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
- ,
- ,
- ,
- ,
- 巻
- 338
- 号
- 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
- 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