The determination of the number and the specificity of peptide hydrolases and arylamidases present in a cell‐free sonicate from Flavobacterium II b, a species phenotypically similar to Flavobacterium balustinum, involved polyacrylamide gel electrophoresis and coloration of end products or staining procedures using diazotation reactions. Only substrates with L‐configuration amino acids and dipeptides with an unsubstituted RN‐group were cleaved. One protein band, that was able to hydrolyse skimmed milk agar, was observed but carboxypeptidase and endopep‐tidase (chymotrypsin and trypsin activities) were absent. Zymograms exhibited ary‐lamidase, dipeptidase and tripeptidase activities. Results underline the distinction between the L‐leucine aminopeptidase and the L‐leucylarylamidase.
Aeromonas hydrophila LP 50, isolated from packaged pasteurized milk, was grown in glucose-polypeptone medium at 30 degrees C. The proteolytic activity of A. hydrophila LP 50, optimum at the stationary phase of growth, is attributed to extracellular or membrane protease; no intracellular proteolytic activity was shown.
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