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Production, Purification and Immobilization of Extracellular Lipases from Thermophilic Bacillus subtilis XRF11 and Bacillus licheniformis XRF12 for Production of Alkyl Esters

Gohel H R1,2, Ghosh S K1, and Bragazna V J1,2
1. Loyola Centre for R & D (LCRD), Xavier Research Foundation, St. Xavier’s College Campus, Navrangpura Ahmedabad-380 009, Gujarat
2. St. Xavier's College, Navrangpura, Ahmedabad-380009, Gujarat
Abstract—Lipase is known for production of alkyl esters by enzymatic transesterification since long. Thermophilic lipases have great stability at higher temperature with faster rate of reaction and immobilization of these enzymes allows repetitive use of them. In this study, thermophilic lipases were produced, purified and immobilized to be used for transesterification. Purification was carried out by salting out and alcohol precipitation followed by affinity chromatography. Sodium alginate was preferred for immobilization of lipase over varieties of other methods. pNPP assay was used for determination of enzymatic activity. As a result of this study, it was found that 87.0% of peanut oil was converted into ethyl esters after 10 h of reaction at 55°C. Results of repetitive use of immobilized enzymes showed that after 18 cycles of reaction the production of ethyl esters decreased drastically. Presence of ethyl esters was confirmed by gas chromatographic analysis where it showed presence of C16:0, C18:0, C18:1, C18:3 and C22:0 fatty acids. 

Index Terms—thermophilic lipase, transesterification, immobilization

Cite: Gohel H R, Ghosh S K, and Bragazna V J, "Production, Purification and Immobilization of Extracellular Lipases from Thermophilic Bacillus subtilis XRF11 and Bacillus licheniformis XRF12 for Production of Alkyl Esters," International Journal of Life Sciences Biotechnology and Pharma Research, Vol. 2, No. 3, pp. 278-286, July 2013.
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