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Isolation and characterization of a novel alpha-glucosidase with transglycosylation activity from Arthrobacter sp DL001
Zhou, Kun1,2; Luan, Hong-wei1; Hu, Ying1; Ge, Guang-bo1; Liu, Xing-bao1; Ma, Xiao-chi3; Hou, Jie3; Wang, Xiu-li1; Yang, Ling1
KeywordArthrobacter Sp. Hydrolysis Transglycosylation Substrate Specificity
Source PublicationJOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
2012-08-01
DOI10.1016/j.molcatb.2012.04.016
Volume80Pages:48-57
Indexed BySCI
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine ; Physical Sciences
WOS SubjectBiochemistry & Molecular Biology ; Chemistry, Physical
WOS Research AreaBiochemistry & Molecular Biology ; Chemistry
WOS KeywordWHITE JADE SNAIL ; OLIGOSACCHARIDE SYNTHESIS ; ENZYMATIC-SYNTHESIS ; SUBSTRATE-SPECIFICITY ; GLYCOSYL HYDROLASES ; APLYSIA-FASCIATA ; BETA-GLYCOSIDASE ; PURIFICATION
AbstractA 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.
Language英语
WOS IDWOS:000305866100007
Citation statistics
Cited Times:1[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/138100
Collection中国科学院大连化学物理研究所
Affiliation1.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
GB/T 7714
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.
APA Zhou, Kun.,Luan, Hong-wei.,Hu, Ying.,Ge, Guang-bo.,Liu, Xing-bao.,...&Yang, Ling.(2012).Isolation and characterization of a novel alpha-glucosidase with transglycosylation activity from Arthrobacter sp DL001.JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,80,48-57.
MLA Zhou, Kun,et al."Isolation and characterization of a novel alpha-glucosidase with transglycosylation activity from Arthrobacter sp DL001".JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 80(2012):48-57.
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