期刊
GLYCOBIOLOGY
卷 21, 期 3, 页码 304-328出版社
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwq165
关键词
beta-d-glucan; non-Leloir beta-glucosyltransferase; oligosaccharide synthesis; proteobacteria
资金
- Icelandic Research Fund
- University of Iceland
Over the years several beta-glucan transferases from yeast and fungi have been reported, but enzymes with such an activity from bacteria have not been characterized so far. In this work, we describe the cloning and expression of genes encoding beta-glucosyltransferase domains of glycosyl hydrolase family GH17 from three species of proteobacteria: Pseudomonas aeruginosa PAO1, P. putida KT2440 and Azotobacter vinelandii ATCC BAA-1303. The encoded enzymes of these GH17 domains turned out to have a non-Leloir trans-beta-glucosylation activity, as they do not use activated nucleotide sugar as donor, but transfer a glycosyl group from a beta-glucan donor to a beta-glucan acceptor. More particularly, the activity of the three recombinant enzymes on linear (beta 1 -> 3)-linked gluco-oligosaccharides (Lam-Glc(4-9)) and their corresponding alditols (Lam-Glc(4-9)-ol) was studied. Detailed structural analysis, based on thin-layer chromatography, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, electrospray ionization mass spectrometry, and 1D/2D H-1 and C-13 nuclear magnetic resonance data, revealed diverse product spectra. Depending on the enzyme used, besides (beta 1 -> 3)-elongation activity, (beta 1 -> 4)- or (beta 1 -> 6)-elongation, or (beta 1 -> 6)-branching activities were also detected.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据