Immobilization and utilization of the recombinant fusion proteins trypsin-streptavidin and streptavidin-transglutaminase for modification of whey protein isolate functionality
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 50(13), 3723–3730.
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
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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