ArticleMolecular biology reports2012
Characterization of a thermostable lipase showing loss of secondary structure at ambient temperature.
Article in Molecular biology reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 38 citations in OpenAlex.
- Genetically engineered lipases: advances in expression and upscaling for industrial applications.Archives of microbiology · 2026Review
- Versatile biocatalyst: lipase fromFrontiers in bioengineering and biotechnology · 2025Article
- Molecular insights and functional analysis of isocitrate dehydrogenase in two gram-negative pathogenic bacteria.World journal of microbiology & biotechnology · 2024Article
- Thermostable lipases and their dynamics of improved enzymatic properties.Applied microbiology and biotechnology · 2021Review
- Recombinant production and characterization of a novel esterase from a hypersaline lake, Acıgöl, by metagenomic approach.Extremophiles : life under extreme conditions · 2019Article
- Article
- Metagenomics of an Alkaline Hot Spring in Galicia (Spain): Microbial Diversity Analysis and Screening for Novel Lipolytic Enzymes.Frontiers in microbiology · 2015Article
- First co-expression of a lipase and its specific foldase obtained by metagenomics.Microbial cell factories · 2014Article
- Biochemical characterization of a carboxylesterase from the archaeon Pyrobaculum sp. 1860 and a rational explanation of its substrate specificity and thermostability.International journal of molecular sciences · 2014Article
- Insights into controlling role of substitution mutation, E315G on thermostability of a lipase cloned from metagenome of hot spring soil.3 Biotech · 2014Article
- New extremophilic lipases and esterases from metagenomics.Current protein & peptide science · 2014Review
- Identification of a novel fumarase C from Streptomyces lividans TK54 as a good candidate for L-malate production.Molecular biology reports · 2014Article
- Hot spring metagenomics.Life (Basel, Switzerland) · 2013Review
- Characterization and evolution of a metagenome-derived lipase towards enhanced enzyme activity and thermostability.Molecular and cellular biochemistry · 2013Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A gene encoding extracellular lipase was cloned and characterized from metagenomic DNA extracted from hot spring soil. The recombinant gene was expressed in E. coli and expressed protein was purified to homogeneity using hydrophobic interactions chromatography. The mature polypeptide consists of 388 amino acids with apparent molecular weight of 43 kDa. The enzyme displayed maximum activity at 50 °C and pH 9.0. It showed thermal stability up to 40 °C without any loss of enzyme activity. Nearly 80% enzyme activity was retained at 50 °C even after incubation for 75 min. However above 50 °C the enzyme displayed thermal instability. The half life of the enzyme was determined to be 5 min at 60 °C. Interestingly the CD spectroscopic study carried out in the temperature range of 25-95 °C revealed distortion in solution structure above 35 °C. However the intrinsic tryptophan fluorescence spectroscopic study revealed that even with the loss of secondary structure at 35 °C and above the tertiary structure was retained. With p-nitrophenyl laurate as a substrate, the enzyme exhibited a K ( m ), V ( max ) and K ( cat ) of 0.73 ± 0.18 μM, 239 ± 16 μmol/ml/min and 569 s(-1) respectively. Enzyme activity was strongly inhibited by CuCl(2), HgCl(2) and DEPC but not by PMSF, eserine and SDS. The protein retained significant activity (~70%) with Triton X-100. The enzyme displayed 100% activity in presence of 30% n-Hexane and acetone.
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