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Engineering the Tat-secretion pathway of Bacillus licheniformis for the secretion of cytoplasmic enzyme arginase.
Ji, Yi; Li, Junliang; Liang, Yonglin; Li, Liang; Wang, Yajun; Pi, Li; Xing, Panpan; Nomura, Christopher T; Chen, Shouwen; Zhu, Chengjun; Wang, Qin.
Afiliación
  • Ji Y; State Key Laboratory of Biocatalysis and Enzyme Engineering, Environmental Microbial Technology Center of Hubei Province, College of Life Science, Hubei University, Wuhan, 430062, People's Republic of China.
  • Li J; State Key Laboratory of Biocatalysis and Enzyme Engineering, Environmental Microbial Technology Center of Hubei Province, College of Life Science, Hubei University, Wuhan, 430062, People's Republic of China.
  • Liang Y; State Key Laboratory of Biocatalysis and Enzyme Engineering, Environmental Microbial Technology Center of Hubei Province, College of Life Science, Hubei University, Wuhan, 430062, People's Republic of China.
  • Li L; State Key Laboratory of Biocatalysis and Enzyme Engineering, Environmental Microbial Technology Center of Hubei Province, College of Life Science, Hubei University, Wuhan, 430062, People's Republic of China.
  • Wang Y; State Key Laboratory of Biocatalysis and Enzyme Engineering, Environmental Microbial Technology Center of Hubei Province, College of Life Science, Hubei University, Wuhan, 430062, People's Republic of China.
  • Pi L; Wuhan Grand Hoyo Co., Ltd, Wuhan, 430075, People's Republic of China.
  • Xing P; Wuhan Grand Hoyo Co., Ltd, Wuhan, 430075, People's Republic of China.
  • Nomura CT; Department of Biological Sciences, University of Idaho, 875 Perimeter Drive, Moscow, ID, 83844, USA.
  • Chen S; State Key Laboratory of Biocatalysis and Enzyme Engineering, Environmental Microbial Technology Center of Hubei Province, College of Life Science, Hubei University, Wuhan, 430062, People's Republic of China.
  • Zhu C; Wuhan Grand Hoyo Co., Ltd, Wuhan, 430075, People's Republic of China. zhuchengjun@gmail.com.
  • Wang Q; State Key Laboratory of Biocatalysis and Enzyme Engineering, Environmental Microbial Technology Center of Hubei Province, College of Life Science, Hubei University, Wuhan, 430062, People's Republic of China. qin.wang@hubu.edu.cn.
Appl Microbiol Biotechnol ; 108(1): 89, 2024 Dec.
Article en En | MEDLINE | ID: mdl-38194145
ABSTRACT
The industrial bacterium Bacillus licheniformis has long been used as a microbial factory for the production of enzymes due to its ability to secrete copious amounts of native extracellular proteins and its generally regarded as safe (GRAS) status. However, most attempts to use B. licheniformis to produce heterologous and cytoplasmic enzymes primarily via the general secretory (Sec) pathway have had limited success. The twin-arginine transport (Tat) pathway offers a promising alternative for the extracellular export of Sec-incompatible proteins because it transports full, correctly folded proteins. However, compared to the Sec pathway, the yields of the Tat pathway have historically been too low for commercial use. To improve the export efficiency of the Tat pathway, we identified the optimal Tat-dependent signal peptides and increased the abundance of the Tat translocases, the signal peptidase (SPase), and the intracellular chaperones. These strategic modifications significantly improved the Tat-dependent secretion of the cytoplasmic enzyme arginase into the culture medium using B. licheniformis. The extracellular enzymatic activity of arginase showed a 5.2-fold increase after these modifications. Moreover, compared to the start strain B. licheniformis 0F3, the production of extracellular GFP was improved by 3.8 times using the strategic modified strain B. licheniformis 0F13, and the extracellular enzymatic activity of SOX had a 1.3-fold increase using the strain B. licheniformis 0F14. This Tat-based production chassis has the potential for enhanced production of Sec-incompatible enzymes, therefore expanding the capability of B. licheniformis as an efficient cellular factory for the production of high-value proteins. KEY POINTS • Systematic genetic modification of Tat-pathway in B. licheniformis. • Significant enhancement of the secretion capacity of Tat pathway for delivery the cytoplasmic enzyme arginase. • A new platform for efficient extracellular production of Sec-incompatible enzymes.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Arginasa / Bacillus licheniformis Tipo de estudio: Prognostic_studies Idioma: En Revista: Appl Microbiol Biotechnol Año: 2024 Tipo del documento: Article Pais de publicación: Alemania

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Arginasa / Bacillus licheniformis Tipo de estudio: Prognostic_studies Idioma: En Revista: Appl Microbiol Biotechnol Año: 2024 Tipo del documento: Article Pais de publicación: Alemania