ArticleBioMed research international2014
Lipolytic potential of Aspergillus japonicus LAB01: production, partial purification, and characterisation of an extracellular lipase.
Article in BioMed research international, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Synthesis of an enhanced nanobiocatalyst system from Aspergillus niger as single green source.Scientific reports · 2025Article
- Lipolytic activity of carotenogenic yeast isolated from the polish ecosystem.Antonie van Leeuwenhoek · 2025Article
- The use of a non-biological, bridging, antiprotrusio cage in complex revision hip arthroplasty and periacetabular reconstructive oncologic surgery. Is still today a valid option?: A mid/long-term survival and complications' analysis.Archives of orthopaedic and trauma surgery · 2022Article
- Fungal Proteases as Emerging Biocatalysts to Meet the Current Challenges and Recent Developments in Biomedical Therapies: An Updated Review.Journal of fungi (Basel, Switzerland) · 2022Review
- Application and characterization of crude fungal lipases used to degrade fat and oil wastes.Scientific reports · 2021Article
- Article
- Immobilization of Moniliella spathulata R25L270 Lipase on Ionic, Hydrophobic and Covalent Supports: Functional Properties and Hydrolysis of Sardine Oil.Molecules (Basel, Switzerland) · 2017Article
- Macaúba (Acrocomia aculeata) cake from biodiesel processing: a low-cost substrate to produce lipases from Moniliella spathulata R25L270 with potential application in the oleochemical industry.Microbial cell factories · 2015Article
- Isolation and Characterization of a New Thermoalkalophilic Lipase from Soil Bacteria.Iranian journal of pharmaceutical research : IJPR · 2015Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipolytic potential of Aspergillus japonicus LAB01 was investigated by describing the catalytic properties and stability of a secreted extracellular lipase. Enzyme production was considered high under room temperature after 4 days using sunflower oil and a combination of casein with sodium nitrate. Lipase was partially purified by 3.9-fold, resulting in a 44.2% yield using ammonium sulphate precipitation (60%) quantified with Superose 12 HR gel filtration chromatography. The activity of the enzyme was maximised at pH 8.5, and the enzyme demonstrated stability under alkaline conditions. The optimum temperature was found to be 45°C, and the enzyme was stable for up to 100 minutes, with more than 80% of initial activity remaining after incubation at this temperature. Partially purified enzyme showed reasonable stability with triton X-100 and was activated in the presence of organic solvents (toluene, hexane, and methanol). Among the tested ions, only Cu(2+), Ni(2+), and Al(3+) showed inhibitory effects. Substrate specificity of the lipase was higher for C14 among various p-nitrophenyl esters assayed. The KM and V max values of the purified enzyme for p-nitrophenyl palmitate were 0.13 mM and 12.58 umol/(L·min), respectively. These features render a novel biocatalyst for industrial applications.
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