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A chitinase with antifungal activity was isolated from mung bean (Phaseolus mungo) seeds. The procedure entailed aqueous extraction, (NH4)(2)SO4 precipitation, ion-exchange chromatography on CM-Sepharose, high-performance liquid chromatography (HPLC) on Poros HS-20, and gel filtration on Sephadex G-75. The protein exhibited a molecular mass of 30.8 kDa in SDS polyacrylamide gel electrophoresis. Its pI was 6.3 as determined by isoelectric focusing. The specific activity of the chitinase was estimated to be 3.81 U/mg. The enzyme expressed its optimum activity at pH 5.4 and was stable from 40 to 50 degrees C. It exerted antifungal action toward Fusarium solani, Fusarium oxysporum, Mycosphaerella arachidicola, Pythium aphanidermatum, and Sclerotium rolfsii. (c) 2004 Elsevier Inc. All rights reserved.
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PROTEIN EXPRESSION AND PURIFICATION
ISSN: 1046-5928
Year: 2005
Issue: 2
Volume: 40
Page: 230-236
1 . 5 5 3
JCR@2005
1 . 4 0 0
JCR@2023
ESI Discipline: BIOLOGY & BIOCHEMISTRY;
JCR Journal Grade:3
Cited Count:
WoS CC Cited Count: 65
SCOPUS Cited Count: 69
ESI Highly Cited Papers on the List: 0 Unfold All
WanFang Cited Count:
Chinese Cited Count:
30 Days PV: 1
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