Besides detailed characterizations of the films and mechanisms to explain their formation, nonspecific protein adsorption using bovine serum albumin (BSA) onto the films was studied using a quartz crystal microbalance with dissipation (QCM-D). 
QCM-D
Exploring Nonspecific Protein Adsorption on Lignocellulosic Amphiphilic Bicomponent Films.In this contribution, we explore the interaction of lignocellulosics and proteins aiming at a better understanding of their synergistic role in natural systems.  In particular, the manufacturing and characterization of amphiphilic bicomponent thin films composed of hydrophilic cellulose and a hydrophobic lignin ester in different ratios is presented which may act as a very simplified model for real systems.  Besides detailed characterizations of the films and mechanisms to explain their formation, nonspecific protein adsorption using bovine serum albumin (BSA) onto the films was studied using a quartz crystal microbalance with dissipation (QCM-D).  As it turns out, the rather low nonspecific protein adsorption of BSA on cellulose is further reduced when these hydrophobic lignins are incorporated into the films.  The lignin ester acts in these blend films as sacrificial component, probably via an emulsification mechanism.  Additionally, the amphiphilicity of the films may prevent the adsorption of BSA as well.  Although there are some indications, it remains unclear whether any kind of protein interactions in such systems are of specific nature.
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