首页> 外文期刊>Journal of industrial microbiology & biotechnology >Construction of a highly efficient Bacillus subtilis 168 whole-cell biocatalyst and its application in the production of L-ornithine
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Construction of a highly efficient Bacillus subtilis 168 whole-cell biocatalyst and its application in the production of L-ornithine

机译:高效枯草芽孢杆菌168全细胞生物催化剂的构建及其在L-鸟氨酸生产中的应用

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摘要

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 A degrees C, respectively. In addition, the recombinant arginase exhibited a strong Mn2+ 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.
机译:鸟氨酸是一种非蛋白质氨基酸,通常从水解蛋白质中提取并通过微生物发酵产生。在这里,我们专注于生产l-鸟氨酸的高效全细胞生物催化剂。从解淀粉芽孢杆菌B10-127克隆了编码精氨酸酶催化l-精氨酸水解为1-鸟氨酸和尿素的基因argI,并在GRAS枯草芽孢杆菌168中表达。该重组菌株的精氨酸酶活性为21.9 U /。毫克,这是野生枯草芽孢杆菌168的26.7倍。纯化的重组精氨酸酶的最佳pH和温度分别为10.0和40 A摄氏度。另外,重组精氨酸酶表现出强烈的Mn2 +偏好性。当使用基于全细胞生物催化剂的生物转化时,在12小时内在5升反应器中采用分批补料策略可实现356.9 g / L的高l-鸟氨酸产量。这项全细胞生物转化研究证明了工业生产左旋鸟氨酸的环保策略。

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