ArticleWorld journal of microbiology & biotechnology2015
Molecular cloning and characterization of a thermostable lipase from deep-sea thermophile Geobacillus sp. EPT9.
Article in World journal of microbiology & biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Perspectives on the microorganism of extreme environments and their applications.Current research in microbial sciences · 2022Review
- Production and Characterization of Cross-Linked Aggregates ofMolecules (Basel, Switzerland) · 2021Article
- Thermostable lipases and their dynamics of improved enzymatic properties.Applied microbiology and biotechnology · 2021Review
- Identification and Heterologous Production of a Lipase from Geobacillus kaustophilus DSM 7263The protein journal · 2021Article
- Identification and Characterization of a Novel Thermostable GDSL-Type Lipase fromJournal of microbiology and biotechnology · 2021Article
- New engineered Geobacillus lipase GD-95RM for industry focusing on the cleaner production of fatty esters and household washing product formulations.World journal of microbiology & biotechnology · 2020Article
- Properties and Applications of Extremozymes from Deep-Sea Extremophilic Microorganisms: A Mini Review.Marine drugs · 2019Review
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Authors and funding
6 authors.
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Abstract
A gene (1,254 bp) encoding a lipase was identified from a deep-sea hydrothermal field thermophile Geobacillus sp. EPT9. The open reading frame of this gene encoded 417 amino acid residues. The gene was cloned, overexpressed in Escherichia coli, and the target protein was purified to homogeneity. The purified recombinant enzyme presented a molecular mass of 44.8 kDa. When p-nitrophenyl palmitate was used as a substrate, the recombinant lipase was optimally active at 55 °C and pH 8.5. The recombinant enzyme retained 44 % residual activity after incubation at 80 °C for 1 h, which indicated that Geobacillus sp. EPT9 lipase was thermostable. Homology modeling of strain EPT9 lipase was developed with the lipase from Bacillus sp. L2 as a template. The core structure exhibits an α/β-hydrolase fold and the typical catalytic triad might consist of Ser142, Asp346, and His387. The enzymatic activity of EPT9 lipase was inhibited by addition of phenylmethylsulfonyl fluoride, indicating that it contains serine residue, which plays an important role in the catalytic mechanism.
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