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题名: Isolation and characterization of a novel alpha-glucosidase with transglycosylation activity from Arthrobacter sp DL001
作者: Zhou, Kun1, 2;  Luan, Hong-wei1;  Hu, Ying1;  Ge, Guang-bo1;  Liu, Xing-bao1;  Ma, Xiao-chi3;  Hou, Jie3;  Wang, Xiu-li1;  Yang, Ling1
关键词: Arthrobacter sp. ;  Hydrolysis ;  Transglycosylation ;  Substrate specificity
刊名: JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
发表日期: 2012-08-01
DOI: 10.1016/j.molcatb.2012.04.016
卷: 80, 页:48-57
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology ;  Life Sciences & Biomedicine ;  Physical Sciences
类目[WOS]: Biochemistry & Molecular Biology ;  Chemistry, Physical
研究领域[WOS]: Biochemistry & Molecular Biology ;  Chemistry
英文摘要: A strain of Arthrobacter sp. DL001 with high transglycosylation activity was successfully isolated from the Yellow Sea of China. To purify the extracellular enzyme responsible for transglycosylation, a four-step protocol was adopted and the enzyme with electrophoretical purity was obtained. The purified enzyme has a molecular mass of 210 kDa and displays a narrow hydrolysis specificity towards alpha-1,4-glucosidic bond. Its hydrolytic activity was identified as decreasing in the order of maltotriose > panose > maltose. Only 3.61% maltose activity occurs when p-nitrophenyl alpha-D-glycopyranoside serves as a substrate, suggesting that this enzyme belongs to the type II alpha-glucosidase. In addition, the enzyme was able to transfer glucosyl groups from the donors containing alpha-1,4-glucosidic bond specific to glucosides, xylosides and alkyl alcohols in alpha-1,4- or alpha-1,6-manners. A decreased order of activity was observed when maltose, maltotriose, panose, beta-cyclodextrin and soluble starch served as glycosyl donors, respectively. When maltose was utilized as a donor and a series of p-nitrophenyl-glycosides as acceptors, the glucosidase was capable of transferring glucosyl groups to p-nitrophenyl-glucosides and p-nitrophenyl-xylosides in alpha-1,4- or alpha-1,6-manners. The yields of p-nitrophenyl-oligosaccharides could reach 42-60% in 2 h. When a series of alkyl alcohols were utilized as acceptors, the enzyme exhibited its transglycosylation activities not only to the primary alcohols but also to the secondary alcohols with carbon chain length 1-4. Therefore, all the results indicated that the purified alpha-glucosidase present a useful tool for the biosynthesis of oligosaccharides and alkyl glucosides. (C) 2012 Elsevier B.V. All rights reserved.
关键词[WOS]: WHITE JADE SNAIL ;  OLIGOSACCHARIDE SYNTHESIS ;  ENZYMATIC-SYNTHESIS ;  SUBSTRATE-SPECIFICITY ;  GLYCOSYL HYDROLASES ;  APLYSIA-FASCIATA ;  BETA-GLYCOSIDASE ;  PURIFICATION
语种: 英语
WOS记录号: WOS:000305866100007
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/138100
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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作者单位: 1.Chinese Acad Sci, Dalian Inst Chem Phys, Lab Pharmaceut Resource Discovery, Dalian 116023, Peoples R China
2.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China
3.Dalian Med Univ, Dalian, Peoples R China

Recommended Citation:
Zhou, Kun,Luan, Hong-wei,Hu, Ying,et al. Isolation and characterization of a novel alpha-glucosidase with transglycosylation activity from Arthrobacter sp DL001[J]. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,2012,80:48-57.
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