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Enhanced Thermostability of Silica-immobilized Lipase from Bacillus coagulans BTS-3 and Synthesis of Ethyl Propionate

Kumar, Satyendra and Pahujani, Shweta and Ola, R. P. and Ola, R. P. and Kanwar, S. S. and Kanwar, S. S. and Gupta, Reena (2006) Enhanced Thermostability of Silica-immobilized Lipase from Bacillus coagulans BTS-3 and Synthesis of Ethyl Propionate. Acta Microbiologica et Immunologica Hungarica, 53 (2). pp. 219-231. ISSN 1217-8950

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Abstract

A lipase from the thermophilic isolate Bacillus coagulans BTS-3 was produced and purified. The enzyme was purified 40-fold to homogeneity by ammonium sulfate precipitation and DEAE-Sepharose column chromatography. Its molecular weight was 31 kDa on SDS-PAGE. The purified lipase was immobilized on silica and its binding efficiency was found to be 60%. The enzyme took 60 min to bind maximally onto the support. The pH and temperature optima of immobilized lipase were same as those of the free enzyme, i.e. 8.5 and 55ºC, respectively.  The immobilized enzyme had shown marked thermostability on the elevated temperatures of 55, 60, 65 and 70ºC. The immobilized enzyme was reused for eigth cycles as it retained almost 80% of its activity. The catalytic activity of immobilized enzyme was enhanced in n-hexane and ethanol. The immobilized enzyme when used for esterification of ethanol and propionic acid showed 96% conversion in n-hexane in 12 h at 55ºC.

Item Type: Article
Subjects: Q Science / természettudomány > QR Microbiology / mikrobiológia
Depositing User: xFruzsina xPataki
Date Deposited: 12 Sep 2017 15:42
Last Modified: 12 Sep 2017 15:42
URI: http://real.mtak.hu/id/eprint/62320

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