Comp Biochem Physiol B Biochem Mol Biol. 1996 Jan;113(1):57-62.

Buffalo (Bos buffali L.) chymosin purification and properties.

Abdel Malak CA, Abou El Adab IF, Vukashinovic V, Zalunin IA, Timokhina EA, Lavrenova GI, Stepanov VM.

Source

Chemistry Department, Mansoura University, Egypt.

Abstract

Buffalo chymosin was isolated from abomasum mucosa extract of buffalo calves by affinity chromatography on gramicidin S-agarose followed by ion exchange chromatography on gamma-aminopropylsilochrom. Its molecular weight, 36 +/- 1 kDa, is similar to that of bovine calf chymosin. The N-terminal sequence Gly-Glu-Val-Ala-Ser-Val-Pro- coincides with that of bovine enzyme, whereas some differences were found in the amino acid composition of these enzymes. Buffalo and bovine enzyme possess similar but not identical structures. General proteolytic and milk-clotting activities of buffalo chymosin are also similar to those of bovine proteinase. pH-Optimum of its activity against hemoglobin lies at pH 4.0, somewhat higher than that for bovine chymosin, which indicates subtle differences in the functional properties of two enzymes.

PMID:

 

8936042

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