作者: Jesper Sørensen , David S. Palmer , Karsten Bruun Qvist , Birgit Schiøtt
DOI: 10.1021/JF104898W
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摘要: Bovine chymosin has long been the preferred enzyme used to coagulate cow's milk, in initial stage of cheese production, during which it cleaves a specific bond milk protein κ-casein. Recently, camel shown have 70% higher clotting activity toward and, moreover, cleave κ-casein more selectively. chymosin, on other hand, is poor agent camel's milk. This paper reports molecular modeling study aimed at understanding this disparity, based homology and dynamics simulations using peptide fragments from cow both bovine chymosin. The results show that complex between fragment indeed less stable binding pocket. also indicate part may be due charge repulsion lysine residue an arginine P4 position