STABILITY OF LIPASE ENZYME IN THE SYNTHESIS OF MONOACYLGLYCEROL A DERIVATIVE VEGETABLE OIL PRODUCT
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Abstract
Nowadays, the biotechnologically production of products using enzymes has received great consideration because the trend towards ecologically acceptable processes or environmentally safer. The employment of lipaseas a biocatalyst in the synthesis of monoacylgliserol (MAG) allows mild reaction conditions and easy recovery of glycerol without purification or chemical waste production. Biocatalyst in this study was commercially immobilized lipase from Candida antarctica. Aim of this study was to investigate the stability of commercially lipaseimmobilized enzyme in the synthesis of MAG, to understand the correlation between parameters, and to estimate the half-life of enzyme activity. Immobilized lipase enzyme was employed in the synthesis of MAG, respectively. The re-use of this enzyme has given importance information for oil and fat’s biotechnological industries. Based on the research results, the composition of MAG for 10 times reaction, respectively, decreased 7%, while the MAG’s yield and the number of products decreased 16%. The correlation between the composition of the MAG and the yield were strong and in the same direction with r = 0,812. The half-life of immobilized lipase enzyme activity in this study was estimated 30 times in the MAG synthesis‘s cycle due to the composition of MAGs.
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References
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