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Novel thermophilic and thermostable lipolytic enzymes from a Thailand hot spring metagenomic library.

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 degrees C, with optimal activity at 70 degrees C and were stable at 70 degrees C for at least 120 min. Both PLP and Est1 exhibited high V(max) toward p-nitrophenyl butyrate. The enzymes had activity toward both short-chain (C(4) and C(5)) and long chain (C(14) and C(16)) 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 C(10). We suggest that PLP and EstA enzymes are novel and have a; b potential use in industrial applications.

journal_name

J Biotechnol

journal_title

Journal of biotechnology

authors

Tirawongsaroj P,Sriprang R,Harnpicharnchai P,Thongaram T,Champreda V,Tanapongpipat S,Pootanakit K,Eurwilaichitr L

doi

10.1016/j.jbiotec.2007.08.046

subject

Has Abstract

pub_date

2008-01-01 00:00:00

pages

42-9

issue

1

eissn

0168-1656

issn

1873-4863

pii

S0168-1656(07)01575-1

journal_volume

133

pub_type

杂志文章

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