Development of novel immobilization supports of lipase for reactions in organic media;seed polymerization of amphiphilic 2-[rho-(1,1,3,3-tetramethyl-butyl)phenoxy-polyethoxy]ethyl methacrylate macromonomers

摘要

To develop a novel support of enzymes for use in the enzymatic reactions in nonaqueous solutions,amphiphilic polymer particles which have 2-[rho-(1,1,3,3-tetramethyl-butyl)phenoxy-polyethoxy]ethyl groups (tert-C_8PHIE_n groups:n is the mean number of the ethylene oxide units) were synthesized by the seed copolymerization of styrene,divinylbenzene,and 2-[rho-(1,1,3,3,-tetramethyl-butyl)phenoxy-polyethoxy]ethyl methacrylate (MAX-n).In seed polymerization,the mean number n of the tert-C_8PHIE_n group did not affect the monomer conversins and the amunt of MAX-n introduced intothe particles.Using Rhizopus delemar lipase as a modelenzyme,the enzyme immobilization on the amphiphilic polymer particles was investigated.The specific hydrolytic activity of the immobilized lipase prepared with the amphiphilic polymer particles was higher than that of native lipase.When the amphiphilic particles synthesized using MAX-15.9 were used to immobilize lipse,the amount oflipase immobilized and the hydrolytic activity and the transesterification activity of the immobilized lipase were the highest.However,the organic solvent stability of the immobilized lipase prepared with the amphiphilic particles syntesize dusing MAX-4.39 was the highest.