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Efficient cascade biosynthesis of (S)-2-hydroxybutyric acid / 生物工程学报
Chinese Journal of Biotechnology ; (12): 4231-4242, 2021.
Artículo en Chino | WPRIM | ID: wpr-921501
ABSTRACT
2-Hydroxybutyric acid (2-HBA) is an important intermediate for synthesizing biodegradable materials and various medicines. Chemically synthesized racemized 2-HBA requires deracemization to obtain optically pure enantiomers for industrial application. In this study, we designed a cascade biosynthesis system in Escherichia coli BL21 by coexpressing L-threonine deaminase (TD), NAD-dependent L-lactate dehydrogenase (LDH) and formate dehydrogenase (FDH) for production of optically pure (S)-2-HBA from bulk chemical L-threonine (L-Thr). To coordinate the production rate and the consumption rate of the intermediate 2-oxobutyric acid in the multi-enzyme cascade catalytic reactions, we explored promoter engineering to regulate the expression levels of TD and FDH, and developed a recombinant strain P21285FDH-T7V7827 with a tunable system to achieve a coordinated multi-enzyme expression. The recombinant strain P21285FDH-T7V7827 was able to efficiently produce (S)-2-HBA with the highest titer of 143 g/L and a molar yield of 97% achieved within 16 hours. This titer was approximately 1.83 times than that of the highest yield reported to date, showing great potential for industrial application. Our results indicated that constructing a multi-enzyme-coordinated expression system in a single cell significantly contributed to the biosynthesis of hydroxyl acids.
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Texto completo: Disponible Índice: WPRIM (Pacífico Occidental) Asunto principal: Treonina Deshidratasa / Escherichia coli / Formiato Deshidrogenasas / Hidroxibutiratos Idioma: Chino Revista: Chinese Journal of Biotechnology Año: 2021 Tipo del documento: Artículo

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Texto completo: Disponible Índice: WPRIM (Pacífico Occidental) Asunto principal: Treonina Deshidratasa / Escherichia coli / Formiato Deshidrogenasas / Hidroxibutiratos Idioma: Chino Revista: Chinese Journal of Biotechnology Año: 2021 Tipo del documento: Artículo