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

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 a...

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Veröffentlicht in:	Biochemical and biophysical research communications 2006-04, Vol.342 (2), p.647-654
Hauptverfasser:	Kappeler, Stefan R., van den Brink, Hans (J.) M., Rahbek-Nielsen, Henrik, Farah, Zakaria, Puhan, Zdenko, Hansen, Egon Bech, Johansen, Eric
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Aspergillus niger Aspergillus niger - genetics Base Sequence Camel chymosin Camelus Camelus dromedarius Caseins - chemistry Cattle Cheese Chymosin - chemistry Chymosin - genetics Chymosin - physiology Fermentation Heterologous gene expression Hydrogen-Ion Concentration Hydrolysis Kinetics Milk - enzymology Milk clotting enzyme Molecular Sequence Data Molecular Weight Recombinant Proteins - chemistry Recombinant Proteins - genetics Temperature Transfection
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