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Immobilization of Pseudomonas Cepacia Lipase on Layered Double Hydroxide of Zn/Al-Cl for Kinetic Resolution of rac-1-phenylethanol

Glauco Silva Dias, Pamela Taisline Bandeira, Silvia Jaerger, Leandro Piovan, David Alexander Mitchell, Fernando Wypych, Nadia Krieger

Enzyme Microb Technol. 2019 Nov;130:109365.

PMID: 31421722

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
AP9001621-F Lipase from Pseudomonas cepacia Lipase from Pseudomonas cepacia 9001-62-1 Price
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