AI Article Synopsis
- A novel xyloglucan-specific endo-beta-1,4-glucanase (XEG) from Geotrichum sp. M128 was isolated, showing a molecular mass of 80 kDa and enzyme activity targeted at xyloglucan, but not at other polysaccharides.
- XEG displays specific substrate recognition with four defined subsites, particularly acknowledging xylose branching at +1 and +2 positions in xyloglucan oligosaccharides.
- The full-length cDNA for XEG was cloned, revealing a sequence coding for a 776-amino acid protein classified as a family 74 glycosyl hydrolase, and the active enzyme was successfully expressed in E. coli.
Article Abstract
A novel xyloglucan-specific endo-beta-1,4-glucanase (XEG), xyloglucanase, with a molecular mass of 80 kDa and a pI of 4.8, was isolated from the fungus Geotrichum sp. M128. It was found to be an endoglucanase active toward xyloglucan and not active toward carboxymethylcellulose, Avicel, or barley 1,3-1,4-beta-glucan. Analysis of the precise substrate specificity using various xyloglucan oligosaccharide structures revealed that XEG has at least four subsites (-2 to +2) and specifically recognizes xylose branching at the +1 and +2 sites. The full-length cDNA encoding XEG was cloned and sequenced. It consists of a 2436-bp open reading frame encoding a 776-amino acid protein. From its deduced amino acid sequence, XEG can be classified as a family 74 glycosyl hydrolase. The cDNA encoding XEG was then expressed in Escherichia coli, and enzymatically active recombinant XEG was obtained.
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| http://dx.doi.org/10.1016/S0014-5793(04)00068-7 | DOI Listing |
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Article Synopsis
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- XEG displays specific substrate recognition with four defined subsites, particularly acknowledging xylose branching at +1 and +2 positions in xyloglucan oligosaccharides.
- The full-length cDNA for XEG was cloned, revealing a sequence coding for a 776-amino acid protein classified as a family 74 glycosyl hydrolase, and the active enzyme was successfully expressed in E. coli.
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