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

@article{Kappeler2006CharacterizationOR,
  title={Characterization of recombinant camel chymosin reveals superior properties for the coagulation of bovine and camel milk.},
  author={Stefan R Kappeler and Hans J M van den Brink and Henrik Rahbek-Nielsen and Zakaria Farah and Zdenko Puhan and Egon Bech Hansen and Eric Johansen},
  journal={Biochemical and biophysical research communications},
  year={2006},
  volume={342 2},
  pages={647-54}
}
Enzymatic milk coagulation for cheese manufacturing involves the cleavage of the scissile bond in kappa-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… CONTINUE READING

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