Publication: Novel thermophilic and thermostable lipolytic enzymes from a Thailand hot spring metagenomic library
Issued Date
2008-01-01
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ISSN
01681656
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2-s2.0-36249002945
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Mahidol University
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SCOPUS
Bibliographic Citation
Journal of Biotechnology. Vol.133, No.1 (2008), 42-49
Suggested Citation
Pacawadee Tirawongsaroj, Rutchadaporn Sriprang, Piyanun Harnpicharnchai, Taksawan Thongaram, Verawat Champreda, Sutipa Tanapongpipat, Kusol Pootanakit, Lily Eurwilaichitr Novel thermophilic and thermostable lipolytic enzymes from a Thailand hot spring metagenomic library. Journal of Biotechnology. Vol.133, No.1 (2008), 42-49. doi:10.1016/j.jbiotec.2007.08.046 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/18994
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Title
Novel thermophilic and thermostable lipolytic enzymes from a Thailand hot spring metagenomic library
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Abstract
Functional screening for lipolytic enzymes from a metagenomic library (origin: Jae Sawn hot spring, Thailand) resulted in isolation of a novel patatin-like phospholipase (PLP) and an esterase (Est1). PLP contained four conserved domains similar to other patatin-like proteins with lipid acyl hydrolase activity. Likewise, sequence alignment analysis revealed that Est1 can be classified as a family V bacterial lipolytic enzyme. Both PLP and Est1 were expressed heterologously as soluble proteins in E. coli and exhibited more than 50% of their maximal activities at alkaline pH, of 7-9 and 8-10, respectively. In addition, both enzymes retained more than 50% of maximal activity in the temperature range of 50-75 °C, with optimal activity at 70 °C and were stable at 70 °C for at least 120 min. Both PLP and Est1 exhibited high Vmaxtoward p-nitrophenyl butyrate. The enzymes had activity toward both short-chain (C4and C5) and long chain (C14and C16) fatty acid esters. The isolated enzymes, are therefore, different from other known patatin-like phospholipases and esterases, which usually show no activity for substrates longer than C10. We suggest that PLP and EstA enzymes are novel and have a; b potential use in industrial applications. © 2007 Elsevier B.V. All rights reserved.