Asp 8.86 9.91 9.60 8.51 9.21 Thr 3.00 3.99 8.02 3.17 3.43 Ser 4.15 5.38 5.38 4.79 4.86 Glu 25.58 21.79 18.32 18.58 21.57 Pro 1.48 1.56 1.73 3.36 3.90 Gly 5.12 5.38 5.32 3.86 4.47 Ala 4.04 3.88 4.48 4.80 4.81 Val 4.06 5.15 4.45 4.57 5.72 Cys 1.00 0 0.47 0.90 1.87 Met 0.61 0 0 1.71 1.77 Ile 2.46 3.57 2.95 3.10 3.69 Leu 6.11 7.99 7.26 6.20 6.99 Tyr 1.88 1.98 3.02 1.82 1.09 Phe 5.19 5.76 5.47 3.87 4.79 Lys 7.38 4.78 5.61 11.76 4.16 His 3.86 2.60 2.82 2.77 2.16 Arg 15.21 16.86 15.03 16.42 15.48 1 Corresponding to table 4, Paper I, 2 (Santoso et al., 1996) 3 (USDA, 2014) Fig. 3. Essential amino acids profile of the three protein fractions obtained on the wet processing of coconut (recalculated from Table 2 and 6). Solubility profile of the press-cake protein Protein solubility is probably the first physicochemical property of interest when characterising the functionality of a protein, since it controls the extent to which functional properties such as emulsification, gelation and water retention are performed (Moure et al., 2006). It means that any change in the protein solubility (concentration) will directly influence the related property of interest. The major coconut protein fraction, cocosin, a storage globulin, is water insoluble, but soluble in aqueous salt solutions at a given ionic strength, as shown in Table 5. The solubility of globular proteins is pH-dependent, exhibiting minimum solubility at the isoelectric point.
Asp Thr Ser Glu Pro Gly Ala Val Cys Met Ile Leu Tyr Phe Lys His Arg 8.86 3.00 4.15 25.58 1.48 5.12 4.04 4.06 1.00 0.61 2.46 6.11 1.88 5.19 7.38 3.86 15.21 9.91 3.99 5.38 21.79 1.56 5.38 3.88 5.15 0 0 3.57 7.99 1.98 5.76 4.78 2.60 16.86 9.60 8.02 5.38 18.32 1.73 5.32 4.48 4.45 0.47 0 2.95 7.26 3.02 5.47 5.61 2.82 15.03 8.51 3.17 4.79 18.58 3.36 3.86 4.80 4.57 0.90 1.71 3.10 6.20 1.82 3.87 11.76 2.77 16.42 9.21 3.43 4.86 21.57 3.90 4.47 4.81 5.72 1.87 1.77 3.69 6.99 1.09 4.79 4.16 2.16 15.48 1 Corresponding to table 4, Paper I, 2 (Santoso et al., 1996) 3 (USDA, 2014) Fig. 3. Essential amino acids profile of the three protein fractions obtained on the wet processing of coconut (recalculated from Table 2 and 6). Solubility profile of the press-cake protein Protein solubility is probably the first physicochemical property of interest when characterising the functionality of a protein, since it controls the extent to which functional properties such as emulsification, gelation and water retention are performed (Moure et al., 2006). It means that any change in the protein solubility (concentration) will directly influence the related property of interest. The major coconut protein fraction, cocosin, a storage globulin, is water insoluble, but soluble in aqueous salt solutions at a given ionic strength, as shown in Table 5. The solubility of globular proteins is pH-dependent, exhibiting minimum solubility at the isoelectric point.
5422124.docx