Faculty of Biotechnology and Food Sciences in Nitra Journal of Microbiology, Biotechnology and Food Sciences 1338-5178 no. 4 vol. 4 2015-02-01 2015-02-01 MOLECULAR CLONING AND CHARACTERIZATION OF NOVEL THERMOSTABLE LIPASE FROM SHEWANELLA PUTREFACIENS AND USING ENZYMATIC BIODIESEL PRODUCTION 397 300 EN Fahri Akbas Fahri Akbas Kaifee Arman Kaifee Arman Zeynep Aydin Sinirlioglu Zeynep Aydin Sinirlioglu Deniz Sinirlioglu Deniz Sinirlioglu A novel thermostable lipase from Shewanella putrefaciens was identified, expressed in Escherichia coli, characterized and used in biodiesel production. Enzyme characterization was carried out by enzyme assay, SDS-PAGE and other biochemical reactions. The recombinant lipase was found to have a molecular mass of 29 kDa and exhibited lipase activity when Tween 80 was used as the substrate. The purified enzyme showed maximum activity at pH 5.0 and at 80°C. The recombinant lipase was used for the transesterification of canola oil and waste oil. The enzyme retains 50% of its activity at 90°C for 30 minutes. It is also able to retain 20% of its activity even at 100 °C for 20 minutes. These properties of the obtained new recombinant thermostable lipase make it promising as a biocatalyst for industrial processes.
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