ArticleScientific reports2020
Gene cloning, heterologous expression, and partial characterization of a novel cold-adapted subfamily I.3 lipase from Pseudomonas fluorescence KE38.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- Recombinant thermotolerant alkaline lipase from Lysinibacillus fusiformis for detergent and hard (Ras) cheese applications: cloning, expression, molecular docking, and characterization.Microbial cell factories · 2026Article
- Production, purification, and characterization of cold-active lipase from the psychrotroph Pseudomonas sp. A6.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Article
- Characterization of a New Thermostable and Organic Solution-Tolerant Lipase fromInternational journal of molecular sciences · 2023Article
- Metagenomic discovery of lipases with predicted structural similarity to Candida antarctica lipase B.PloS one · 2023Article
- Characterization ofMicrobiology spectrum · 2022Article
- Industrial applications of cold-adapted enzymes: challenges, innovations and future perspective.3 Biotech · 2021Review
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
A novel cold-active true lipase from Pseudomonas sp. KE38 was cloned, sequencing and expressed in E. coli by degenerate PCR and genome walking technique. The open reading frame of the cloned gene encoded a polypeptide chain of 617 amino acids with a confirmed molecular weight of 64 kD. Phylogenetic analysis of the deduced amino acid sequence of the lipase indicated that it had high similarity with lipases of subfamily Ι.3 of bacterial lipases. Recombinant lipase was purified in denatured form as inclusion bodies, which were then renatured by urea followed by dialysis. Lipase activity was determined titrimetrically using olive oil as substrate. The enzyme showed optimal activity at 25 °C, pH 8.5 and was highly stable in the presence of various metal ions and organic solvents. Low optimal temperature and high activity in the presence of methanol and ethanol make this lipase a potential candidate for transesterification reactions and biodiesel production.
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