| Literature DB >> 26314414 |
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
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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