NDLI: Identification and characterization of an unusual glycosyltransferase-like enzyme with ß-galactosidase activity from a soil metagenomic library.

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Identification and characterization of an unusual glycosyltransferase-like enzyme with ß-galactosidase activity from a soil metagenomic library.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wang, Si-di Guo, Geng-shan Li, Liang Cao, Li-chuang Tong, Ling Ren, Guang-hui Liu, Yu-huan
Spatial Coverage	China
Description	Author Affiliation: Wang SD ( School of Life Sciences, Sun Yat-sen University, Guangzhou 510275, People's Republic of China.); Guo GS ( School of Life Sciences, Sun Yat-sen University, Guangzhou 510275, People's Republic of China.); Li L ( School of Life Sciences, Sun Yat-sen University, Guangzhou 510275, People's Republic of China.); Cao LC ( School of Life Sciences, Sun Yat-sen University, Guangzhou 510275, People's Republic of China.); Tong L ( School of Life Sciences, Sun Yat-sen University, Guangzhou 510275, People's Republic of China.); Ren GH ( School of Life Sciences, Sun Yat-sen University, Guangzhou 510275, People's Republic of China.); Liu YH ( School of Life Sciences, Sun Yat-sen University, Guangzhou 510275, People's Republic of China. Electronic address: lsslyh@mail.sysu.edu.cn.)
Abstract	Glycosyltransferases and glycoside hydrolases are two diversified groups of carbohydrate-active enzymes (CAZymes) in existence, they serve to build and break down the glycosidic bonds, respectively, and both categories have formed many sequence-based families. In this study, a novel gene (glyt110) conferring ß-galactosidase activity was obtained from a metagenomic library of Turpan Basin soil. Sequence analysis revealed that glyt110 encoded a protein of 369 amino acids that, rather than belonging to a family typically known for ß-galactosidase activity, belonged to glycosyltransferase family 4. Because of this unusual sequence information, the novel gene glyt110 was subsequently expressed in Escherichia coli BL21(DE3), and the recombinant enzyme (Glyt110) was purified and characterized. Biochemical characterization revealed that the ß-galactosidase activity of Glyt110 toward o-nitrophenyl-ß-D-galactopyranoside (ONPG) and lactose were identified to be 314±18.3 and 32±2.7 U/mg, correspondingly. In addition, Glyt110 can synthesize galacto-oligosaccharides (GOS) using lactose as substrate. A GOS yield of 47.2% (w/w) was achieved from 30% lactose solution at 50 °Ð¡, pH 8.0 after 10 h reaction. However, Glyt110 was unable to glycosylate either N-acetylated saccharides or lactose and galactose using UDP-gal as sugar donor, and its glycosyltransferase activity needs further investigation. These results indicated that Glyt110 is an unusual enzyme with ß-galactosidase activity but phylogenetically related to glycosyltransferase. Our findings may provide opportunities to improve the insight into the relationship between glycosyltransferases and glycoside hydrolases and the sequence-based classification.
File Format	HTM / HTML
ISSN	01410229
Volume Number	57
e-ISSN	18790909
Journal	Enzyme and Microbial Technology
Language	English
Publisher	Elsevier
Publisher Date	2014-04-10
Publisher Place	United States
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Microbiology Discipline Biochemistry Discipline Biotechnology Glycosyltransferases Genetics Metabolism Metagenome Soil Microbiology Beta-galactosidase Amino Acid Sequence Bacterial Proteins Classification China Cloning, Molecular Genes, Bacterial Genomic Library Kinetics Molecular Sequence Data Oligosaccharides Biosynthesis Phylogeny Recombinant Proteins Sequence Homology, Amino Acid Substrate Specificity Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

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