Portal de Periódicos da CAPES

Artigo Produção Nacional Revisado por pares

BIBTEX RIS

Immobilization of Pseudomonas cepacia lipase on layered double hydroxide of Zn/Al-Cl for kinetic resolution of rac-1-phenylethanol

2019; Elsevier BV; Volume: 130; Linguagem: Inglês

10.1016/j.enzmictec.2019.109365

1879-0909

Glauco Silva Dias, Pamela T. Bandeira, Silvia Jaerger, Leandro Piovan, David A. Mitchell, Fernando Wypych, Nádia Krieger,

Electrochemical sensors and biosensors

Layered double hydroxides (LDHs) are cheap materials suitable for immobilization of enzymes. In this study, we prepared Zn/Al-Cl LDHs with different Zn:Al molar ratios for immobilization of the lipase from Pseudomonas cepacia. The best values for activity retention (188%), immobilization efficiency (96%) and hydrolytic activity in organic medium (279 U g−1) were obtained with a molar ratio of Zn:Al of 4:1, a protein loading of 162 mg g−1 and Tris-HCl buffer (10 mmol L−1, pH 7.5) as the solvent for preparing the lipase solution. The immobilized lipase keeps its activity when stored at 4 °C during 30 days. The immobilized lipase gave a conversion of 50% in 1 h for the kinetic resolution of the alcohol rac-1-phenylethanol, with both ees and eep higher than 99% and E higher than 200. In the reutilization study, 30 successive 1-h kinetic resolutions were done with the same batch of immobilized enzyme. For all 30 resolutions, 50% conversion was maintained, with ees and eep higher than 99% and E higher than 200. These are promising results that lay the basis for further studies of immobilization of lipases onto LDHs for applications in organic media.