Different core-shell polymeric supports, exhibiting different morphologies and composition, were produced through simultaneous suspension and emulsion polymerization, using styrene (S) and divinylbenzene (DVB) as co-monomers. Supports composed of polystyrene in both the core and the shell (PS/PS) and the new poly(styrene-co-divinylbenzene) support (PS-co-DVB/PS-co-DVB) were used for the immobilization of three different lipases (from Rhizomucor miehie (RML), from Themomyces lanuginosus (TLL) and the form B from Candida antarctica, (CALB)) and of the phospholipase Lecitase Ultra (LU). The features of the new biocatalysts were evaluated and compared to the properties of commercial biocatalysts (Novozym 435 (CALB), Lipozyme RM IM and Lipozyme TL IM) and biocatalysts prepared by enzyme immobilization onto commercial octyl-agarose, a support reported as very suitable for lipase immobilization. It was shown that protein loading and stability of the biocatalysts prepared with the core-shell supports were higher than the ones obtained with commercial octyl-agarose or the commercial lipase preparations. Besides, it was shown that the biocatalysts prepared with the core-shell supports also presented higher activities than commercial biocatalysts when employing different substrates, encouraging the use of the produced core-shell supports for immobilization of lipases and the development of new applications.

A recombinant lipase B from Candida antarctica (LipB) in Pichia pastoris was synthesized through submerged fermentation using crude glycerin as substrate. The immobilization of this enzyme on the core–shell polymeric supports is an effective alternative for its application. The supports with distinct levels of hydrophobicity were produced through combined suspension and emulsion polymerization in pilot scale. Particles with distinct compositions were synthesized (PMMA/PMMA; PMMA‐co‐DVB/PMMA‐co‐DVB; and PS‐co‐DVB/PS‐co‐DVB) and employed on the immobilization of the produced lipase (LipB) and the commercial enzyme (CalB). The morphological properties (specific area, average pore diameter, specific volume of pores, and hydrophobicity level) and the influence of the polymerization conditions on the morphology of the supports were studied. The thermal stability of such biocatalysts was also investigated in the presence of calcium cation (Ca+2), maintained 100% of the activity after 3 h at 50°C when the PMMA‐co‐DVB/PMMA‐co‐DVB was employed. The synthesized enzyme and supports manufactured in pilot scale were employed successfully for production of esters using residual fatty acids as substrates, adding value to these raw materials and increasing the ranges of possible applications.

New nanoparticles are synthesized through emulsion polymerization, using distinct comonomers (styrene, divinylbenzene, glycidyl methacrylate and pentafluorostyrene). Then, for the first time, two strategies are adopted to functionalize such nanoparticles using benzylamine and thiophenol: (i) after the manufacture of the nanoparticles; and (ii) in situ during the polymerization reaction. Afterwards, the functionalized nanoparticles are used as nanosupports for immobilization of lipase B from Candida antarctica and the performance of the novel nanobiocatalysts are evaluated. It is shown that the nanoparticles exhibit different properties (specific areas ranging from 34 m2 g−1 to 324 m2 g−1; and contact angles ranging from 29° to 126°), indicating that both procedures can be used to adjust the properties of the polymer supports. Moreover, the nanobiocatalysts are applied successfully in hydrolysis and esterification reactions, exhibiting higher activities than the non‐functionalized biocatalysts. It is also observed that more hydrophilic supports result in more active biocatalysts in hydrolysis (27 ± 1 U g−1) and intermediate hydrophobic matrices conduct to more active biocatalysts in esterification reactions (1564 ± 50 U g−1). It is shown that highly hydrophobic surfaces may cause a significant decrease in the activity of such biocatalysts, probably due to distortions on the enzyme active center and to more intense chemical partitioning effects.

Core–shell polymer supports with different morphological features and compositions are prepared through combined suspension and emulsion polymerizations. It is shown that proper manipulation of the divinylbenzene (DVB) feed content allows for maximization of specific areas, porosities, and mechanical resistances. Additionally, it is shown that feeding of previously prepared miniemulsions leads to core–shell particles with smaller specific areas, due to less efficient coating of the cores. Particularly, the combined manipulation of polymerization times and DVB feed compositions allows for production of particles with pronounced specific area (50 m2 g−1) and porosity (0.30 cm3 g−1). Produced core–shell polymer particles are employed as supports for the immobilization of lipase B from Candida antarctica, and the obtained enzymatic activities for both hydrolysis (A hyd) and esterification (A est) reactions are very high (A hyd = 34.7 ± 3.8 U/g; A est = 3564.6 ± 581 U/g), even when compared to activities obtained using the reference commercial biocatalyst Novozym 435 (A hyd = 7.6 ± 1.8 U/g, A est = 2384.7 ± 307.2 U/g). Finally, biocatalysts prepared with the core–shell supports present higher enzymatic activities than biocatalysts prepared with supports of higher specific area obtained through conventional emulsion polymerizations, indicating that the porous structure of the shell can be beneficial for the immobilization and activity of the enzymes.

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