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- W2000801278 abstract "Stenotrophomonas maltophilia chitinase (StmChiA and StmChiB) genes were cloned and expressed as soluble proteins of 70.5 and 41.6 kDa in Escherichia coli. Ni-NTA affinity purified StmChiA and StmChiB were optimally active at pH 5.0 and 7.0, respectively and exhibited broad range pH activity. StmChiA and StmChiB had an optimum temperature of 40°C and are stable up to 50 and 40°C, respectively. Hydrolytic activity on chitooligosaccharides indicated that StmChiA was an endo-acting enzyme releasing chitobiose and StmChiB was both exo/endo-acting enzyme with the release of GlcNAc as the final product. StmChiA showed higher preference to β-chitin and exhibited transglycosylation on even chain length tetra- and hexameric substrates. StmChiA, and not StmChiB, was active on chitinous polymers and showed antifungal activity against Fusarium oxysporum." @default.
- W2000801278 created "2016-06-24" @default.
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- W2000801278 date "2013-04-01" @default.
- W2000801278 modified "2023-09-23" @default.
- W2000801278 title "Chitinase A from Stenotrophomonas maltophilia shows transglycosylation and antifungal activities" @default.
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- W2000801278 doi "https://doi.org/10.1016/j.biortech.2013.01.103" @default.
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