Abstract
•Lipase PS has been immobilized on Accurel in less than 1h with a 70% increase in activity.•Irreversible inhibition with D-pNPP suggested the involvement of the open form of the lipase in the immobilization process.•The new biocatalyst is much more active that the commercial one in hydrolysis and synthetic reactions.•The resolution of (±)-1,3,4-tri-O-benzyl-myo-inositol (1) has been optimized using RSM.•The new biocatalyst is more efficient in kinetic resolution of 1 than Novozym 435.
Lipase from Burkholderia cepacia (PS) has been immobilized on Accurel MP 1000, and their performance has been compared to that of the most widely used immobilized commercial preparation of this enzyme. The maximum loading was 18mgprotein/g support, and its thermal and solvent stability was much higher than that of the commercial. PS preparations were used in hydrolysis of triacetin and methyl mandelate, in the esterification of oleic acid and ethanol and in the kinetic resolution of 1,3,4-tri-O-benzyl-myo-inositol (DL-1) using vinylacetate as activated acyl donor. For all reactions studied, PS on Accurel was more active than PS-IM. The conversion in the kinetic resolution of racemic DL-1 was optimized using response surface methodology. Optimal conditions were determined to be 2.0mg/mL of substrate, temperature of 40°C, 2.0mL of vinyl acetate and without water addition. Under these conditions, maximum loaded Accurel-PS preparation permitted to improve the activity in this kinetic resolution compared to the PS commercial preparation by a 55-fold factor, and compared to Novozym 435 (the most active described in literature for this reaction) by a 23-fold factor. The conversion attained was 49.9%±0.3 of conversion and ee of 99% after 24h. The reusability studies showed maintenance of conversion and ee during eight cycles.