Isolation and characterization of a novel alpha-glucosidase with transglycosylation activity from Arthrobacter sp DL001

	Isolation and characterization of a novel alpha-glucosidase with transglycosylation activity from Arthrobacter sp DL001
	Zhou, Kun 1,2; Luan, Hong-wei 1; Hu, Ying 1; Ge, Guang-bo 1; Liu, Xing-bao 1; Ma, Xiao-chi 3; Hou, Jie 3; Wang, Xiu-li 1; Yang, Ling 1
刊名	journal of molecular catalysis b-enzymatic
	2012-08-01
卷号	80 页码:48-57
关键词	Arthrobacter sp. Hydrolysis Transglycosylation Substrate specificity
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.
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
关键词[WOS]	white jade snail ; oligosaccharide synthesis ; enzymatic-synthesis ; substrate-specificity ; glycosyl hydrolases ; aplysia-fasciata ; beta-glycosidase ; purification
收录类别	SCI
语种	英语
WOS记录号	WOS:000305866100007
公开日期	2015-11-10
内容类型	期刊论文
源URL	[http://159.226.238.44/handle/321008/138100]
专题	大连化学物理研究所_中国科学院大连化学物理研究所
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
推荐引用方式 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.