論文

査読有り
2003年10月

A synergistic reaction mechanism of a cycloalternan-forming enzyme and a D-glucosyltransferase for the production of cycloalternan in Bacillus sp NRRL B-21195

CARBOHYDRATE RESEARCH
  • YK Kim
  • ,
  • M Kitaoka
  • ,
  • HA Kiyoshi
  • ,
  • CH Kim
  • ,
  • GL Cote

338
21
開始ページ
2213
終了ページ
2220
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1016/S0008-6215(03)00375-6
出版者・発行元
ELSEVIER SCI LTD

Cycloalternan-forming enzyme (CAFE) was first described as the enzyme that produced cycloalternan from alternan. In this study, we found that a partially purified preparation of CAFE containing two proteins catalyzed the synthesis of cycloalternan from maltooligosaccharides, whereas the purified CAFE alone was unable to do so. In addition to the 117 kDa CAFE itself, the mixture also contained a 140 kDa protein. The latter was found to be a disproportionating enzyme (DE) that catalyzes transfer of a D-glucopyranosyl residue from the non-reducing end of one maltooligosaccharide to the non-reducing end of another, forming an isomaltosyl residue at the non-reducing end. CAFE then transfers the isomaltosyl residue to the non-reducing end of another isomaltosyl maltooligosaccharide, to form an alpha-isomaltosyl-(1-->3)-alpha-isomaltosyl-(1-->4)-maltooligosaccharide, and subsequently catalyzes a cyclization to produce cycloalternan. Thus, DE and CAFE act synergistically to produce cycloalternan directly from maltodextrin or starch. (C) 2003 Elsevier Ltd. All rights reserved.

リンク情報
DOI
https://doi.org/10.1016/S0008-6215(03)00375-6
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/14553982
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000186003700007&DestApp=WOS_CPL
ID情報
  • DOI : 10.1016/S0008-6215(03)00375-6
  • ISSN : 0008-6215
  • eISSN : 1873-426X
  • PubMed ID : 14553982
  • Web of Science ID : WOS:000186003700007

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