%0 Journal Article
%T Construction of Novel Recombinant Escherichia coli Capable of Producing 1,3-propanediol
产1,3-丙二醇新型重组大肠杆菌的构建
%A ZHANG Xiao-Mei
%A TANG Xue-Ming
%A ZHUGE Bin
%A SHEN Wei
%A RAO Zhi-Ming
%A FANG Hui-Ying
%A ZHUGE Jian
%A
张晓梅 唐雪明 诸葛斌 沈微
%A 饶志明 方慧英 诸葛健
%J 生物工程学报
%D 2005
%I
%X The 1,3-propanediol oxidoreductase isoenzyme encoding gene (yqhD) from E. coli was amplified by PCR. yqhD was inserted in pEtac to yield the recombinant expression vector pEtac-yqhD. Over-expression of yqhD in E. coli JM109 was achieved with pEtac-yqhD. SDS-PAGE analysis showed an over-expressed recombinant product at about 43 kD, consistent with the molecular weight predicted from gene sequence. Compared with E. coli JM109 (pEtac), the 1,3-propanediol oxidoreductase isoenzyme activity of the recombinant E. coli (pEtac-yqhD) reached 120 u/mg protein under the induction of 1.0 mmol/L IPTG at 37 degrees C for 4 hours; at similar conditions, enzyme activity of E. coli JM109 (pEtac) was only 0.5 u/mg protein. The recombinant E. coli JM109 (pUCtac-dhaB, pEtac-yqhD) was constructed. After induction with 1.0 mmol/L IPTG, the recombinant strain could transform 50 g/L glycerol to 38 g/L 1,3-propanediol under aerobic conditions. This work demonstrated firstly that the 1,3-propanediol oxidoreductase isoenzyme could show high activity under aerobic conditions.
%K 1
%K 3-propanediol oxidoreductase isoenzyme
%K recombinant Escherichia coli
%K 1
%K 3-propanediol
1
%K 3-丙二醇氧化还原酶同工酶,重组大肠杆菌,
%K 1
%K 3-丙二醇
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=76181A0CD23AD92E&yid=2DD7160C83D0ACED&vid=659D3B06EBF534A7&iid=94C357A881DFC066&sid=6EDA906E07280FB0&eid=F4DCFB3CB96519BF&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=9&reference_num=16