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RECENTLY IDENTIFIED ENZYMES OF BREVIBACTERIUM LINENS ATCC 9174 ‐ A REVIEW
Author(s) -
RATTRAY FERGAL P.,
FOX PATRICK F.
Publication year - 1998
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1998.tb00250.x
Subject(s) - aminopeptidase , brevibacterium , biochemistry , enzyme , extracellular , intracellular , esterase , chemistry , tributyrin , exopeptidase , biology , amino acid , lipase , leucine , bacteria , microorganism , genetics
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.