Immobilization and Utilization of the Recombinant Fusion Proteins Trypsin−Streptavidin and Streptavidin−Transglutaminase for Modification of Whey Protein Isolate Functionality
Wilcox, C. P., Clare, D. A., Valentine, V. W., & Swaisgood, H. E. (2002, May 21). Journal of Agricultural and Food Chemistry.
author keywords: immobilization; trypsin; transglutaminase; whey protein; functionality
MeSH headings : Adsorption; Biotinylation; Chemical Phenomena; Chemistry, Physical; Cross-Linking Reagents; DNA, Recombinant; Dithiothreitol / pharmacology; Enzymes, Immobilized; Escherichia coli / genetics; Gels; Glass; Milk Proteins / chemistry; Milk Proteins / metabolism; Recombinant Fusion Proteins; Streptavidin / genetics; Temperature; Transglutaminases / genetics; Transglutaminases / metabolism; Trypsin / genetics; Trypsin / metabolism; Viscosity; Whey Proteins
topics (OpenAlex): Proteins in Food Systems; Blood properties and coagulation; Transgenic Plants and Applications
TL;DR:
By combining limited proteolysis with controlled cross-linking, it was possible to create derivatives of whey proteins with enhanced functional properties that allowed for recycling of the enzyme, eliminated the requirement for a downstream inactivation step, and permitted control over the extent of modification.
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