Prediction and comparison of textural properties of magnetic copolymer supports for enzyme immobilization

• Published in: Journal of Applied Polymer Science
• Main Authors: Rosa, Cintia Maria Rodrigues, da Silva, Mateus Vinícius Casagrande, de Aguiar, Leandro Gonçalves, de Castro, Heizir Ferreira, Freitas, Larissa
• Other Authors: Coordenação de Aperfeiçoamento de Pessoal de Nível Superior, Fundação de Amparo à Pesquisa do Estado de São Paulo
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 2020
• Subjects: Antarc*; Antarctica
• Online Access: http://dx.doi.org/10.1002/app.49258; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fapp.49258; https://onlinelibrary.wiley.com/doi/pdf/10.1002/app.49258; https://onlinelibrary.wiley.com/doi/full-xml/10.1002/app.49258

Abstract Magnetic polymers supports have proven to be valuable materials for enzyme immobilization, as they allow recovering the catalyst by magnetic separation, precluding the need for costly and time‐consuming separation steps. In this study, magnetic copolymer supports were synthesized using styrene (STY) and different crosslinking agents (divinylbenzene, ethylene glycol dimethacrylate, or triethylene glycol dimethacrylate) and initiators (azobisisobutyronitrile or benzoyl peroxide) and used to immobilize Candida antarctica lipase B (CALB). The aim was to obtain biocatalysts with high enzymatic activity and satisfactory morphological properties for use in biotransformation reactions. Two morphological properties known to influence the immobilization yield were taken into consideration, specific surface area, and swelling index. Experimental data were compared to the predictions of a model based on molar balance, method of moments, numerical fractionation, and elementary gel structures. The high correlation ( R 2 = 0.9974) between experimental and predicted values demonstrated the suitability of the model for estimating the textural properties of enzyme supports. CALB was successfully immobilized, showing high hydrolytic activity (500–700 U g −1 ) and good thermal stability at 50°C. CALB/STY‐EGDMA‐M was 14 times more stable than free CALB. The results confirm the efficiency of the immobilization method and the suitability of the copolymers for enzyme immobilization.