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Initial Stage of Cheese Production: A Molecular Modeling Study of Bovine and Camel Chymosin Complexed with Peptides from the Chymosin-Sensitive Region of κ-Casein
被引:17
|作者:
Sorensen, Jesper
[1
,2
,3
]
Palmer, David S.
[3
]
Qvist, Karsten Bruun
[4
]
Schiott, Birgit
[1
,2
]
机构:
[1] Aarhus Univ, Ctr Insoluble Prot Struct InSPIN, DK-8000 Aarhus C, Denmark
[2] Aarhus Univ, Interdisciplinary Nanosci Ctr INANO, DK-8000 Aarhus C, Denmark
[3] Aarhus Univ, Dept Chem, DK-8000 Aarhus C, Denmark
[4] Chr Hansen Inc, Cultures & Enzymes Div, Innovat, DK-2970 Horsholm, Denmark
关键词:
chymosin;
kappa-casein;
molecular dynamics;
homology modeling;
X-RAY-ANALYSIS;
ACTIVE-SITE;
ASPARTIC PROTEINASES;
DYNAMICS;
RESOLUTION;
PREDICTION;
RATIONALIZATION;
SIMULATIONS;
COAGULATION;
REFINEMENT;
D O I:
10.1021/jf104898w
中图分类号:
S [农业科学];
学科分类号:
09 ;
摘要:
Bovine chymosin has long been the preferred enzyme used to coagulate cow's milk, in the initial stage of cheese production, during which it cleaves a specific bond in the milk protein kappa-casein. Recently, camel chymosin has been shown to have a 70% higher clotting activity toward cow's milk and, moreover, to cleave kappa-casein more selectively. Bovine chymosin, on the other hand, is a poor clotting agent toward camel's milk. This paper reports a molecular modeling study aimed at understanding this disparity, based on homology modeling and molecular dynamics simulations using peptide fragments of kappa-casein from cow and camel in both bovine and camel chymosin. The results show that the complex between bovine chymosin and the fragment of camel kappa-casein is indeed less stable in the binding pocket. The results also indicate that this in part may be due to charge repulsion between a lysine residue in bovine chymosin and an arginine residue in the P4 position of camel kappa-casein.
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页码:5636 / 5647
页数:12
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