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Purification and characterization of two chitinases from Streptomyces albovinaceus S-22
Two chitinases, A and B, were purified from the culture supernatant of Streptomyces albovinaceus S-22 by ammonium sulphate fraction (80%) and Sephadex G-200 gel filtration. Both enzymes had molecular weights estimated to be 43 and 45kDa by SDS polyacrylamide gel electrophoresis. The enzymes were act...
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Published in: | World journal of microbiology & biotechnology 2000-02, Vol.16 (1), p.87-89 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
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Summary: | Two chitinases, A and B, were purified from the culture supernatant of Streptomyces albovinaceus S-22 by ammonium sulphate fraction (80%) and Sephadex G-200 gel filtration. Both enzymes had molecular weights estimated to be 43 and 45kDa by SDS polyacrylamide gel electrophoresis. The enzymes were active at 40°C and pH 5.6 after 120min, and stable at temperatures below 40°C in the absence of chitin. The purified enzyme had potential for cell wall lysis of fungal pathogenesis tested.[PUBLICATION ABSTRACT] |
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ISSN: | 0959-3993 1573-0972 |
DOI: | 10.1023/A:1008926214392 |