A NEW KIND OF IMMOBILIZED LIPASE INORGANIC SOLVENT AND ITS STRUCTURE MODEL

In this paper, we used Ca-alginate gel beads coated with polyetheneimi ne and glutaraldehyde to adsorb Expansum penicillium lipase. The immob ilized lipase catalyzed esterification of 1-dodecanol with;dodecanoic acid in benzene. The results show that when the concentration of Ca-al ginate, polyetheneimine (PEI) and glutaraldehyde is 1%, Gland 1%, resp ectively, the activity of the immobilized lipase and the amount of ads orbed protein are the highest. The immobilized lipase is better than t he SDS-immobilized lipase. The activity of the immobilized lipase conn ected by glutaraldehyde is higher than the activity of that without gl utaraldehyde. The initial rate of the immobilized lipase and lyophiliz ed lipase powder is 5.9 x 10(2) nmol/min.mgpr and 2.8 X 10(1) nmol/min .mgpr, respectively. After the immobilized lipase catalyzed the esteri fication reaction at 37 degrees C for about 12 hours, 93.3% of 2-dodec anol was converted to eater, but for lyophilized lipase powder, only 1 7.5% converted. Based on all above results, we have presumed and expla ined the structure of this kind of immobilized lipase. (C) 1994 Academ ic Press, Inc.