Abstract
An extracellular proteinase and an aminopeptidase and an intracellular aminopeptidase and esterase were isolated from Brevibacterium linens ATCC 9174. The proteinase was a serine enzyme with relatively broad specificity on α s1 -and β-caseins. The extracellular aminopeptidase was a metallo enzyme but the intracellular aminopeptidase was a thiol enzyme with rather narrow specificity for small side chains, e.g., Gly and Ala. The organism possessed two intracellular esterases, one of which was purified to homogeneity. This enzyme was a tetramer of MW 200 kDa, was strongly inhibited by thiol blocking agents and showed a high specificity for short chain fatty acids with no lipolytic activity on tributyrin or milk fat.
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