Recently identified enzymes of Brevibacterium linens ATCC 9174--a review

• Published in: Journal of food biochemistry Vol. 22; no. 5; pp. 353 - 373
• Main Authors: Rattray, F.P, Fox, P.F
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.11.1998; Blackwell
• Subjects: aminopeptidases; Bacteriology; Biological and medical sciences; Brevibacterium linens; characterization; cheese ripening; cheeses; enzyme activity; esterases; Food industries; Food microbiology; Fundamental and applied biological sciences. Psychology; Metabolism. Enzymes; metal ions; Microbiology; microorganisms; purification; serine proteinases; temperature; Enzymatic activity; Brevibacteriaceae; Bacteria; Actinomycetes; Review; Intracellular; Extracellular; Brevibacterium linens
• ISSN: 0145-8884; 1745-4514
• DOI: 10.1111/j.1745-4514.1998.tb00250.x

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 alpha s1- and beta-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.