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- W2135040897 abstract "To detect cellulases encoded by uncultured microorganisms, we constructed metagenomic libraries from Korean soil DNAs. Screenings of the libraries revealed a clone pCM2 that uses carboxymethyl cellulose (CMC) as a sole carbon source. Further analysis of the insert showed two consecutive ORFs (celM2 and xynM2) encoding proteins of 226 and 662 amino acids, respectively. A multiple sequence analysis with the deduced amino acid sequences of celM2 showed 36% sequence identity with cellulase from the Synechococcus sp., while xynM2 had 59% identity to endo-1,4-β-xylanase A from Cellulomonas pachnodae. The highest enzymatic CMC hydrolysis was observable at pH 4.0 and 45 °C with recombinant CelM2 protein. Although the enzyme CelM2 additionally hydrolyzed avicel and xylan, no substrate hydrolysis was observed on oligosaccharides such as cellobiose, pNP-β-cellobioside, pNP-β-glucoside, and pNP-β-xyloside. These results showed that CelM2 is a novel endo-type cellulase." @default.
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- W2135040897 date "2008-05-01" @default.
- W2135040897 modified "2023-10-11" @default.
- W2135040897 title "Characterization of a gene encoding cellulase from uncultured soil bacteria" @default.
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- W2135040897 doi "https://doi.org/10.1111/j.1574-6968.2008.01097.x" @default.
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