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Highly efficient bio-production of putrescine from L-arginine with arginase and L-ornithine decarboxylase in engineered Escherichia coli.
Wang, Jing; Du, Min; Wang, Xin; He, Junchen; Zhang, Alei; Chen, Kequan.
Afiliación
  • Wang J; State Key Laboratory of Materials-Oriented Chemical Engineering, College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing 211816, Jiangsu, China.
  • Du M; State Key Laboratory of Materials-Oriented Chemical Engineering, College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing 211816, Jiangsu, China.
  • Wang X; State Key Laboratory of Materials-Oriented Chemical Engineering, College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing 211816, Jiangsu, China.
  • He J; State Key Laboratory of Materials-Oriented Chemical Engineering, College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing 211816, Jiangsu, China.
  • Zhang A; State Key Laboratory of Materials-Oriented Chemical Engineering, College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing 211816, Jiangsu, China.
  • Chen K; State Key Laboratory of Materials-Oriented Chemical Engineering, College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing 211816, Jiangsu, China. Electronic address: kqchen@njtech.edu.cn.
Bioresour Technol ; 413: 131471, 2024 Dec.
Article en En | MEDLINE | ID: mdl-39260727
ABSTRACT
To achieve industrial-scale putrescine production, a high efficient bio-synthesis of putrescine involving arginase (ARG, EC 3.5.3.1) and L-ornithine decarboxylase was evaluated here. Among the four arginases tested, ARGBT from Bos Taurus showed the highest activity (1966 U/mg). Compared to the L-arginine decarboxylase (ADC) pathway, the strain expressing ARGBT and L-ornithine decarboxylase (SpeC) produced 28.7 g/L putrescine, a 38.6 % increase. Two pyridoxal phosphate (PLP) salvage pathways were evaluated, and the strain BL-PTac-PdxK co-expressed pyridoxal kinase (PdxK) performed better. D-Glucose was used as the co-substrate to improve the putrescine titer further. Under optimal conditions, 43.6 g/L putrescine was produced from 87.1 g/L L-arginine, and 76 g/L putrescine was synthesized on a 0.5 L scale. Using L-arginine fermentation broth (60 g/L) as the substrate, a titer of 30 g/L putrescine was achieved. This efficient biotransformation process presented here enables feasible industrial-scale putrescine production.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ornitina Descarboxilasa / Arginasa / Arginina / Putrescina / Escherichia coli Límite: Animals Idioma: En Revista: Bioresour Technol Asunto de la revista: ENGENHARIA BIOMEDICA Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ornitina Descarboxilasa / Arginasa / Arginina / Putrescina / Escherichia coli Límite: Animals Idioma: En Revista: Bioresour Technol Asunto de la revista: ENGENHARIA BIOMEDICA Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido