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1392/9/14، جلد ۵، شماره ۴، صفحات -
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| عنوان فارسی |
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| چکیده فارسی مقاله |
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| کلیدواژههای فارسی مقاله |
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| عنوان انگلیسی |
Characterization of a lipase from a newly isolated Pseudomonas sp. |
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| چکیده انگلیسی مقاله |
Background and Objectives: Lipases are valuable biocatalysts which are widely used in the detergent, food, dairy and pharmaceutical industries. The aims of the present study included the isolation of a lipase-producer from industrial zones and the partial characterization of the enzyme. Materials and Methods: A number of bacteria were isolated from sites related to the oil industries. An isolate forming a halo zone in a selective medium (TW agar) was then selected and grown on a medium suitable for the production of lipase. The isolate was subsequently identified by the 16S rRNA sequencing method, and its enzyme activity was measured by a spectrophotometer using p NPP as a substrate. Results: The selected isolate was identified by the molecular method as Pseudomonas sp. Its extracellular lipase activity was 41.5 ± 1.4 U/ml, and the high affinity of this enzyme for the substrate was indicated by the kinetic parameters of Km and Vm, which were estimated by the the Lineweaver-Burk plot as 0.77 mM and 49.5 U/ml, respectively. Activation energy of lipase calculated from the Arrhenius plot was found to be 20.78 kJ/mol, and a temperature coefficient (Q10) of 4.39 indicated the high catalytic activity of the enzyme and the temperature dependence of the enzymatic reaction. Conclusion: The results demonstrated that the indigenous isolate could have potential applications in many relevant industries. Keywords: Lipase, Pseudomonas , Kinetic constants, Thermodynamic parameters |
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| کلیدواژههای انگلیسی مقاله |
Keywords: Lipase, Pseudomonas , Kinetic constants, Thermodynamic parameters |
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| نویسندگان مقاله |
51597---51598---51599---51600--- |
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| نشانی اینترنتی |
http://ijm.tums.ac.ir/index.php/ijm/article/viewArticle/512 |
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| زبان مقاله منتشر شده |
en |
| موضوعات مقاله منتشر شده |
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| نوع مقاله منتشر شده |
Articles |
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