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Overproduction of Cellulose in Acetobacter xylinum KCCM 10100 Defective in GDP-Mannosyltransferase  

Park Sang-Tae (Children's Hospital Boston, Harvard Medical School)
Kim Eung-Bin (Department of Biology and Institute of Life Science and Biotechnology, Yonsei University)
Kim Young-Min (Department of Biology and Institute of Life Science and Biotechnology, Yonsei University)
Publication Information
Journal of Microbiology and Biotechnology / v.16, no.6, 2006 , pp. 961-964 More about this Journal
Abstract
GDP-mannosyltransferase (GMT) is an enzyme responsible for the addition of a mannose to glucose ($\alpha$[1$\rightarrow$3]) during biosynthesis of the water-soluble branched polysaccharide acetan in Acefobacter species. In an effort to obtain a cellulose-overproducing bacterium, a mutant defective in GMT of Acetobacter xylinum KCCM 10100 was constructed by single crossover homologous recombination using part of the aceA gene encoding GMT amplified by polymerase chain reaction. The GMT-disrupted mutant produced 23% more cellulose, but 16% less water-soluble polysaccharide than those of the wild-type strain. Analysis of the sugar composition by gel permeation chromatography revealed that water-soluble polysaccharides produced by the GMT-defective mutant contained no mannose molecule.
Keywords
Acetobacter xylinum; cellulose; aceA; GDP-mannosyltransferase; water-soluble polysaccharide;
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