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Lipase(triacylglycerol ester hydrolase, E.C.3.1.1.3) from Candida rugosa was immobilized on hydrophobic microporous polypropylene supports by physical adsorption. The immobilized enzyme catalysts were employed for the selective hydrolysis and esterification of borage oil and evening primrose oil to contrate their GLA contents in glycerides. The Michaelis constant Km and the maximum rate constant Vm for the lipolysis of borage oil by Candida rugosa are 0.107 M and 393.89 U/mg protein, respectively. Product inhibition with a dissociation constant of the enzyme-product complex Ki=25 mM was confirmed.
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