A new heterofunctional support for enzyme immobilization: PEI functionalized Fe 3 O 4 MNPs activated with divinyl sulfone. Application in the immobilization of lipase from Thermomyces lanuginosus.
Autor: | Bezerra RM; Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, CEP 60455760, Fortaleza, CE, Brazil., Monteiro RRC; Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, CEP 60455760, Fortaleza, CE, Brazil., Neto DMA; Grupo de Química de Materiais Avançados (GQMat), Universidade Federal do Ceará, Campus do Pici, CP 12100, CEP 60451-970, Fortaleza, CE, Brazil., da Silva FFM; Instituto Federal de Educação, Ciência e Tecnologia do Rio Grande do Norte, Campus Apodi, CEP 59700-000, Apodi, RN, Brazil., de Paula RCM; Departamento de Química Orgânica e Inorgânica, Universidade Federal do Ceará, Campus do Pici, CEP 60455760, Fortaleza, CE, Brazil., de Lemos TLG; Departamento de Química Orgânica e Inorgânica, Universidade Federal do Ceará, Campus do Pici, CEP 60455760, Fortaleza, CE, Brazil., Fechine PBA; Grupo de Química de Materiais Avançados (GQMat), Universidade Federal do Ceará, Campus do Pici, CP 12100, CEP 60451-970, Fortaleza, CE, Brazil., Correa MA; Departamento de Física, Universidade Federal do Rio Grande do Norte, CEP 59078900 Natal, RN, Brazil., Bohn F; Departamento de Física, Universidade Federal do Rio Grande do Norte, CEP 59078900 Natal, RN, Brazil., Gonçalves LRB; Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, CEP 60455760, Fortaleza, CE, Brazil. Electronic address: lrg@ufc.br., Dos Santos JCS; Instituto de Engenharias e Desenvolvimento Sustentável, Universidade da Integração Internacional da Lusofonia Afro-Brasileira, Campus das Auroras, CEP 62790970, Redenção CE, Brazil. Electronic address: jcs@unilab.edu.br. |
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Jazyk: | angličtina |
Zdroj: | Enzyme and microbial technology [Enzyme Microb Technol] 2020 Aug; Vol. 138, pp. 109560. Date of Electronic Publication: 2020 Apr 23. |
DOI: | 10.1016/j.enzmictec.2020.109560 |
Abstrakt: | Lipase from Thermomyces lanuginosus (TLL) was immobilized onto a novel heterofunctional support, divinyl sulfone (DVS) superparamagnetic nanoparticles (SPMNs) functionalized with polyethyleneimine (PEI). Particle size and zeta potential measurements, elemental analysis, X-ray powder diffraction, magnetic measurements, and infrared spectroscopy analysis were used to characterize the TLL preparations. At pH 10, it was possible to achieve 100 % of immobilization yield in 1 h. The immobilization pH gives TLL preparations with different stabilities; indeed the TLL preparation immobilized at pH 5.0 was the most stable during the thermal inactivation at all pH values. For the hydrolysis of racemic methyl mandelate, the nanobiocatalysts immobilized at pH 5.0 and blocked with ethylenediamine (EDA) and ethanolamine (ETA) obtained good enantioselectivities (68 % and 72 %, respectively) with high catalytic activities in the reaction medium at pH 7.0. The operational stability of the systems was evaluated in the esterification reaction of benzyl alcohol, obtaining up to 61 % conversion after the seventh reaction cycle. These results show that SPMN@PEI-DVS support is a robust strategy for the easy and rapid recovery of the nanobiocatalyst by applying a magnetic field, showing great potential for industrial applications. Competing Interests: Declaration of Competing Interest The authors whose names are listed immediately below certify and/or informed consent that they have NO affiliations with or involvement in any organization or entity with any financial interest (such as honoraria; educational grants; participation in speakers’ bureaus; membership, employment, consultancies, stock ownership, or other equity interest; and expert testimony or patent-licensing arrangements), or research involving human participants and/or animals, or non-financial interest (such as personal or professional relationships, affiliations, knowledge or beliefs) in the subject matter or materials discussed in this manuscript. (Copyright © 2020 Elsevier Inc. All rights reserved.) |
Databáze: | MEDLINE |
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