期刊文献+
共找到1篇文章
< 1 >
每页显示 20 50 100
Expression of a New hemA Gene from Agrobacterium radiobacter in Escherichia coli for 5-Aminolevulinate Production 被引量:4
1
作者 LIU Xiaoxia(刘晓侠) +5 位作者 LIN Jianping(林建平) QIN gang(秦钢) CEN Peilin(岑沛霖) 《Chinese Journal of Chemical Engineering》 SCIE EI CAS CSCD 2005年第4期522-528,共7页
A new hemA gene encoding 5-aminolevulinate (ALA) synthase was cloned from Agrobacterium ra- diobacter zju-0121. The ALA synthase catalyzes the pyridoxal phosphate-dependent condensation of succinyl coen- zyme A (succi... A new hemA gene encoding 5-aminolevulinate (ALA) synthase was cloned from Agrobacterium ra- diobacter zju-0121. The ALA synthase catalyzes the pyridoxal phosphate-dependent condensation of succinyl coen- zyme A (succinyl-CoA) and glycine to produce ALA. Four plasmids carrying the A, radiobacter hemA gene were transformed into different E. coli strains. The effects of both genetic and physiological factors on the expression of ALA synthase and ALA production were studied. The results indicated that the final intracellular activity of ALA synthase and the production of ALA in different expression systems varied largely. Among them, the recombinant E. coli BL21 (DE3) harboring the expression plasmid pET28-A. R-hemA was the most suitable one. The effects of isopropyl-β-D-thiogalactopyranoside (IPTG) addition time, IPTG concentration, culture temperature and the initial concentration of precursors and glucose on the ALA production were also evaluated. The expressed ALA synthase accounted for about 23.7% of the intracellular soluble protein. The highest specific activity of ALA syn- thase was 13.8nmol·min-1·mg-1 of intracellular soluble protein. In the batch culture of the recombinant E. coli, the extracellular ALA concentration reached 0.9 g·L-1. 展开更多
关键词 5-aminolevulinate (ALA) ALA synthase metabolic engineering
下载PDF
上一页 1 下一页 到第
使用帮助 返回顶部