Polyacrylic resins with immobilized

Polyacrylic resins were employed to study how immobilization resin particle size influences Candida antarctica Lipase B (CALB) loading, fraction of active sites, and catalytic properties for polyester synthesis. CALB adsorbed more rapidly on smaller beads. Saturation occurred in less than 30 seconds and 48 h for beads with diameters 35 and 560-710 pm, respectively. Infrared microspectroscopy showed that CALB forms protein loading fronts for resins with particle sizes 560-710 and 120 pm while CALB appears evenly distributed throughout 35 pm resins. The fraction of active CALB molecules adsorbed onto resins not influenced by particle size was less than 50 %. At about 5% w/w CALB loading, decrease in the immobilization support diameter from 560-710 to 120,75 and 35 pm increased conversion of s-CL to polyester (20 to 36, 42 and 61%, respectively, at 80 min). Similar trends were observed for condensation polymerizations of 1,8-octanediol and adipic acid. 

Enzymatic polymerization has emerged in the last few decades as a field of considerable interest and commercial promises. It proceeds with high regio-, enantio-, and chemos-electivity under relatively mild conditions. So far, enzymes have been used to synthesize polyesters, polysaccharides, polycarbonates, polyphenols, polyanilines, vinyl polymers, and poly(amino acid)s. Namely, the lipase B of Candida antarctica (Cal-B, a serine hydrolase) immobilized on polyacrylic resin (Novozyme 435) has proven to be a very versatile catalyst in terms of reaction conditions and acceptance of various substrates. For example, this enzyme has been successfully used to synthesize polyesters. ° However, little has been reported so far on the synthesis of polyamides catalyzed by enzymes. " ... 

The immobilized thermolysin was prepared by adsorption of the enzyme onto the supports, polyacrylic ester resins (AmberUte series) and pore glass particles (CPG series), followed by crosslinking with glutaraldehyde in aqueous solutions. The activity of the immobilized enzyme was assayed by measuring the initial synthetic rate of fV-(benzyloxycarbonyl)-L-phenylalanyl-L-phynylalanine methyl ester in the biphasic reaction system. 

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