ArticleBrazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]2012
Screening and characterization of a novel alkaline lipase from Acinetobacter calcoaceticus 1-7 Isolated from bohai bay in china for detergent formulation.
Article in Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 23 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
- Article
- Metagenomic views on taxonomic and functional profiles of the Himalayan Tsomgo cold lake and unveiling its deterzome potential.Current genetics · 2022Article
- A jacalin-related lectin domain-containing lipase from chestnut (Current research in food science · 2022Article
- Production and purification of an alkaline lipase from3 Biotech · 2018Article
- Article
- Utilization of acid pre-treated coconut dregs as a substrate for production of detergent compatible lipase by Bacillus stratosphericus.AMB Express · 2017Article
- QSAR study and the hydrolysis activity prediction of three alkaline lipases from different lipase-producing microorganisms.Lipids in health and disease · 2012Article
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
A novel alkaline lipase-producing strain 1-7 identified as Acinetobacter calcoaceticus was isolated from soil samples collected from Bohai Bay, China, using an olive oil alkaline plate, which contained olive oil as the sole carbon source. The lipase from strain 1-7 showed the maximum activity at pH 9.0 under 40 °C. One interesting feature of this enzyme is that it exhibits lipase activity over a broad range of temperatures and good stability. It is also stable at a broad range of pHs from 4.0 to 10.0 for 24 h. Its catalytic activity was highly enhanced in the presence of Ca(2+), Mg(2+) and K(+), but partially inhibited by Cu(2+), Al(3+), Fe(3+), Ba(2+)and Zn(2+). The fact that it displays marked stability and activity in the presence of TritonX-100, Tween-20, Tween-80, SDS, Hydrogen peroxide, Sodium perborate, Sodium hypochlorite, Sodium citrate, Sodium taurocholate, Glycerine and NaCl suggests that this lipase is suitable as an additive in detergent formulations.
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