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PublicationRSC Advances
Pages62814 - 62824

Design of a core-shell support to improve lipases features by immobilization

Authors:Roberto Fernandez-Lafuente
Groups of research:Optimización de biocatalizadores y bioprocesos enzimáticos
Evelin A. Manoel a,b,c,+, Martina Pinto d,+, José C. S. dos Santos c,e,+, Veymar G. Tacias-Pascaciob,f, Denise M. G. Freire b, José Carlos Pinto *,d and Roberto Fernandez-Lafuente *,b
a Departamento de Biotecnologia Farmacêutica,  Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.
bDepartamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.
c Department of Biocatalysis, ICP-CSIC, Campus UAM-CSIC, Cantoblanco, 28049, Madrid, Spain.
d Programa de Engenharia Química, COPPE, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.
eInstituto de Engenharias e Desenvolvimento Sustentável, Universidade da Integração Internacional da Lusofonia Afro-Brasileira, CEP 62785-000, Acarape, CE, Brazil.
Unidad de Investigación y Desarrollo en Alimentos. Instituto Tecnológico de Veracruz, Calzada Miguel A. de Quevedo 2779, 91897 Veracruz, Mexico

Two 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 the 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. 
Keywords:Hydrophobic supports, interfacial activation, Polymeric supports; core-shell particles; lipase immobilization
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