Proteinases of Streptomyces fradiae. III. Catalytic and some physico- chemical properties of keratinolytic proteinase. |
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| Authors: | E Galas M Ka?u?ewska |
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| Affiliation: | Institute of Technical Biochemistry, Technical University, Lód?, Poland. |
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| 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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