Comparison of the hydrolysis of bovine κ-casein by camel and bovine chymosin: A kinetic and specificity study

Journal of Agricultural and Food Chemistry

Volumn 60, Issue 21, 2012, Pages 5454-5460

  Møller, Kirsten Kastberg ^a,b   Rattray, Fergal P ^b   Sørensen, Jens Christian ^a   Ardö, Ylva ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b CHR HANSEN A S   (Denmark)

Author keywords

casein; bovine chymosin; camel chymosin; enzyme specificity; Michaelis.Menten kinetics

Indexed keywords

CATALYTIC EFFICIENCIES; CHARGED CLUSTERS; CHEESE MAKING; CHYMOSIN; ELECTROSTATIC BINDING; ENZYME SPECIFICITY; FORMATION RATES; KINETIC PROPERTIES; LIQUID CHROMATOGRAPHY-MASS SPECTROMETRY; MECHANISTIC DIFFERENCES; MICHAELIS-MENTEN; MILK COAGULATION; PROTEOLYTIC ACTIVITIES; REVERSED PHASE; SUBSTRATE AFFINITY; TURNOVER RATE;

CAPILLARY ELECTROPHORESIS; CASEIN; COAGULATION; ENZYMES; HYDROLYSIS; KINETICS; PROTEOLYSIS;

MAMMALS;

CASEIN; CHYMOSIN;

ANIMAL; ARTICLE; CAMEL; CATTLE; CHEMISTRY; COMPARATIVE STUDY; HYDROLYSIS; KINETICS; PH; SPECIES DIFFERENCE;

ANIMALS; CAMELS; CASEINS; CATTLE; CHYMOSIN; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; SPECIES SPECIFICITY;

BOVINAE;

EID: 84861612118     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf300557d     Document Type: Article

References (42)

1. Walstra, P., Wouters, J. T. M., and Geurts, T. J. Dairy Science and Technology, 2 nd ed.; CRC Press: Boca Raton, FL, 2006.
2. Jacob, M.; Jaros, D.; Rohm, H. Recent advances in milk clotting enzymes Int. J. Dairy Technol. 2011, 64, 14-33
3. Gilliland, G. L.; Winborne, E. L.; Nachman, J.; Wlodawer, A. The three-dimensional structure of recombinant bovine chymosin at 2.3 Å resolution Proteins: Struct., Funct., Genet. 1990, 8, 82-101
4. Harboe, M.; Broe, M. L.; Qvist, K. B. The production, action and application of rennet and coagulants. In Technology of Cheesemaking, 2 nd ed.; Law, B. A.; Tamime, A., Eds.; Wiley-Blackwell: Oxford, United Kingdom, 2010; pp 98-129.
5. Claverie-Martín, F.; Vega-Hernández, M. C. Aspartic proteases used in cheese making. In Industrial Enzymes-Structure, Function and Applications; Polaina, J.; MacCabe, A. P., Eds.; Springer: Dordrecht, the Netherlands, 2007; pp 207-219.
6. Houen, G.; Madsen, M. T.; Harlow, K. W.; Lønblad, P.; Foltmann, B. The primary structure and enzymatic properties of porcine prochymosin and chymosin Int. J. Biochem. Cell Biol. 1996, 28, 667-675
7. Carles, C.; Martin, P. Kinetic study of the action of bovine chymosin and pepsin A on bovine κ -casein Arch. Biochem. Biophys. 1985, 242, 411-416
8. Vreeman, H. J.; Visser, S.; Slangen, C. J.; Vanriel, J. A. M. Characterization of bovine κ -casein fractions and the kinetics of chymosin-induced macropeptide release from carbohydrate-free and carbohydrate-containing fractions determined by high-performance gel-permeation chromatography Biochem. J. 1986, 240, 87-97
9. Gustchina, E.; Rumsh, L.; Ginodman, L.; Majer, P.; Andreeva, N. Post X-ray crystallographic studies of chymosin: the existence of two structural forms and the regulation of activity by the interaction with the histidine-proline cluster of κ -casein FEBS Lett. 1996, 379, 60-62
10. Hill, R. D. The nature of the rennin sensitive bond in casein and its possible relation to sensitive bonds in other proteins Biochem. Biophys. Res. Commun. 1968, 33, 659-663
11. Visser, S.; Vanrooijen, P. J.; Slangen, C. J. Peptide substrates for chymosin (rennin)-Isolation and substrate behavior of two tryptic fragments of bovine κ-casein Eur. J. Biochem. 1980, 108, 415-421
12. Visser, S.; Slangen, C. J.; Vanrooijen, P. J. Peptide substrates for chymosin (rennin)-Interaction sites in κ -casein-related sequences located outside the (103-108)-hexapeptide region that fits into the enzyme's active-site cleft Biochem. J. 1987, 244, 553-558
13. Palmer, D. S.; Christensen, A. U.; Sørensen, J.; Celik, L.; Qvist, K. B.; Schiøtt, B. Bovine chymosin: a computational study of recognition and binding of bovine κ-casein Biochemistry 2010, 49, 2563-2573
14. Kappeler, S. R.; van den Brink, H. J. M.; Rahbek-Nielsen, H.; Farah, Z.; Puhan, Z.; Hansen, E. B.; Johansen, E. Characterization of recombinant camel chymosin reveals superior properties for the coagulation of bovine and camel milk Biochem. Biophys. Res. Commun. 2006, 342, 647-654
15. Wangoh, J.; Farah, Z.; Puhan, Z. Extraction of camel rennet and its comparison with calf rennet extract Milchwissenschaft 1993, 48, 322-325
16. Bansal, N.; Drake, M. A.; Piraino, P.; Broe, M. L.; Harboe, M.; Fox, P. F.; McSweeney, P. L. H. Suitability of recombinant camel (Camelus dromedarius) chymosin as a coagulant for Cheddar cheese Int. Dairy J. 2009, 19, 510-517
17. Sørensen, J.; Palmer, D. S.; Qvist, K. B.; Schiøtt, B. 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 J. Agric. Food Chem. 2011, 59, 5636-5647
18. Jensen, J. L.; Mølgaard, A.; Poulsen, J.-C. N. H. M. K.; Harboe, M. K.; Simonsen, J. B.; Lorentzen, A. M.; Hjernø, K.; van den Brink, J. M.; Qvist, K. B.; Larsen, S. The relation between the properties and the structure of the two milk-clotting enzymes bovine and camel chymosin. Acta Crystallogr., Sect. D: Biol. Crystallogr., under revision.
19. ISO11815:IDF157. Milk-Determination of Total Milk-Clotting Activity of Bovine Rennets; International Dairy Federation: Brussels, Belgium, 2007.
20. Hollar, C. M.; Law, A. J. R.; Dalgleish, D. G.; Brown, R. J. Separation of major casein fractions using cation-exchange fast protein liquid chromatography J. Dairy Sci. 1991, 74, 2403-2409
21. S1-casein A J. Dairy Sci. 1974, 57, 341-344
22. Creamer, L. K. Milk proteins/Casein nomenclature, structure and association properties. In Encyclopedia of Dairy Sciences; Fuquay, J.; Roginski, H.; Fox, P. F., Eds.; Elsevier Science: London, 2002; Vol. 1, pp 1895-1902.
23. Harboe, M. C. Hansen A/S, Hørsholm, Denmark. Personal communication, 2010.
24. Recio, I.; Olieman, C. Determination of denatured serum proteins in the casein fraction of heat-treated milk by capillary zone electrophoresis Electrophoresis 1996, 17, 1228-1233
25. Otte, J.; Ardö, Y.; Weimer, B.; Sørensen, J. Capillary electrophoresis used to measure proteolysis in cheese Bull. IDF 1999, 337, 10-16
26. McGann, T. C. A.; Mathiassen, A.; O'Connell, J. A. Applications of the Pro-Milk Mk II. Part III. Rapid estimation of casein in milk and protein in whey Lab. Pract. 1972, 21, 628-631
27. Tolkach, A.; Kulozik, U. Fractionation of whey proteins and caseinomacropeptide by means of enzymatic crosslinking and membrane separation techniques J. Food Eng. 2005, 67, 13-20
28. Otte, J.; Midtgaard, L.; Qvist, K. B. Analysis of caseinomacropeptide(s) by free solution capillary electrophoresis Milchwissenschaft 1995, 50, 75-79
29. Farrell, H. M.; Jimenez-Flores, R.; Bleck, G. T.; Brown, E. M.; Butler, J. E.; Creamer, L. K.; Hicks, C. L.; Hollar, C. M.; Ng-Kwai-Hang, K. F.; Swaisgood, H. E. Nomenclature of the proteins of cows' milk-Sixth revision J. Dairy Sci. 2004, 87, 1641-1674
30. 2- macroglobulin Nippon Nogeikagaku Kaishi 1971, 45, 449-453 (in Japanese)
31. Mollé, D.; Léonil, J. Heterogeneity of the bovine κ -casein caseinomacropeptide, resolved by liquid chromatography on-line with electrospray ionization mass spectrometry J. Chromatogr. 1995, 708, 223-230
32. Azuma, N.; Kaminogawa, S.; Yamauchi, K. Properties of glycomacropeptide and para-κ -casein derived from human κ -casein and comparison of human and bovine κ -caseins as to susceptibility to chymosin and pepsin Agric. Biol. Chem. 1984, 48, 2025-2031
33. Garnier, J.; Mocquot, G.; Ribadeau-Dumas, B.; Maubois, J.-L. Coagulation of milk by rennet: scientific and technological aspects Ann. Nutr. Aliment. 1968, 22, B495-B552
34. Turhan, M.; Mutlu, M. Kinetics of κ-casein/chymosin hydrolysis Milchwissenschaft 1997, 52, 559-563
35. Vreeman, H. J. Association of bovine SH-κ-casein at pH 7.0 J. Dairy Res. 1979, 46, 271-276
36. Payens, T. A. J.; Both, P. Enzymatic coagulation processes. IV. The chymosin-triggered clotting of p -κ-casein. In Bioelectrochemistry: Ions, Surfaces, Membranes; Blank, M., Ed.; American Chemical Society: Washington, DC, 1980; pp 129-141.
37. Farrell, H. M.; Cooke, P. H.; Wickham, E. D.; Piotrowski, E. G.; Hoagland, P. D. Environmental influences on bovine κ-casein: Reduction and conversion to fibrillar (amyloid) structures J. Protein Chem. 2003, 22, 259-273
38. Hyslop, D. B. Enzymatic coagulation of milk. In Advanced Dairy Chemistry Vol. 1: Proteins Part B, 3 rd ed.; Fox, P. F.; McSweeney, P. L. H., Eds.; Kluwer Academic/Plenum Publishers: New York, 2003; pp 839-878.
39. van Hooydonk, A. C. M.; Walstra, P. Interpretation of the kinetics of the renneting reaction in milk Neth. Milk Dairy J. 1987, 41, 19-47
40. Vallejo, J. A.; Ageitos, J. M.; Poza, M.; Villa, T. G. Short communication: A comparative analysis of recombinant chymosins J. Dairy Sci. 2012, 95, 609-613
41. Safro, M. G.; Andreeva, N. S.; Blundell, T. L. Role of peripheral interactions in the specificity of chymosin Mol. Biol. 1987, 21, 1292-1297
42. Berg, J. M.; Tymoczko, J. L.; Stryer, L. Biochemistry, 5 th ed.; W. H. Freeman and Company: New York, 2002.