@article{
author = "Velicić, Zorica and Rusmirović, Jelena and Prlainović, Nevena and Tomić, Nataša and Veličković, Zlate and Taleb, Khaled and Marinković, Aleksandar",
year = "2020",
abstract = "In this work, the optimization of synthesis of terpolymer monolith based on glycidyl methacrylate (GMA), ethylene glycol dimethacrylate (EGDMA) and additional cross-linkers: trimethylolpropanetriacrylate (TMPTA) or triethylene glycol dimethacrylate (TEGDMA) was performed. Moreover, novel vinyl functionalized cross-linkable polymers: ethanolamine (EA)/methacryloyl (MAC) modified poly (methyl methacrylate) (PMMA), and hydrolyzed poly (ethylene-co-vinyl acetate) copolymer (EVOH) modified with MAC either directly or via ethyl malonyl chloride/EA bridging group (m-EVA) were used as cross-linkable polymer to improve mechanical/elastic properties of the obtained monoliths. Optimization procedure, performed applying response surface methodology (RSM), was focused on the production of materials with improved dimensional stability/integrity and porosity with abundance of epoxide groups capable for immobilization of lipase from Candida rugosa (CRL). Structural characterization of the synthesized monoliths was determined using FTIR, Raman and H-1 NMR spectroscopies, while morphology/porosity was determined by SEM technique and image analysis; and mechanical properties by diametral compression testing. The most potential monolith containing m-EVA polymeric cross-linker, i.e. GMA/EGDMA/TEGDMA/m-EVA monolith, was used as CRL carrier in a two-step immobilization process. Enzyme loading and the activity of obtained preparations for various initial enzyme concentrations were monitored after 4 and 48 h of immobilization. The resulting catalysts show high potency in biocatalytic reactions with the highest percentage of retained initial lipase activity of 64.5%.",
publisher = "Springer, Dordrecht",
journal = "Journal of Polymer Research",
title = "The optimization of glycidyl methacrylate based terpolymer monolith synthesis: an effective Candida rugosa lipase immobilization support",
number = "5",
volume = "27",
doi = "10.1007/s10965-020-02127-z"
}