Hot-spot mapping of the interactions between chymosin and bovine κ-casein
Sørensen, Jesper and Palmer, David and Schiøtt, Birgit (2013) Hot-spot mapping of the interactions between chymosin and bovine κ-casein. Journal of Agricultural and Food Chemistry, 61 (33). pp. 7949-7959. ISSN 0021-8561 (https://doi.org/10.1021/jf4021043)
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Chymosin is a commercially important enzyme in the manufacturing of cheese. Chymosin cleaves the milk protein -casein, which initiates the clotting process. Recently, it has been shown that camel chymosin has superior enzymatic properties toward cow’s milk, compared to bovine chymosin. The two enzymes possess a high degree of homology. There are only minor differences in the binding cleft; hence, these must be important for binding the substrate. Models for the binding of a 16 amino acid fragment, consisting of the chymosin-sensitive region of bovine kappa-casein (97-112), to both enzymes have previously been presented. Computational alanine scanning for mutating 39 residues in the substrate and the bovine enzyme are presented herein, and warm- (ΔΔG > 1 kcal/mol) and hot-spot (ΔΔG > 2 kcal/mol) residues in the bovine enzyme are identified. These residues are relevant for site-directed mutagenesis, with the aim of modifying the binding affinity and in turn affecting the catalytic efficacy of the enzyme.
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Item type: Article ID code: 45157 Dates: DateEvent8 July 2013PublishedSubjects: Science > Physics Department: Faculty of Science > Physics Depositing user: Pure Administrator Date deposited: 15 Oct 2013 09:47 Last modified: 08 Apr 2024 20:49 Related URLs: URI: https://strathprints.strath.ac.uk/id/eprint/45157