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A Thermostable Chitinase with Chitin‐Binding Activity from Phaseolus limensis
Author(s) -
Wang S.Y.,
Zhou J.J.,
Shao B.,
Lu Y.J.,
Rao P.F.
Publication year - 2008
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1750-3841.2008.00800.x
Subject(s) - chitinase , chitin , isoelectric point , phaseolus , pythium aphanidermatum , affinity chromatography , ammonium sulfate precipitation , chromatography , chemistry , sclerotium , isoelectric focusing , high performance liquid chromatography , rhizoctonia solani , enzyme , biochemistry , biology , botany , size exclusion chromatography , biological pest control , chitosan
A 28.6‐kDa chitinase with chitin‐binding activity was isolated from the large lima bean ( Phaseolus limensis ) seeds. The procedure entailed extraction, ammonium sulfate precipitation, affinity chromatography on Affi‐gel blue gel, and high‐performance liquid chromatography (HPLC) on SP‐Toyopearl. There was an almost 108‐fold increase in specific activity of the purified chitinase compared with that of the crude extract. The enzyme exhibited a pI of 7.8 by isoelectric focusing electrophoresis. The optimum pH and the optimum temperature for activity toward N‐acetyld‐glucosamine were 5.4 and 40 to 50 °C, respectively. The enzyme was stable up to 55 °C. It exerted a potent inhibitory action toward fungal species, including Fusarium solani, Pythium aphanidermatum , and Sclerotium rolfsii.