Novel thermophilic and thermostable lipolytic enzymes from a Thailand hot spring metagenomic library
| Autor: | Kusol Pootanakit, Pacawadee Tirawongsaroj, Rutchadaporn Sriprang, Verawat Champreda, Sutipa Tanapongpipat, Piyanun Harnpicharnchai, Lily Eurwilaichitr, Taksawan Thongaram |
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| Rok vydání: | 2007 |
| Předmět: |
Lipolysis
Molecular Sequence Data Bioengineering Sequence alignment Phospholipase Biology Applied Microbiology and Biotechnology Esterase Hot Springs Enzyme activator Species Specificity Peptide Library Enzyme Stability chemistry.chemical_classification Base Sequence Thermophile Esterases Temperature Fatty acid Chromosome Mapping General Medicine Thailand Lipids Enzyme Activation Enzyme Biochemistry chemistry Patatin-like phospholipase Phospholipases Biotechnology |
| Zdroj: | Journal of biotechnology. 133(1) |
| ISSN: | 0168-1656 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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