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.
引用
收藏
页码:5636 / 5647
页数:12
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  • [1] PROTON ASSIGNMENT AND STRUCTURAL FEATURES OF A PEPTIDE FROM THE CHYMOSIN-SENSITIVE REGION OF BOVINE KAPPA-CASEIN DETERMINED BY 2D-NMR SPECTROSCOPY
    PLOWMAN, JE
    SMITH, MH
    CREAMER, LK
    LIDDELL, MJ
    CODDINGTON, JM
    GIBSON, JJ
    ENGELBRETSEN, DR
    MAGNETIC RESONANCE IN CHEMISTRY, 1994, 32 (08) : 458 - 464