BACTERIAL CARBOXYPEPTIDASE AND ITS PRODUCTION

摘要

PURPOSE:To obtain the subject new enzyme, useful for analyzing, etc., the primary structure of a peptide due to the efficient cleavage of prolylproline bond in the peptide continuously having proline such as the one capable of inhibiting angiotensin converting enzymes from its C-terminal. CONSTITUTION:The objective carboxypeptidase. Action and substrate specificity; catalyzing the hydrolysis of prolylproline bond in a (protected)peptide continuously having proline. Optimum pH and stable pH; the optimum pH is 7.5 and stable pH is 4.5-9 when a peptide of the formula (Boc is t-butyloxycarbonyl) is used as a substrate. Action temperature; the action temperature is 5-60 deg.C and the optimum action temperature is 50 deg.C when the peptide of the formula is used as a substrate and bovine albumin is added. Inhibitor; ethylenediaminetetraacetic acid and o-phenanthroline. Isoelectric point; about 6. Molecular weight; 160000, etc. This enzyme is obtained from a culture prepared by culturing a microorganism of the genus Xanthomonas [preferably Xanthomonas sp. NA-62 strain (FERM P-12666)].