Effects of organic solvents on immobilized lipase in pectin microspheres

COSTAS LUCIANA; BOSIO VALERIA E.; PANDEY ASHOK; CASTRO, GUILLERMO R

APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY

Springer

Año: 2008 vol. 151 p. 578 - 586

0273-2289

Lipase from Brevibacillus agri 52 was found stable up to 90% diethylenglycol (DEG), glycerol (GLY),and 1,2 propanediol (1,2 PRO) at 37ºC for one hour, and the stability was reduced only approximately20% after twelve hours incubation, but in 40% dimethylsulfoxide (DMSO) lipase activity was stableonly for one hour. Inhibition of the biocatalysts with dimethylformamide (DMF) was detected at 20%solvent concentration. In water immiscible systems the stability of lipase in n-hexane, n-tetradecane andn-heptane resembles the water activity, but in presence of isobutanol, 1-hexanol and butylbutirate thestability was significatively reduced.Lipase 52 precipitates in presence of 50% acetone or ethanol/water mixtures, but enzymatic activity waspartially recovered by adding 20% GLY, DEG, 1,2 PRO or DMSO to the reaction mixture. Also, byincreasing DEG in 70% DMF/DEG mixtures, the lipase activity was protected.Encapsulation of lipase in pectin gels cross-linked with calcium ions brings three to four times moreenzymatic activity in 70% water miscible organic solvents compared to aqueous systems.