Synthesis of sucrose 6-acetate by immobilized aspergillus Niger lipase imprinted with oleic acid and sorbitol.

Biological and interfacial imprinting both were effective methods to improve the catalytic performance of lipase in organic solvent. Bioimprinting combined with interfacial activation of lipase was investigated for obtaining imprinted lipase with excellent catalytic performance. Enzymatic synthesis of sucrose-6-acetate in organic solvents to test the performance of imprinted lipase immobilized by adsorbing on macroporous resin. Lipase imprinted by substrate analog (oleic acid) then immobilization catalyzed the synthesis of sucrose-6-acetate with a 1.7 times increase in sucrose esterification rate compared to unimprinted immobilized lipase and a selectivity toward sucrose-6-acetate of 91.7 %. The sucrose esterification rate of reaction catalyzed by immobilized lipase was increased to 2.0 times with addition of sorbitol after imprinting by oleic acid. Imprinting by oleic acid and interfacial effect generated by oleic acid with sorbitol both induced zymoprotein secondary structure change that were conducive to enhance catalytic activity and stability of lipase in organic solvent.