Abstract
Lipase from Rhizopus sp. was immobilized in the polymer matrix prepared by polymerization of n -vinyl-2-pyrrolidone, 2-hydroxymethacrylate or n-isopropylacrylamide. The esterification of oleic acid and glycerol was carried out at 310 K by using the immobilized lipase or free lipase. The selectivity of monoolein was dependent on the hydrohobicity of the polymer matrix immobilizing lipase. The hydrophilic polymer provided a high selectivity for monoolein in the esterification. It was found that controlling the hydrophobicity of the enzyme-immobilized matrix allowed the final constitution of the equilibrium state to be shifted.
Original language | English |
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Pages (from-to) | 565-567 |
Number of pages | 3 |
Journal | kagaku kogaku ronbunshu |
Volume | 29 |
Issue number | 4 |
DOIs | |
Publication status | Published - Jul 2003 |
All Science Journal Classification (ASJC) codes
- Chemistry(all)
- Chemical Engineering(all)