Structural characterization of linear isomalto-/malto-oligomer products synthesized by the novel GTFB 4,6-α-glucanotransferase enzyme from Lactobacillus reuteri 121

被引：76

作者：

Dobruchowska, Justyna M. ^{[1
]}

Gerwig, Gerrit J. ^{[1
]}

Kralj, Slavko ^{[1
]}

Grijpstra, Pieter ^{[1
]}

Leemhuis, Hans ^{[1
]}

Dijkhuizen, Lubbert ^{[1
]}

Kamerling, Johannis P. ^{[1
]}

机构：

[1] Univ Groningen, Dept Microbiol, Groningen Biomol Sci & Biotechnol Inst GBB, NL-9747 AG Groningen, Netherlands

来源：

GLYCOBIOLOGY | 2012年 / 22卷 / 04期

关键词：

alpha-d-glucans; glucansucrase; GTFB; 4; 6-alpha-glucanotransferase; Lactobacillus reuteri; structural analysis; ALPHA-D-GLUCANS; REUTERANSUCRASE; SPECIFICITY; MECHANISM; MUTANT;

D O I：

10.1093/glycob/cwr167

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Recently, a novel glucansucrase (GS)-like gene (gtfB) was isolated from the probiotic bacterium Lactobacillus reuteri 121 and expressed in Escherichia coli. The purified recombinant GTFB enzyme was characterized and turned out to be inactive with sucrose, the natural GS substrate. Instead, GTFB acted on malto-oligosaccharides (MOSs), thereby yielding elongated gluco-oligomers/polymers containing besides (alpha 1 -> 4) also (alpha 1 -> 6) glycosidic linkages, and it was classified as a 4,6-alpha-glucanotransferase. To gain more insight into its reaction specificity, incubations of the GTFB enzyme with a series of MOSs and their corresponding alditols [degree of polymerization, DP2(-ol)-DP7(-ol)] were carried out, and (purified) products were structurally analyzed with matrix-assisted laser desorption ionization time-of-flight mass spectrometry and one-/two-dimensional H-1 and C-13 nuclear magnetic resonance spectroscopy. With each of the tested malto-oligomers, the GTFB enzyme yielded series of novel linear isomalto-/malto-oligomers, in the case of DP7 up to DP > 35.

引用

页码：517 / 528

页数：12

共 15 条

[1]

DISPROPORTIONATION REACTIONS CATALYZED BY LEUCONOSTOC AND STREPTOCOCCUS GLUCANSUCRASES [J].