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Characterization of recombinant camel chymosin reveals superior properties for the coagulation of bovine and camel milk

2006; Elsevier BV; Volume: 342; Issue: 2 Linguagem: Inglês

10.1016/j.bbrc.2006.02.014

1090-2104

Stefan Kappeler, Hans M. van den Brink, Henrik Rahbek-Nielsen, Zakaria Farah, Z. Puhan, Egon Bech Hansen, Eric Johansen,

Protein purification and stability

Enzymatic milk coagulation for cheese manufacturing involves the cleavage of the scissile bond in κ-casein by an aspartic acid protease. Bovine chymosin is the preferred enzyme, combining a strong clotting activity with a low general proteolytic activity. In the present study, we report expression and enzymatic properties of recombinant camel chymosin expressed in Aspergillus niger. Camel chymosin was shown to have different characteristics than bovine chymosin. Camel chymosin exhibits a 70% higher clotting activity for bovine milk and has only 20% of the unspecific protease activity for bovine chymosin. This results in a sevenfold higher ratio of clotting to general proteolytic activity. The enzyme is more thermostable than bovine chymosin. Kinetic analysis showed that half-saturation is achieved with less than 50% of the substrate required for bovine chymosin and turnover rates are lower. While raw camel milk cannot be clotted with bovine chymosin, a high clotting activity was found with camel chymosin.