A new cold-active and alkaline pectate lyase from Antarctic bacterium with high catalytic efficiency
作者: Yumeng TangPan WuSijing JiangJonathan Nimal SelvarajShihui YangGuimin Zhang
作者单位: 1State Key Laboratory of Biocatalysis and Enzyme Engineering, Hubei Collaborative Innovation Center for Green Transformation of Bio-Resources, School of Life Sciences, Hubei University
刊名: Applied Microbiology and Biotechnology, 2019, Vol.103 (13), pp.5231-5241
来源数据库: Springer Nature Journal
DOI: 10.1007/s00253-019-09803-1
关键词: Pectate lyaseEnzymatic assayCold-activeSpecific activityMutation analysis
英文摘要: Abstract(#br)Cold-active enzymes have become attractive biocatalysts in biotechnological applications for their ability to retain high catalytic activity below 30 °C, which allows energy reduction and cost saving. Here, a 1041 bp gene pel1 encoding a 34.7 KDa pectate lyase was cloned from a facultatively psychrophilic Antarctic bacterium Massilia eurypsychrophila and heterologously expressed in Escherichia coli . PEL1 presented the highest 66% identity to the reported mesophilic pectate lyase PL Xc . The purified PEL1 exhibits the optimum temperature and pH of 30 °C and 10 toward polygalacturonic acid, respectively. PEL1 is a cold-active enzyme that can retain 60% and 25% relative activity at 10 °C and 0 °C, respectively, while it loses most of activity at 40 °C for 10 min. PEL1 has the...
全文获取路径: Springer Nature  (合作)
影响因子:3.689 (2012)