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Immobilization of Escherichia coli containing ω-transaminase activity in LentiKats®

Cárdenas-Fernández, Max, Neto, Watson, López, Carmen, Álvaro, Gregorio, Tufvesson, Pär, Woodley, John M. (2012) Immobilization of Escherichia coli containing ω-transaminase activity in LentiKats®. Biotechnology Progress, 28 (3). pp. 693-698. ISSN 8756-7938. E-ISSN 1520-6033. (doi:10.1002/btpr.1538) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:88155)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
https://doi.org/10.1002/btpr.1538

Abstract

Whole Escherichia coli cells overexpressing ω‐transaminase (ω‐TA) and immobilized cells entrapped in LentiKats® were used as biocatalysts in the asymmetric synthesis of the aromatic chiral amines 1‐phenylethylamine (PEA) and 3‐amino‐1‐phenylbutane (APB). Whole cells were permeabilized with different concentrations of cetrimonium bromide (CTAB) and ethanol; the best results were obtained with CTAB 0.1% which resulted in an increase in reaction rate by 40% compared to the whole cells. The synthesis of PEA was carried out using isopropyl amine (IPA) and L‐alanine (Ala) as amino donors. Using whole cell biocatalysis, the reaction with IPA was one order of magnitude faster than with Ala. No reaction was detected when permeabilized E. coli cells containing ω‐TA were employed using Ala as the amino donor. Additionally, the synthesis of APB from 4‐phenyl‐2‐butanone and IPA was studied. Whole and permeabilized cells containing ω‐TA and their immobilized LentiKats® counterparts showed similar initial reactions rates and yields in the reaction systems, indicating 100% of immobilization efficiency (observed activity/activity immobilized) and absence of diffusional limitations (due to the immobilization). Immobilization of whole and permeabilized cells containing ω‐TA in LentiKats® allowed improved stability as the biocatalyst was shown to be efficiently reused for five reaction cycles, retaining around 80% of original activity.

Item Type: Article
DOI/Identification number: 10.1002/btpr.1538
Uncontrolled keywords: whole cell biocatalysis; ω‐transaminase; asymmetric synthesis; chiral amines; cell permeabilization; immobilization by entrapment; LentiKats®
Subjects: Q Science > QR Microbiology
Divisions: Divisions > Division of Natural Sciences > School of Biosciences
Depositing User: Max Cardenas Fernandez
Date Deposited: 14 May 2021 15:25 UTC
Last Modified: 10 Jun 2021 15:33 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/88155 (The current URI for this page, for reference purposes)
Cárdenas-Fernández, Max: https://orcid.org/0000-0003-1422-5369
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