Abstract
GDP-mannosyltransferase (GMT) is an enzyme responsible for the addition of a mannose to glucose (α[1→3]) during biosynthesis of the water-soluble branched polysaccharide acetan in Acetobacter 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.
| Original language | English |
|---|---|
| Pages (from-to) | 961-964 |
| Number of pages | 4 |
| Journal | Journal of microbiology and biotechnology |
| Volume | 16 |
| Issue number | 6 |
| Publication status | Published - 2006 Jun 1 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
- Applied Microbiology and Biotechnology
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Overproduction of cellulose in Acetobacter xylinum KCCM 10100 defective in GDP-mannosyltransferase. / Park, Sang Tae; Kim, Eungbin; Kim, Young Min.
In: Journal of microbiology and biotechnology, Vol. 16, No. 6, 01.06.2006, p. 961-964.Research output: Contribution to journal › Article
TY - JOUR
T1 - Overproduction of cellulose in Acetobacter xylinum KCCM 10100 defective in GDP-mannosyltransferase
AU - Park, Sang Tae
AU - Kim, Eungbin
AU - Kim, Young Min
PY - 2006/6/1
Y1 - 2006/6/1
N2 - GDP-mannosyltransferase (GMT) is an enzyme responsible for the addition of a mannose to glucose (α[1→3]) during biosynthesis of the water-soluble branched polysaccharide acetan in Acetobacter 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.
AB - GDP-mannosyltransferase (GMT) is an enzyme responsible for the addition of a mannose to glucose (α[1→3]) during biosynthesis of the water-soluble branched polysaccharide acetan in Acetobacter 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=33745587537&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:33745587537
VL - 16
SP - 961
EP - 964
JO - Journal of Microbiology and Biotechnology
JF - Journal of Microbiology and Biotechnology
SN - 1017-7825
IS - 6
ER -