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Received February 23, 2021
Accepted May 22, 2021
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This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/3.0) which permits
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Application of L-glutamate oxidase from Streptomyces sp. X119-6 with catalase (KatE) to whole-cell systems for glutaric acid production in Escherichia coli
Sion Ham
Yeong-Hoon Han
Sang Hyun Kim
Min Ju Suh
Jang Yeon Cho
Hong-Ju Lee
See-Hyoung Park1
Kyungmoon Park1
Jung-Oh Ahn2
Jeong Chan Joo3
Shashi Kant Bhatia†
ung-Hun Yang†
Department of Biological Engineering, College of Engineering, Konkuk University, Seoul 05029, Korea 1Department of Biological and Chemical Engineering, Hongik University, Sejong 30016, Korea 2Biotechnology Engineering Center, Korea Research Institute Bioscience Biotechnology (KRIBB), Cheongju-si 28116, Korea 3Department of Biotechnology, The Catholic University of Korea, Bucheon-si, Gyeonggi 14662, Korea
shashibiotechhpu@gmail.com
Korean Journal of Chemical Engineering, October 2021, 38(10), 2106-2112(7), 10.1007/s11814-021-0855-8
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Abstract
Whole-cell systems offer many benefits for biochemical production, such as relatively easy enzyme control and higher tolerance toward harsh environments, than purified enzymes. These systems can be applied to many bioconversion reactions, but they sometimes require cofactor regeneration units to support reactions at high substrate concentrations. Here, we examined L-glutamate oxidase (GOX) from Streptomyces sp. X119-6, which produces α- ketoglutarate (α-KG) from L-glutamate, and catalase (KatE) from Escherichia coli, which removes hydrogen peroxide generated by GOX. After optimizing the expression vector, pH, strains, culture conditions, and isopropyl β-D-1-thiogalactopyranoside concentration, we compared their efficiency to that of a previously reported GOX from Streptomyces mobaraensis. Our results indicated that GOX from Streptomyces sp. X119-6 and KatE increased α-KG production by 2.76-fold. This GOX required high levels of α-KG as an amino donor to convert 5-aminovaleric acid to glutaric acid. Performing the reaction at pH 8 enabled us to avoid the exogenous addition of catalase, but severe substrate inhibition was observed, resulting in the production of 287mM glutaric acid. This α-KG regeneration system has potential for improving production in various aminotransferase systems.
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