Indexed by:
Abstract:
A chitinase with antifungal activity was isolated from mung bean (Phaseolus mungo) seeds. The procedure entailed aqueous extraction, (NH4) 2SO4 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°C. It exerted antifungal action toward Fusarium solani, Fusarium oxysporum, Mycosphaerella arachidicola, Pythium aphanidermatum, and Sclerotium rolfsii. © 2004 Elsevier Inc. All rights reserved.
Keyword:
Reprint 's Address:
Email:
Source :
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
JCR Journal Grade:3
Cited Count:
SCOPUS Cited Count:
ESI Highly Cited Papers on the List: 0 Unfold All
WanFang Cited Count:
Chinese Cited Count:
30 Days PV: 1
Affiliated Colleges: