Structural Analysis of Bioengineered α-d-Glucan Produced by a Triple Mutant of the Glucansucrase GTF180 Enzyme from Lactobacillus reuteri Strain 180: Generation of

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• 作者：Sander S. van Leeuwen ; Slavko Kralj ; Gerrit J. Gerwig ; Lubbert Dijkhuizen ; Johannis P. Kamerling
• 刊名：Biomacromolecules
• 出版年：2008
• 出版时间：August 2008
• 年：2008
• 卷：9
• 期：8
• 页码：2251-2258
• 全文大小：234K
• 年卷期：v.9,no.8(August 2008)
• ISSN：1526-4602

文摘

Site-directed mutagenesis of the glucansucrase gtf180 gene from Lactobacillus reuteri strain 180 was used to transform the active site region. The α-d-glucan (mEPS-PNNS) produced by the triple mutant V1027P:S1137N:A1139S differed in structure from that of the wild-type α-d-glucan (EPS180). Besides (α1→3) and (α1→6) linkages, as present in EPS180, mEPS-PNNS also contained (α1→4) linkages. Linkage analysis, periodate oxidation, and 1D/2D ¹H NMR spectroscopy of the intact mEPS-PNNS, as well as MS and NMR analysis of oligosaccharides obtained by partial acid hydrolysis of mEPS-PNNS afforded a composite model, which includes all identified structural features.