Development of Biocatalysts Based on <i>Candida Antarctica B</i> Lipase Immobilized Onto Crosslinked Porous Polymers Containing Varied Monomeric Compositions

ABSTRACT Crosslinked polymer particles can be used successfully as support for enzyme immobilization. For this reason, the relationship between the particle morphology and immobilization parameters is investigated in the present manuscript. Particularly, this study focuses on the preparation of biocatalysts using lipase from Candida antarctica B (Cal‐B) and crosslinked polymers made from divinylbenzene (DVB) and ethylene glycol dimethacrylate (EGDMA). Several monomers were utilized in this process, including methyl methacrylate (MMA), styrene (Sty), glycidyl methacrylate (GMA), methacrylic acid (MA), vinylbenzyl chloride (VBC), and 2‐vinylpyridine (Vpy). Many of these monomers were used to synthesize biocatalysts for the first time. The highest immobilization yields were achieved using Sty‐DVB, MA‐DVB, and DVB supports, which presented high surface areas and pore diameters. Among the developed biocatalysts, CalB‐MMA‐DVB, which presented a specific area of 320.9 m 2 /g, presented the highest esterification activity of 1410 ± 176 U/g bio −1 . In contrast, biocatalysts manufactured with polymer particles with smaller specific areas but containing polar monomers, such as Cal‐B‐MA‐EDGMA, Cal‐B‐GMA‐EDGMA, Cal‐B‐Vpy‐DVB, and Cal‐B‐VBC‐EDGMA, presented higher hydrolytic activities (HA). Cal‐B‐VBC‐EDGMA achieved a catalytic constant (Kcat) of 73.48 × 10 2 s −1 .