Overproduction of cellulose in Acetobacter xylinum KCCM 10100 defective in GDP-mannosyltransferase

Sang Tae Park; Eungbin Kim; Young Min Kim

Overproduction of cellulose in Acetobacter xylinum KCCM 10100 defective in GDP-mannosyltransferase

Sang Tae Park, Eungbin Kim, Young Min Kim

Department of Systems Biology

Research output: Contribution to journal › Article

5 Citations (Scopus)

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

All Science Journal Classification (ASJC) codes

Biotechnology
Applied Microbiology and Biotechnology

Access to Document

Fingerprint Dive into the research topics of 'Overproduction of cellulose in Acetobacter xylinum KCCM 10100 defective in GDP-mannosyltransferase'. Together they form a unique fingerprint.

Cite this

Park, S. T., Kim, E., & Kim, Y. M. (2006). Overproduction of cellulose in Acetobacter xylinum KCCM 10100 defective in GDP-mannosyltransferase. Journal of microbiology and biotechnology, 16(6), 961-964.

@article{b31f37b57987404a86047a6d059d4b2c,

title = "Overproduction of cellulose in Acetobacter xylinum KCCM 10100 defective in GDP-mannosyltransferase",

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.",

author = "Park, {Sang Tae} and Eungbin Kim and Kim, {Young Min}",

year = "2006",

month = jun,

day = "1",

language = "English",

volume = "16",

pages = "961--964",

journal = "Journal of Microbiology and Biotechnology",

issn = "1017-7825",

publisher = "Korean Society for Microbiolog and Biotechnology",

number = "6",

}

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.

UR - http://www.scopus.com/inward/record.url?scp=33745587537&partnerID=8YFLogxK

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 -