A thermostable esterase from Thermoanaerobacter tengcongensis opening up a new推荐.pdfVIP

Biochimica et Biophysica Acta 1814 (2011) 1695–1702 Contents lists available at SciVerse ScienceDirect Biochimica et Biophysica Acta journal homepage: /locate/bbapap A thermostable esterase from Thermoanaerobacter tengcongensis opening up a new family of bacterial lipolytic enzymes Lang Rao a,b, Yanfen Xue a, Cheng Zhou a,b, Jin Tao c, Gang Li a,b, Jian R. Lu d,⁎, Yanhe Ma a,⁎ a State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China b The Graduate School, Chinese Academy of Sciences, Beijing 100049, China c Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, Changchun 130023, Jilin, China d Biological Physics Laboratory, School of Physics and Astronomy, the University of Manchester, Schuster Building, Oxford Road, Manchester M13 9PL, United Kingdom a r t i c l e i n f o a b s t r a c t Article history: An unidentified α/β hydrolase gene lipA3 from thermostable eubacterium species Thermoanaerobacter teng- Received 8 April 2011 congensis MB4 was cloned and heterologously expressed by Escherichia coli BL21(DE3)pLysS. The purified re- Received in revised form 22 August 2011 combinant enzyme EstA3 turned out to be a monomeric thermostable esterase with optimal activity at 70 °C Accepted 24 August 2011 and pH 9.5. The enzyme showed lipolytic activity towards a wide range of ester substrates including p-nitro- Available online 31 August 2011 phenyl esters and triacylglycerid