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Twin-arginine signal peptide of Bacillus licheniformis GlmU efficiently mediated secretory expression of protein glutaminase
Niu, Dandan; Li, Congying; Wang, Peng; Huang, Lei; Mchunu, Nokuthula Peace; Singh, Suren; Prior, Bernard A; Ye, Xiuyun.
  • Niu, Dandan; Fuzhou University. College of Biological Science and Engineering. Fujian Provincial Key Laboratory of Marine Enzyme Engineering. Fuzhou. CN
  • Li, Congying; Fuzhou University. College of Biological Science and Engineering. Fujian Provincial Key Laboratory of Marine Enzyme Engineering. Fuzhou. CN
  • Wang, Peng; Fuzhou University. College of Biological Science and Engineering. Fujian Provincial Key Laboratory of Marine Enzyme Engineering. Fuzhou. CN
  • Huang, Lei; Tianjin University of Science and Technology. College of Chemical Engineering and Material Sciences. Tianjin. CN
  • Mchunu, Nokuthula Peace; Durban University of Technology. Faculty of Applied Sciences. Department of Biotechnology and Food Technology. Durban. ZA
  • Singh, Suren; Durban University of Technology. Faculty of Applied Sciences. Department of Biotechnology and Food Technology. Diamantina. ZA
  • Prior, Bernard A; Stellenbosch University. Department of Microbiology. Matieland. ZA
  • Ye, Xiuyun; Fuzhou University. College of Biological Science and Engineering. Fujian Provincial Key Laboratory of Marine Enzyme Engineering. Fuzhou. CN
Electron. j. biotechnol ; 42: 49-55, Nov. 2019. tab, ilus, graf
Artigo em Inglês | LILACS | ID: biblio-1087461
ABSTRACT

Background:

Protein glutaminase specifically deamidates glutamine residue in protein and therefore significantly improves protein solubility and colloidal stability of protein solution. In order to improve its preparation efficiency, we exploited the possibility for its secretory expression mediated by twin-arginine translocation (Tat) pathway in Bacillus licheniformis.

Results:

The B. licheniformis genome-wide twin-arginine signal peptides were analyzed. Of which, eleven candidates were cloned for construction of expression vectors to mediate the expression of Chryseobacterium proteolyticum protein glutaminase (PGA). The signal peptide of GlmU was confirmed that it significantly mediated PGA secretion into media with the maximum activity of 0.16 U/ml in Bacillus subtilis WB600. A mutant GlmU-R, being replaced the third residue aspartic acid of GlmU twin-arginine signal peptide with arginine by site-directed mutagenesis, mediated the improved secretion of PGA with about 40% increased (0.23 U/ml). In B. licheniformis CBBD302, GlmU-R mediated PGA expression in active form with the maximum yield of 6.8 U/ml in a 25-l bioreactor.

Conclusions:

PGA can be produced and secreted efficiently in active form via Tat pathway of B. licheniformis, an alternative expression system for the industrial-scale production of PGA.
Assuntos


Texto completo: DisponíveL Índice: LILACS (Américas) Assunto principal: Bacillus licheniformis / Glutaminase Idioma: Inglês Revista: Electron. j. biotechnol Assunto da revista: Biotecnologia Ano de publicação: 2019 Tipo de documento: Artigo País de afiliação: China / África do Sul Instituição/País de afiliação: Durban University of Technology/ZA / Fuzhou University/CN / Stellenbosch University/ZA / Tianjin University of Science and Technology/CN

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Texto completo: DisponíveL Índice: LILACS (Américas) Assunto principal: Bacillus licheniformis / Glutaminase Idioma: Inglês Revista: Electron. j. biotechnol Assunto da revista: Biotecnologia Ano de publicação: 2019 Tipo de documento: Artigo País de afiliação: China / África do Sul Instituição/País de afiliação: Durban University of Technology/ZA / Fuzhou University/CN / Stellenbosch University/ZA / Tianjin University of Science and Technology/CN