Purification and characterization of an extracellular lipase from a novel strain Penicillium sp. DS-39 (DSM 23773)
| العنوان: | Purification and characterization of an extracellular lipase from a novel strain Penicillium sp. DS-39 (DSM 23773) |
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| المؤلفون: | Gary T. M. Henehan, Dharmendra S. Dheeman, Sanjay Antony-Babu, Jesus M. Frias |
| المساهمون: | DIT, Partenaires INRAE, Interactions Arbres-Microorganismes (IAM), Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL), Newcastle University [Newcastle], DIT ABBEST [PB 03557/2007] |
| المصدر: | Journal of Molecular Catalysis B: Enzymatic Journal of Molecular Catalysis B: Enzymatic, Elsevier, 2011, 72 (3-4), pp.256-262. ⟨10.1016/j.molcatb.2011.06.013⟩ |
| بيانات النشر: | Elsevier BV, 2011. |
| سنة النشر: | 2011 |
| مصطلحات موضوعية: | 0106 biological sciences, ORGANIC-SOLVENTS, ENZYMATIC-SYNTHESIS, Interesterified fat, Characterization, [SDV]Life Sciences [q-bio], Penicillium sp DS-39, EXPANSUM, Bioengineering, 01 natural sciences, Biochemistry, Catalysis, 03 medical and health sciences, chemistry.chemical_compound, 010608 biotechnology, BINDING, Triolein, Lipase, Purification, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Chromatography, STABILITY, biology, Process Chemistry and Technology, Substrate (chemistry), Biodegradation, biology.organism_classification, BACTERIAL LIPASES, Organic solvent-tolerant lipase, chemistry, 13. Climate action, Biodiesel production, CRUDE LIPASE, ACID, Penicillium, biology.protein, Extracellular lipase, ENZYMES, BIOCATALYSTS, Polyunsaturated fatty acid |
| الوصف: | International audience; A newly isolated fungal strain, Penicillium sp. DS-39 (DSM 23773), was found to produce an inducible extracellular lipase when grown in a medium containing 1.0% (v/v) olive oil. Maximum lipase activity was obtained after 120h of incubation at 28 degrees C. The lipase was purified 129-fold with a final specific activity of 308.73 IU/mg. The molecular weight of the homogeneous lipase was 43 kDa as determined by SDS-PAGE. It was optimally active at pH 5.5 and 45 degrees C. The lipase was most active on triolein and exhibited a broad substrate range with a preference for triacylglycerols containing long chain unsaturated fatty acids. It showed no regio-specificity for the ester bond in triolein. It was activated by Ca(2+) and Mn(2+), while significant inhibition was observed with Hg(2+) and Zn(2+). The lipase showed significant stability and activation in the presence of organic solvents with log P >= 2.0. These features render Penicillium sp. DS-39 lipase (PEL) a potential biocatalyst for applications such as biodiesel production, enzymatic restructuring, by interesterification of different oils and fats, and biodegradation of oil spills in the environment. (C) 2011 Elsevier B.V. All rights reserved. |
| تدمد: | 1381-1177 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b619dce24e20407c8498877375ce91de https://doi.org/10.1016/j.molcatb.2011.06.013 |
| حقوق: | CLOSED |
| رقم الأكسشن: | edsair.doi.dedup.....b619dce24e20407c8498877375ce91de |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 13811177 |
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