): KRAFT, András
Journal: Byzantion
DOI: 10.2143/BYZ.82.0.2174089
Christian apocalyptic sentiments of the late seventh century produced the Apocalypse of Pseudo-Methodius, a Syriac composition which proposes the immediate downfall of the Arab dominion at the hands of a last Roman emperor. This notion of the Last Roman Emperor who – after having defeated the Arabs – would usher in a time of prosperity, face the eschatological people of the North, and ultimately abdicate to God at the end of times developed into an apocalyptic motif of ubiquitous influence. Out of its long-standing and wide-ranging tradition the present article deals with the afterlife of the Pseudo-Methodian Last Roman Emperor motif in the earlier Byzantine apocalyptic tradition. By means of conceptual comparison I map the use and the adaptations of this literary topos, thereby learning how this motif was accommodated to the Byzantine audience and how it became one of the most prominent motifs of Byzantine apocalyptic thought. My source material comprises the original Syriac Apocalypse, two Syriac apocalypses that are closely related to it, its first Greek redaction, five apocalypses from the Visions of Daniel group, and the Andreas Salos Apocalypse. Among others, I conclude that these apocalyptic texts show a tendency to fragment the Last Roman Emperor motif and delay the ultimate end of the world by prolonging the eschatological decline of the Roman Empire.


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What It Takes to Build the Next Edtech Hotspot
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By Michelle Dervan Feb 27, 2015
Flickr user Tom Simpson
New York's Economic Development Corporation (NYEDC) recently asked the local edtech community to share ideas for ways to build a vibrant edtech ecosystem in the city. The agency is beginning to see edtech's potential as an engine for economic growth—and rightly so; an investment in edtech can not only create jobs and economic prosperity, but unlike adtech and fintech, can contribute to a better-educated population and workforce—-the cornerstone of an innovation economy.
NYEDC's call for ideas attracted an energetic group of educators, edupreneurs, investors and officials who suggested many ways to build New York's capacity as a hot spot. The enthusiasm displayed for this local initiative made me curious about what other cities are doing to build their edtech ecosystems, whether local activities like this can impact the industry at large and if so, what are some of the ingredients for success in creating an "Edtech Valley"? Can edtech gain insights from other sectors?
Interesting insights can be found by looking outside of edtech. Research by Michael Porter at Harvard has shown that industries participating in a strong local cluster exhibit higher employment growth, higher wage growth, more businesses created, and more patents. A cluster is defined as a mass of linked industries and institutions located in one place that enjoys unusual competitive success in a particular field.
According to Porter, certain micro-economic conditions are needed for a cluster to take root; local demand for the product/service (in the case of edtech, a large student population), presence of related industries, availability of resources such as skilled labor and capital, favorable business conditions and rivalry between firms.
However, even when all of these conditions are in place, cities have struggled to replicate the success of clusters, such as Boston's biotech hub. In his article "Why Silicon Valley Can't Be Copied," Vivek Wadhwa points to a cultural explanation. He argues cluster-building strategies have often failed because they are managed in a top-down fashion by government. In contrast, the success of the tech cluster in Silicon Valley hinged on the willingness and ability of industry stakeholders to share information and collaborate while also competing with one another.
When it comes to education, collaboration and co-opetition become even more important as ingredients for a successful cluster. Edtech's mission is more complex than your average industry; its purpose is not just to sell products, but to improve learning outcomes. The type of innovation required to improve education can't happen in a vacuum. It requires input from a multitude of stakeholders across schools, districts, institutions, government and industry.
To reflect this, the US Department of Education's Office of Education Technology has built on Porter's original research and proposed a more nuanced concept of the "Education Innovation Cluster." According to that definition, this is a forward-thinking region where commercial, academic and education partners come together to form an innovation cluster focusing on a specific challenge that their region is uniquely suited to address and solve.
Several of these forward-thinking regions are starting to emerge and experiment with different approaches to collaboration. Tom VanderArk's book, Smart Cities That Work for Everyone, provides a great analysis of the dynamics of education ecosystems across 30 U.S. cities.
Here are some of the collaboration initiatives that I think are worthy of note:
In Chicago, LEAP Innovations' Collaboratory provides space for educators, researchers and companies to scale the use of personalized technologies and tools.
In Baltimore, Edtech Maryland's Research Consortium brings together schools, universities and companies to design and implement rapid short cycle research on promising early-stage education technology and other innovative practices.
In Boston, LearnLaunch offers a physical space for Boston's edtech community and receives support from both industry and philanthropic supporters. Eileen Rudden, a partner at LearnLaunch, is an outspoken champion of edtech as a growth sector for New England. Rudden highlights institutional engagement as the next frontier for the growing edtech cluster in Boston. "To be really successful, we need more engagement of the K-12 and higher education sectors with the emerging edtech community," she says.
My hometown of Dublin, Ireland launched the Learnovate Center in 2013 to enhance the competitive advantage of the learning technology industry by partnering businesses with leading researchers from world-class higher-ed institutions. It is a public-private partnership that currently works with over 50 edtech industry partners (publishers and startups, as well as technology giants like Google) and connects them with learning technology research capabilities in Irish universities.
Meanwhile here in New York, grand plans are being laid for the city's cluster initiative. John Katzman, CEO of Noodle, has started four education companies here and he believes that a physical hub is a necessary next step to facilitate collaboration. His observation: "Bringing together for-profits and non-profits, large and small--a hub would not only provide a central space for meetups and collaboration, it would also be a place where educators and administrators could come to teach and learn from the companies."
It's still early days for each of the emerging Edtech Valleys. These regional clusters have the potential to add great value to the economy through job creation and by improving educational outcomes and achievement. The success of each city or region will depend on the degree to which they can foster a culture of collaboration and co-opetition. As members of the edtech community, we each have an exciting opportunity (and perhaps even responsibility) to look outside of our individual domains and actively support cross-sector initiatives that help strengthen education innovation clusters locally.
EdSurge Podcast
Sal Khan: Test Prep Is 'the Last Thing We Want to Be'
By Stephen Noonoo
Pearson Signals Major Shift From Print by Making All Textbook Updates 'Digital First'
By Tony Wan
Reaching the Quiet Kids in Class
By Stacey Roshan
Minerva Project Raises $57M to Support Its Tech Platform—and Spin Off Its School


Welcome to "newtech.law," the new tech law blog of Wardyński & Partners.
The collection of users' personal data is treated as a segregated database stored on the server of the portal newtech.law in a special, secure area ensuring adequate protection. Full access to the database is provided to only a small number of people authorised by the controller.


Raw material compliance and GMP do not eliminate variability. Quality by Design should minimize the risk that raw material variability will adversely affect the finished product Critical Quality Attributes. The sources of technological risk from excipients are reviewed and approaches to excipient risk management are discussed. Supplier involvement throughout the product life-cycle is recommended to minimize excipient-related risk.
CARLIN, Brian. Quality Risk Management of Compliant Excipients. Journal of Excipients and Food Chemicals, [S.l.], v. 3, n. 4, p. 143-153, dec. 2012. ISSN 21502668. Available at: <https://ojs.abo.fi/ojs/index.php/jefc/article/view/190>. Date accessed: 24 apr. 2019.


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← John G. Wright
Catherine Annie(Cote) Fifield →
Joseph "Joe" E. Burt
Posted on May 23, 2021 by Mike
Joseph "Joe" E. Burt, 63, a long-time resident of Winchester and formerly of Northfield and Greenfield, MA. died on Sunday, May 23, 2021, at Cheshire Dartmouth-Hitchcock Medical Center in Keene. He passed peacefully with the love of family near after a brief period of decline.
Joseph was born the son of the late Ruth (Phelps) and Harold Burt Jr. on December 17, 1957, in Ludlow, MA. He was educated in Montague, MA., and graduated from Franklin County Tech. School class of 1980.
On February 26, 1982, he exchanged vows with Lindsey E. Gallant in a simple service with close family and friends in attendance.
Joe was employed by McDonald's in Keene as a morning food preparation chef. Prior, he had worked at First Student School Bus Co. as a driver for five years. He retired from the United Natural Foods Company as a Warehouse and Maintenance Technician in 2007 after eight years.
He enjoyed working in his flower and vegetable gardens. Joe also raised pet goats and was a man of the lord. He was an active member of Grace Christian Fellowship in Winchester. He was a member of Stand Strong Men's Ministry at the church. Joe was a committed member of the Maintenance Committee of the Elm St. Co-Operative for several years.
Mr. Burt is survived by his wife, Lindsey E. Burt of Winchester. His three children; Elizabeth R. Angrove and her husband, Dean of Granville, N.Y. Sarah L. Sentoni of North Adams, MA. and Joanne E. Kingsley and her husband, Tristan of Ocala, FL. Six siblings; Rosemary Kampher and her husband, Richard of Lebanon, Sheila Thurston, and her husband, Jim of Hancock, VT. Ken Burt and his wife, Andrea of Irving, MA. Henry Burt and his wife, Connie Richardson of Shelburne, MA. Lou Burt and his wife, Rose of Corinth, VT. and Hazel Morse and her husband, Tim of Greenfield, MA. In addition, he is survived by; eight grandchildren, cousins, nieces, nephews, extended family, and friends. Joe is predeceased by his brother, David Burt.
In keeping with Joe's wishes, there are no calling hours. A celebration of life service will be held on Sunday, May 30, 2021, at 4 pm. in the Grace Christian Fellowship, 81 Ashuelot St. Winchester, NH. 03470. Flowers will gladly be accepted. Burial will take place later. All services are under the care of Cheshire Family Funeral Home and Crematories, 46 S. Winchester St. Swanzey, NH. 034446. WWW.cheshirefamilyfh.com


I would like to request details in regards to the request by Onerahi Primary School for Recapitation, in particular any information and details on the reasons around the request being declined by the Ministry of Education, and any communications from other parties that may have contributed to the request being declined.
In particular, the letter sent to the Board of Trustees on 22 August 2016 stated 'some of the schools within your local network have expressed concern about the change', I would like to know what concerns were raised by the other schools.
The Act allows up to 20 working days for a response, making 15 August 2017 the latest date for our response to you. If more than 20 working days are needed due to the potential workload involved in answering your request, we will notify you accordingly.


Four great options that deliver similar sound quality, battery life and comfort without the hefty price tag.
Love 'em or hate 'em, AirPods are here to stay.
These durable leather designs are built to last.
You'll be surprised at what kind of value Bose offers compared to similar sound bars from top brands.
Don't put this futuristic tech in the past just yet.


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Apr 17, 2018 8:13 am 2018-08-13T02:41:08-05:00
Overwatch just launched a season of competitive 6 vs. 6 elimination
The short season went live last night.
Image via Blizzard Entertainment
A new competitive season went live in Overwatch last night, adding a brand new ranked playlist designed specifically for Competitive Elimination players.
The new season of six vs. six Competitive Elimination will run until May 7 at 7pm CT. To access the mode, players should navigate to Overwatch's Arcade and select the Competitive Elimination card from there. As with the regular Competitive Play mode, Overwatch players will have to complete 10 placement matches.
Related: Whoops—Blizzard accidentally uploaded a minor Hanzo buff
Six vs. six Competitive Elimination pits two teams of six, naturally, against each other. There are no objectives to pursue; instead, players must eliminate the enemy team before they get eliminated themselves. Once a player has died, they can't respawn.
Overwatch developer Scott Mercer also explained that the game's "lockout" rule set is in place—meaning that when a team wins with a particular hero, that hero becomes unavailable to them for the rest of the match. Multiple rounds are placed, and the team with the most points at the end of a match wins.
"All previous elimination maps are available to play this season, but we've also added Autthaya to the mix as an elimination map," Mercer wrote in the Overwatch forum. "To play, simply choose the Competitive Elimination card in the Arcade."
Overwatch's Archives event is ongoing until April 30. There's no shortage of things to do in Overwatch this month, that's for sure. If all of Overwatch's regular modes aren't enough, the new event brought two playable brawls to Overwatch—one brand new this year, the other returning from last year.
Raze can reach the skybox on Ascent in VALORANT
Jalen Lopez - January 15, 2021
VALORANT Patch 2.01 nerfs Jett and makes extensive changes to Split
VALORANT players can trap enemies with Yoru's Dimensional Rift ability


Guests are overjoyed with the location of this private quayside development, five minutes walk to the town's centre and adjacent to the famous Ffestiniog Railway steam train station and beautiful estuary.
The apartments vary in style some are single storey whilst others occupy two floors, nearly all have open plan living rooms which include a galley kitchen and patio doors to a balcony or patio area. They all have direct access to the quayside which is surrounded by boats and yachts, and boat mooring is available by arrangement.
This select development is on an 'island' separated from the main town by the Glaslyn river and harbour. WiFi access is available at an extra charge, payable locally.
South Snowdon Wharf is a super location for a holiday it is a discrete distance (500m) from the towns many and varied amenities. These include a cinema, swimming pool and a vast selection of gift shops and restaurants.
There is easy access to sandy beaches at Borth y Gest (15 min walk) & Morfa Bychan's Black rock sands beach (2 miles).Snowdon and the pretty village of Beddgelert is 7 miles away, Portmeirion village, prestigious hotel and gardens are 2 miles. Cricieth, Caernarfon, Harlech are just a few of the castles in the area. Open farms will delight all, as will the mountain, river and costal walks on the doorstep.
The accommodation is extremely comfortably prepared with spacious rooms all on the ground floor and within a few minutes walk of Porthmadog high street with its many shops and restaurants, leisure centre and museums.
This attractive ground floor harbour-side flat on South Snowdon Wharf has the most tranquil southerly views of the estuary and Snowdonia mountains from the living room and one bedroom.


What is a Deep-Plane/Composite Face Lift?
During a deep plane/composite face lift, the face is reshaped. This involves cutting the skin under the eyes and then lifting skin, muscle and fat, as well as repositioning the muscle and removing excess fat and skin. Stitches are then used to hold the face in its desired position.
A deep-plane/composite face lift can be utilized in cases of facial trauma, sagging skin, wrinkles and congenital birth defects.
Anti-aging skincare products are a non-surgical alternative to a deep-plane composite face lift. Surgical alternatives to the procedure include laser skin resurfacing, thread lift, injectable agents, chemical skin peel, face lift, collagen replacement therapy, dermabrasion and microdermabrasion.
A deep-plane/composite face lift is performed under general anesthesia, which means that the patient is asleep and completely unaware during the procedure.
Possible risks following a deep-plane composite face lift include infection, bleeding, swelling, bruising, facial paralysis and a negative reaction to the anesthesia.
The prognosis for a positive end result following a deep-plane composite face lift is good. However, the face is still subject to the normal process of aging following the procedure.
Total recovery from a deep-plane composite face lift takes two to four weeks.


When Julian was designing his new family home he knew he wanted to create something contemporary yet elegant. The idea came to him to use matching flooring materials inside and out, however he could only find rustic materials, such as stone, which didn't suit the modern style of his home…and so Valverdi Indoor-Out was born.
Creating an indoor-outdoor living area is an excellent way to maximise space – whether you have a lot or a little. Our range of matching porcelain tiles helps you blur the lines between internal and external living spaces, creating the illusion of a seamless transition.
Take a look at our gallery for more indoor-outdoor inspiration or get in touch if you need any advice.


A December webinar by American School & University will look at how new lighting systems can improve safety and efficiency in school parking.
Universities and institutions in all markets are learning the importance of providing an inviting, safe and secure parking experience. Whether the parking area is used for students, staff or visitors see what a difference LED lighting can make to positively affect a school's expense line, virtually eliminate maintenance costs and most importantly change an age old negative perception of the parking space.
A webinar December 8 hosted by American School & University magazine will offer a deep dive on new possibilities in parking area lighting for schools and other institutional facilities. Presenters will include John Casadonte, product marketing manager for Cree Lighting, and Joe Agron, associate publisher of AS&U.
Here's where you can register: How LEDs Help Solve the Campus Parking Space Predicament.


Timmon who says she is a Christian, therefore not Muslim as the burka would suggest, was largely ignored by Scott supporters. I was intrigued, and frankly a little bored waiting for Scott's bus to roll in, so I figured I'd find out more about her.
Looking into legal suits that Timmon has filed over the years shows a person who is extremely litigious, with every case using 42 U.S. Code 1983 as the nature of the suit. U.S. Code 1983 is civil action for deprivation of rights which helps protect people and provides a remedy for a wide array of civil rights violations. What she probably didn't know at the time was that state and regional legislators, local legislatures, city council members, and county commissioners are immune from this law.
In 2006, filed suit against the City of Lansing, Michigan for violating her First and Fourteenth Amendment rights while making her refrain from saying derogatory comments about others who were non-commission members during public comments.
In November 2009, Timmon filed a suit against City Council members of Lansing, Michigan under Section 1983. Case Dismissed.
In August 2010, filed a suit under Section 1983 against a Lansing Michigan Councilwoman A'Lynne Robinson which was denied.
In November 2012, she filed a suit against President Barack Obama, House Speaker John Boehner and Senate Majority Leader Harry Reid under Section 1983.
In December 2012, she filed a suit against the United States Government and Attorney General Eric Holder under Section 1983.
In 2013, she filed a Section 1983 Civil Rights case against Rick Scott, Christopher Smith, Perry Thurston, Pam Bondi and all State of Florida Legislators, which was dismissed.
Most recently, Timmon filed a Civil Rights suit under Section 1983 against the City of Hollywood, FL in July 2014.
Timmon also claims or never denies to be an attorney in this article, however, she is neither a member of the Florida Bar or Michigan bar.
One of the things she was protesting about during Governor Scott's visit to South Florida was State Bill 178 which attempted to revise alimony laws. The bill passed in the Florida House and Senate but was ultimately vetoed by Rick Scott in May, 2013. If it had passed, it would have ended permanent alimony in Florida, making it harder to get alimony in short-term marriages, and prevented alimony payments from lasting longer than half the length of the marriage. The bill also would have required judges to give divorced parents equal custody of their children, absent extraordinary circumstances.
Timmon said that after Scott vetoed it, it caused the murder of several children.
When I looked, there were no children…anywhere.
Timmon also told me that she is responsible for all the welfare reform in this country and even worked with Newt Gingrich.
In her handout, it says that her running-mate for Governor, Charles Tolbert (NPA) is a Pastor who has a doctorate in education, a master's in theology and is a retired master sergeant in the US Army. Their brochure says they will add "spice and diversity" to the race.
One of their campaign promises is to make all driver's licenses and car registrations permanent by only registering once at the time of purchase and never again until you buy another one. A driver's license would be permanent unless one gets too many tickets.
Tamarac residents: if you're not happy with Crist or Scott, you now have another option in this election and she'll provide a lot of great material for me too.


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