Literature DB >> 26314414

Construction of a highly efficient Bacillus subtilis 168 whole-cell biocatalyst and its application in the production of L-ornithine.

Meizhou Wang1, Meijuan Xu1, Zhiming Rao2, Taowei Yang1, Xian Zhang1.   

Abstract

L-Ornithine, a non-protein amino acid, is usually extracted from hydrolyzed protein as well as produced by microbial fermentation. Here, we focus on a highly efficient whole-cell biocatalyst for the production of L-ornithine. The gene argI, encoding arginase, which catalyzes the hydrolysis of L-arginine to L-ornithine and urea, was cloned from Bacillus amyloliquefaciens B10-127 and expressed in GRAS strain Bacillus subtilis 168. The recombinant strain exhibited an arginase activity of 21.9 U/mg, which is 26.7 times that of wild B. subtilis 168. The optimal pH and temperature of the purified recombinant arginase were 10.0 and 40 °C, respectively. In addition, the recombinant arginase exhibited a strong Mn(2+) preference. When using whole-cell biocatalyst-based bioconversion, a hyper L-ornithine production of 356.9 g/L was achieved with a fed-batch strategy in a 5-L reactor within 12 h. This whole-cell bioconversion study demonstrates an environmentally friendly strategy for L-ornithine production in industry.

Entities:  

Keywords:  B. subtilis 168; L-Ornithine; Recombinant arginase; Whole-cell bioconversion

Mesh:

Substances:

Year:  2015        PMID: 26314414     DOI: 10.1007/s10295-015-1672-z

Source DB:  PubMed          Journal:  J Ind Microbiol Biotechnol        ISSN: 1367-5435            Impact factor:   3.346


  38 in total

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Journal:  Gene       Date:  1997-07-09       Impact factor: 3.688

4.  REQUIREMENTS FOR TRANSFORMATION IN BACILLUS SUBTILIS.

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Journal:  J Bacteriol       Date:  1961-05       Impact factor: 3.490

5.  Overexpression of (His)6-tagged human arginase I in Saccharomyces cerevisiae and enzyme purification using metal affinity chromatography.

Authors:  Andriy E Zakalskiy; Oksana M Zakalska; Yuriy A Rzhepetskyy; Natalia Potocka; Oleh V Stasyk; Daniel Horak; Mykhailo V Gonchar
Journal:  Protein Expr Purif       Date:  2011-09-17       Impact factor: 1.650

6.  Genetic manipulation of a primary metabolic pathway for L-ornithine production in Escherichia coli.

Authors:  Young-Joon Lee; Jae-Yong Cho
Journal:  Biotechnol Lett       Date:  2006-08-25       Impact factor: 2.461

7.  Lysine and glutamate production by Corynebacterium glutamicum on glucose, fructose and sucrose: roles of malic enzyme and fructose-1,6-bisphosphatase.

Authors:  Tobias Georgi; Doris Rittmann; Volker F Wendisch
Journal:  Metab Eng       Date:  2005-07       Impact factor: 9.783

8.  Effect of supplemental ornithine on wound healing.

Authors:  Han Ping Shi; Rhonda S Fishel; David T Efron; Jeremy Z Williams; Matthew H Fishel; Adrian Barbul
Journal:  J Surg Res       Date:  2002-08       Impact factor: 2.192

9.  Effect of increased glutamate availability on L-ornithine production in Corynebacterium glutamicum.

Authors:  Joong-Hee Hwang; Gui-Hye Hwang; Jae-Yong Cho
Journal:  J Microbiol Biotechnol       Date:  2008-04       Impact factor: 2.351

10.  Expression, purification and characterization of arginase from Helicobacter pylori in its apo form.

Authors:  Jinyong Zhang; Xiaoli Zhang; Chao Wu; Dongshui Lu; Gang Guo; Xuhu Mao; Ying Zhang; Da-Cheng Wang; Defeng Li; Quanming Zou
Journal:  PLoS One       Date:  2011-10-20       Impact factor: 3.240

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  1 in total

Review 1.  Our microbes not only produce antibiotics, they also overproduce amino acids.

Authors:  Sergio Sanchez; Romina Rodríguez-Sanoja; Allison Ramos; Arnold L Demain
Journal:  J Antibiot (Tokyo)       Date:  2017-11-01       Impact factor: 2.649

  1 in total

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