Adsorption of lipases on porous silica-based materials for esterification in a solvent-free system

Kelly C N R Pedro; João V V da Silva; Eliane P Cipolatti; Evelin A Manoel; Ivone S P Campisano; Cristiane A Henriques; Marta A P Langone

doi:10.1007/s13205-023-03801-x

Adsorption of lipases on porous silica-based materials for esterification in a solvent-free system

3 Biotech. 2023 Nov;13(11):380. doi: 10.1007/s13205-023-03801-x. Epub 2023 Oct 25.

Authors

Kelly C N R Pedro¹, João V V da Silva¹, Eliane P Cipolatti², Evelin A Manoel³, Ivone S P Campisano¹, Cristiane A Henriques¹, Marta A P Langone^{1

4}

Affiliations

¹ Departamento de Química Analítica, Instituto de Química, Universidade do Estado do Rio de Janeiro (UERJ), Rua São Francisco Xavier, 524, 20550-900 Rio de Janeiro, RJ Brasil.
² Departamento de Engenharia Química, Instituto de Tecnologia, Universidade Federal Rural Do Rio de Janeiro, Rodovia BR 465, Km 07- Zona Rural, 23890-000 Seropédica, RJ Brasil.
³ Departamento de Biotecnologia Farmacêutica, Faculdade de Farmácia, Universidade Federal Do Rio de Janeiro (UFRJ), 21941-170 Rio de Janeiro, RJ Brasil.
⁴ Instituto Federal de Educação, Ciência e Tecnologia Do Rio de Janeiro, Rua Senador Furtado, 121, 20260-100 Rio de Janeiro, RJ Brasil.

PMID: 37900269
PMCID: PMC10600090 (available on 2024-11-01)
DOI: 10.1007/s13205-023-03801-x

Abstract

This study deals with lipase immobilization on micro- and mesoporous silica-based materials. The effects of the type of support (silica MCM-41, zeolite HZSM-5 (SAR 25), zeolite HZSM-5 (SAR 280), and the silica-aluminas Siral 10, Siral 20, and Siral 40) were investigated on the immobilization of lipase B from Candida antarctica (CALB) and lipase from Rhizomucor miehei (RML). The supports that allowed the highest immobilization efficiencies for the CALB were Siral 40 (91.4%), HZSM-5 (SAR 280) (90.6%), and MCM-41 (89.4%). Siral 20 allowed the highest immobilization efficiency for RML (97.6%), followed by HZSM-5 (SAR 25) (77.1%) and HZSM-5 (SAR 280) (62.7%). The effect of protein concentration on lipase immobilization was investigated, and the results adjusted well on the Langmuir isotherm model (R² > 0.9). The maximum protein adsorption capacity of the support determined by the Langmuir model was equal to 10.64 and 20.97 mg_protein g_support^-1 for CALB and RML, respectively. The effects of pH (pH 7.0 and pH 11.0) and phosphate buffer solution concentration (5 and 100 mmol L^-1) were also investigated on lipase immobilization. The immobilization efficiency for both lipases was similar for the different pH values. The use of 100 mmol L^-1 phosphate buffer decreased the lipase immobilization efficiency. The biocatalysts (CALB-Siral 40 and RML-Siral 20) were tested in the ethyl oleate synthesis. The conversion of 61.7% was obtained at 60 °C in the reaction catalyzed by CALB-Siral 40. Both heterogeneous biocatalysts showed increased thermal stability compared with their free form. Finally, the reuse of the biocatalysts was studied. CALB-Siral 40 and RML-Siral 20 maintained about 30% of the initial conversion after 3 batches of ethyl oleate synthesis. Silica-aluminas (Siral 20 and 40) proved to be a support that allowed a high efficiency of immobilization of lipases and activity for esterification reaction.

Keywords: Adsorption; Enzyme immobilization; Ethyl oleate; Langmuir isotherm; Lipases.

© King Abdulaziz City for Science and Technology 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.