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author:

Niu, Dandan (Niu, Dandan.) [1] | Li, Congying (Li, Congying.) [2] | Wang, Peng (Wang, Peng.) [3] | Huang, Lei (Huang, Lei.) [4] | Mchunu, Nokuthula Peace (Mchunu, Nokuthula Peace.) [5] | Singh, Suren (Singh, Suren.) [6] | Prior, Bernard A. (Prior, Bernard A..) [7] | Ye, Xiuyun (Ye, Xiuyun.) [8] (Scholars:叶秀云)

Indexed by:

EI Scopus SCIE

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 25-1 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. (C) 2019 Pontificia Universidad Catolica de Valparaiso. Production and hosting by Elsevier B.V. All rights reserved.

Keyword:

Arginine Aspartic acid Bacillus licheniformis Bacillus subtilis Escherichia coli Prostaglandins A Protein glutaminase Protein sorting signals Secretion expression Signal peptide Tat pathway

Community:

  • [ 1 ] [Niu, Dandan]Fuzhou Univ, Coll Biol Sci & Engn, Fujian Prov Key Lab Marine Enzyme Engn, Fuzhou 350108, Fujian, Peoples R China
  • [ 2 ] [Li, Congying]Fuzhou Univ, Coll Biol Sci & Engn, Fujian Prov Key Lab Marine Enzyme Engn, Fuzhou 350108, Fujian, Peoples R China
  • [ 3 ] [Wang, Peng]Fuzhou Univ, Coll Biol Sci & Engn, Fujian Prov Key Lab Marine Enzyme Engn, Fuzhou 350108, Fujian, Peoples R China
  • [ 4 ] [Ye, Xiuyun]Fuzhou Univ, Coll Biol Sci & Engn, Fujian Prov Key Lab Marine Enzyme Engn, Fuzhou 350108, Fujian, Peoples R China
  • [ 5 ] [Niu, Dandan]Tianjin Univ Sci & Technol, Coll Chem Engn & Mat Sci, Tianjin 300457, Peoples R China
  • [ 6 ] [Huang, Lei]Tianjin Univ Sci & Technol, Coll Biotechnol, Tianjin 300457, Peoples R China
  • [ 7 ] [Mchunu, Nokuthula Peace]Durban Univ Technol, Fac Appl Sci, Dept Biotechnol & Food Technol, Durban, South Africa
  • [ 8 ] [Singh, Suren]Durban Univ Technol, Fac Appl Sci, Dept Biotechnol & Food Technol, Durban, South Africa
  • [ 9 ] [Prior, Bernard A.]Stellenbosch Univ, Dept Microbiol, Matieland, South Africa

Reprint 's Address:

  • 牛丹丹

    [Niu, Dandan]Fuzhou Univ, Coll Biol Sci & Engn, Fujian Prov Key Lab Marine Enzyme Engn, Fuzhou 350108, Fujian, Peoples R China;;[Niu, Dandan]Tianjin Univ Sci & Technol, Coll Chem Engn & Mat Sci, Tianjin 300457, Peoples R China

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Source :

ELECTRONIC JOURNAL OF BIOTECHNOLOGY

ISSN: 0717-3458

Year: 2019

Volume: 42

Page: 49-55

2 . 8 9 4

JCR@2019

2 . 3 0 0

JCR@2023

ESI Discipline: BIOLOGY & BIOCHEMISTRY;

ESI HC Threshold:189

JCR Journal Grade:2

CAS Journal Grade:4

Cited Count:

WoS CC Cited Count:

SCOPUS Cited Count: 10

ESI Highly Cited Papers on the List: 0 Unfold All

WanFang Cited Count:

Chinese Cited Count:

30 Days PV: 4

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