Initial stage of cheese production: a molecular modeling study of bovine and camel chymosin complexed with peptides from the chymosin-sensitive region of kappa-casein

J. Sørensen, D. S. Palmer, K. B. Qvist, B. Schiøtt

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

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.
LanguageEnglish
Pages5636-5647
Number of pages12
JournalJournal of Agricultural and Food Chemistry
Volume59
Issue number10
DOIs
Publication statusPublished - 1 May 2011

Fingerprint

Chymosin
chymosin
Camelus
Cheeses
Molecular modeling
kappa-casein
Cheese
camels
Caseins
cheeses
peptides
Peptides
cattle
Milk
camel milk
milk
Peptide Fragments
molecular dynamics
Milk Proteins
Molecular Dynamics Simulation

Keywords

  • bovine chymosin
  • peptides
  • cheese production

Cite this

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title = "Initial stage of cheese production: a molecular modeling study of bovine and camel chymosin complexed with peptides from the chymosin-sensitive region of kappa-casein",
abstract = "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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author = "J. S{\o}rensen and Palmer, {D. S.} and Qvist, {K. B.} and B. Schi{\o}tt",
year = "2011",
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T1 - Initial stage of cheese production: a molecular modeling study of bovine and camel chymosin complexed with peptides from the chymosin-sensitive region of kappa-casein

AU - Sørensen, J.

AU - Palmer, D. S.

AU - Qvist, K. B.

AU - Schiøtt, B.

PY - 2011/5/1

Y1 - 2011/5/1

N2 - 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.

AB - 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.

KW - bovine chymosin

KW - peptides

KW - cheese production

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