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Proteinases of Streptomyces fradiae. III. Catalytic and some physico- chemical properties of keratinolytic proteinase.

作者信息

Galas E, Kałuźewska M

机构信息

Institute of Technical Biochemistry, Technical University, Lódź, Poland.

出版信息

Acta Microbiol Pol. 1992;41(3-4):169-177.

PMID:1284846
Abstract

It has been shown that keratinase--proteinase PIV, the main enzyme of the proteolytic system of S. fradiae, is characterized by high effectiveness in its action on AcAla3OMe--exceeding elastase in catalytic effectiveness several times. This proteinase also cleaves ester and amide bonds formed by the residues of aromatic and basic amino acids, but with a lower effectiveness than chymotrypsin or trypsin. It has also been shown that proteinase IV is a typical serine enzyme highly sensitive to DFP, acting in strongly alkaline pH (about 11.2), with molecular weight 24 kDa and does not contain cysteine.

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