BUFFALO (BOS-BUFFALI L) CHYMOSIN PURIFICATION AND PROPERTIES

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 molecul ar weight, 36 +/- 1 kDa, is similar to that of bovine calf chymosin. T he N-terminal sequence Gly-Glu-Val-Ala-Ser-Val-Pro- coincides with tha t of bovine enzyme, whereas some differences were found in the amino a cid composition of these enzymes. Buffalo and bovine enzyme possess si milar but not identical structures. General proteolytic and milk-clott ing 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 su btle differences in the functional properties of two enzymes.