ArticleInternational journal of molecular sciences2010
Purification and characterization of organic solvent and detergent tolerant lipase from thermotolerant Bacillus sp. RN2.
Article in International journal of molecular sciences, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 41 citations in OpenAlex.
- A CALB-like Cold-Active Lipolytic Enzyme fromMarine drugs · 2025Article
- A lipase from Lacticaseibacillus rhamnosus IDCC 3201 with thermostability and pH resistance for use as a detergent additive.Applied microbiology and biotechnology · 2024Article
- Characterization of a novel subfamily 1.4 lipase from Bacillus licheniformis IBRL-CHS2: Cloning and expression optimization.PloS one · 2024Article
- Molecular study on recombinant cold-adapted, detergent- and alkali stable esterase (EstRag) from Lysinibacillus sp.: a member of family VI.World journal of microbiology & biotechnology · 2022Article
- Identification of a Novel Lipase with AHSMG Pentapeptide in Hypocreales and Glomerellales Filamentous Fungi.International journal of molecular sciences · 2022Article
- Production optimization, characterization, and covalent immobilization of a thermophilic Serratia rubidaea lipase isolated from an Algerian oil waste.Molecular biology reports · 2019Article
- Lipase and biosurfactant from Ochrobactrum intermedium strain MZV101 isolated by washing powder for detergent application.Lipids in health and disease · 2017Article
- Article
- Production of a solvent, detergent, and thermotolerant lipase by a newly isolated Acinetobacter sp. in submerged and solid-state fermentations.Journal of biomedicine & biotechnology · 2011Article
- Screening, purification, and characterization of an extracellular lipase from Aureobasidium pullulans isolated from stuffed buns steamers.Journal of Zhejiang University. Science. BArticle
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aim of this study was to characterize the organic solvent and detergent tolerant properties of recombinant lipase isolated from thermotolerant Bacillus sp. RN2 (Lip-SBRN2). The isolation of the lipase-coding gene was achieved by the use of inverse and direct PCR. The complete DNA sequencing of the gene revealed that the lip-SBRN2 gene contains 576 nucleotides which corresponded to 192 deduced amino acids. The purified enzyme was homogeneous with the estimated molecular mass of 19 kDa as determined by SDS-PAGE and gel filtration. The Lip-SBRN2 was stable in a pH range of 9-11 and temperature range of 45-60 °C. The enzyme was a non metallo-monomeric protein and was active against pNP-caprylate (C8) and pNP-laurate (C12) and coconut oil. The Lip-SBRN2 exhibited a high level of activity in the presence of 108% benzene, 102.4% diethylether and 112% SDS. It is anticipated that the organic solvent and detergent tolerant enzyme secreted by Bacillus sp. RN2 will be applicable as catalysts for reaction in the presence of organic solvents and detergents.
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