Synthesis, structural analysis and application of novel acarbose-fructoside using levansucrase

被引：9

作者：

Nam, Seung-Hee ^{[3
]}

Moon, Young-Hwan ^{[4
]}

Kang, Jin ^{[1
,2
]}

Kim, Young-Min ^{[1
,2
]}

Robyt, John F. ^{[5
]}

Kim, Doman ^{[1
,2
]}

机构：

[1] Chonnam Natl Univ, Sch Biol Sci & Technol, Kwangju 500757, South Korea

[2] Chonnam Natl Univ, Res Inst Catalysis, Kwangju 500757, South Korea

[3] Jeonnam Agr Res & Extens Serv, Jeonnam 520715, South Korea

[4] Univ Maryland, Dept Mol Genet & Cell Biol, College Pk, MD 20742 USA

[5] Iowa State Univ, Dept Biochem Biophys & Mol Biol, Ames, IA 50011 USA

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 2009年 / 45卷 / 04期

关键词：

Acarbose; Acceptor reaction; Levansucrase; Leuconostoc mesenteroides; Dextransucrase; ALPHA-GLUCOSIDASE; INHIBITION; ANALOGS; GLYCOSIDASES; AMYLASES;

D O I：

10.1016/j.enzmictec.2009.07.005

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 [微生物学]; 090105 [作物生产系统与生态工程];

摘要：

Acarbose-fructoside (acarbose-Fru) was newly synthesized via the acceptor reaction of a levansucrase from Leuconostoc mesenteroides B-512 FMC with acarbose and sucrose. The resultant product was separated with 10.5% purification yield via Bio-gel P-2 column chromatography and HPLC. Its structure was determined to be 1(1)-beta-D-fructofuranosyl alpha-acarbose, according to the results of H-1, C-13, HSQC, and HMBC analyses. Acarbose-Fru was inhibited competitively on alpha-glucosidase (A. niger and baker's yeast) but mixed noncompetitively on alpha-amylases (A. oryzae and porcine pancreatic). Compared to acarbose, acarbose-Fru exhibited inhibition potency of 1.12 or 1.52 on A. niger alpha-glucosidase or A. oryzae alpha-amylase, respectively. Additionally, acarbose-Fru was identified as a novel substrate for dextransucrase with K-m and V-max values of 189.0 mM and 8.51 mu mol/(mg min), respectively. Therefore, acarbose-Fru as a substrate might be synthesized novel acarbose derivatives by using dextransucrase. (C) 2009 Elsevier Inc. All rights reserved.

引用

页码：247 / 252

页数：6

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