中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Characterization and high-level expression of a metagenome-derived alkaline pectate lyase in recombinant Escherichia coli

文献类型:期刊论文

作者Wang, Huilin1,2; Li, Xiaoman1,2; Ma, Yanhe1,2,3; Song, Jiangning1,2,4,5
刊名PROCESS BIOCHEMISTRY
出版日期2014
卷号49期号:1页码:69-76
关键词Metagenomic-derived Alkaline pectate lyase Recombinant Escherichia coli Characterization Overproduction
英文摘要Alkaline pectate lyases (PLs) play an important role in mild and eco-friendly bioscouring pretreatment processes in the textile industry. However, to date, only a few PLs can be applied in industrial-scale production, and many of them exhibit high production cost, low activity, and/or do not meet the treatment requirements. In this study, an alkaline PL gene was cloned from the metagenomic DNA of alkaline environment soils. The gene pelB consisted of 1263 nucleotides and encoded a mature protein (PelB) of 399 amino acids, which was expressed in Escherichia coli. The maximum catalytic activity of the enzyme exhibited a bimodal distribution at pH 8.1 and 9.8 and an optimal temperature of 55 degrees C. The K-m and V-max values of PelB were 1.78 g/L and 1084.8 mu mol/(L min) at 45 degrees C, respectively. Substrate specificity analysis demonstrated the high cleavage capability of PelB on a broad range of substrates of natural methylated pectin. Based on the degradation products, PelB was considered to be an endo-acting lyase. Using high-cell-density cultivation in 7-L bioreactor, the highest PL activity (1816.2 U/mL) was achieved. Thus, the recombinant PelB, with promising properties for use in bioscouring in the textile pretreatment process, should be a potential enzyme for industrial applications. (C) 2013 Elsevier Ltd, All rights reserved.
WOS标题词Science & Technology ; Life Sciences & Biomedicine ; Technology
类目[WOS]Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology ; Engineering, Chemical
研究领域[WOS]Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology ; Engineering
关键词[WOS]CELL-DENSITY CULTURE ; BACILLUS-SUBTILIS ; POLYGALACTURONATE LYASE ; INDUSTRIAL APPLICATIONS ; SEQUENCE ALIGNMENT ; METHYLATED PECTIN ; BETA-ELIMINATION ; HIGH-THROUGHPUT ; PURIFICATION ; ENZYMES
收录类别SCI
语种英语
WOS记录号WOS:000331156100010
公开日期2014-11-23
源URL[http://124.16.173.210/handle/311007/430]  
专题天津工业生物技术研究所_结构生物信息学和整合系统生物学实验室 宋江宁_期刊论文
作者单位1.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Natl Engn Lab Ind Enzymes, Tianjin 300308, Peoples R China
2.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Key Lab Syst Microbial Biotechnol, Tianjin 300308, Peoples R China
3.Chinese Acad Sci, Inst Microbiol, State Key Lab Microbial Resources, Beijing 100101, Peoples R China
4.Monash Univ, Fac Med, Dept Biochem & Mol Biol, Melbourne, Vic 3800, Australia
5.Monash Univ, Fac Med, ARC Ctr Excellence Struct & Funct Microbial Gen, Melbourne, Vic 3800, Australia
推荐引用方式
GB/T 7714
Wang, Huilin,Li, Xiaoman,Ma, Yanhe,et al. Characterization and high-level expression of a metagenome-derived alkaline pectate lyase in recombinant Escherichia coli[J]. PROCESS BIOCHEMISTRY,2014,49(1):69-76.
APA Wang, Huilin,Li, Xiaoman,Ma, Yanhe,&Song, Jiangning.(2014).Characterization and high-level expression of a metagenome-derived alkaline pectate lyase in recombinant Escherichia coli.PROCESS BIOCHEMISTRY,49(1),69-76.
MLA Wang, Huilin,et al."Characterization and high-level expression of a metagenome-derived alkaline pectate lyase in recombinant Escherichia coli".PROCESS BIOCHEMISTRY 49.1(2014):69-76.

入库方式: OAI收割

来源:天津工业生物技术研究所

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