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Co-immobilised aspartase and transaminase for high-yield synthesis of l-phenylalanine

Cárdenas-Fernández, Max, Khalikova, Elvira, Korpela, Timo, López, Carmen, Álvaro, Gregorio (2014) Co-immobilised aspartase and transaminase for high-yield synthesis of l-phenylalanine. Biochemical Engineering Journal, 93 . pp. 173-178. ISSN 1369-703X. (doi:10.1016/j.bej.2014.10.010) (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:88159)

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.
Official URL:
https://doi.org/10.1016/j.bej.2014.10.010

Abstract

l-phenylalanine (Phe) was synthesised by coupling the enzymes aspartase (AspB) catalysing the synthesis of l-aspartate from fumarate and NH4Cl and microbial aspartate transaminase (TA) catalysing the transfer of the amino group from l-aspartate to phenylpyruvate. Phe synthesis was studied with enzymes in solution and immobilised separately and together on amino-epoxy Relizyme® support. Immobilisation efficiencies and recovered activities of co-immobilised enzymes were slightly lower than those obtained when immobilised separately. Substrate and enzyme concentrations for the synthesis reactions were optimised as follows: co-immobilised 0.3 U/mL AspB and 2 U/mL TA, 0.15 M fumarate, 0.3 M NH4Cl, 0.1 M phenylpyruvate, 0.1 mM pyridoxal-5′-phosphate (PLP) at pH 7.5 and 37 °C. Total reaction yield of 83% and Phe yield of 95% were obtained. The initial rates of the reactions catalysed by co-immobilised enzymes were similar to those obtained when the reactions were catalysed by free enzymes, indicating negligible diffusional limitations associated to the application of the co-immobilised enzymes.

Item Type: Article
DOI/Identification number: 10.1016/j.bej.2014.10.010
Uncontrolled keywords: One-pot multienzymatic reaction; Co-immobilised enzymes; l-phenylalanineAspartase; Transaminase; Immobilisation on epoxy support
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Max Cardenas Fernandez
Date Deposited: 14 May 2021 15:37 UTC
Last Modified: 17 Aug 2022 11:02 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/88159 (The current URI for this page, for reference purposes)

University of Kent Author Information

Cárdenas-Fernández, Max.

Creator's ORCID: https://orcid.org/0000-0003-1422-5369
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