STABILITY OF LIPASE ENZYME IN THE SYNTHESIS OF MONOACYLGLYCEROL A DERIVATIVE VEGETABLE OIL PRODUCT

Prima Luna

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 lipase
as 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 lipase
immobilized 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.

Keywords


Enzyme stability, Re-use immobilized enzyme, Monoasilgliserol, Yield, Half-life Enzyme

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DOI: http://dx.doi.org/10.14203/widyariset.15.3.2012.673–682

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