Purifications and Some Properties of Two Chitinases fromStreptomyces orientalisWhich LyseRhizopusCell Wall
- 1 December 1976
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 40 (12) , 2325-2333
- https://doi.org/10.1080/00021369.1976.10862407
Abstract
S. orientalis was selected as a microorganism which produced chitinase having lytic acitivity on Rhizopus cell wall. Two chitinases (chitinase I and II) which had very similar properties were purified to an ultracentrifugally homogeneous state from the culture broth of this organism by SP-Sephadex and Sephadex G-100 chromatographies. MW of chitinase I and II were estimated as about 33,000 and 25,000, and isoelectric points as pH 8.80 and 8.65, respectively. Both chitinases were most active at pH values from 5.5-6.5, and were stable in the range of pH 6.0-8.0 at 40.degree. C for 3 h. They were stable at temperatures below 50.degree. C for 15 min. Rhizopus cell wall was almost completely degraded by a cooperative action of these chitinases, and a protease and a chitosanase from Bacillus R-4.This publication has 4 references indexed in Scilit:
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