Construction of novel recombinant Escherichia coli capable of producing 1,3-propanediol / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 743-747, 2005.
Article
in Chinese
| WPRIM
| ID: wpr-237080
ABSTRACT
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Propylene Glycols
/
Alcohol Dehydrogenase
/
Recombinant Proteins
/
Genetic Engineering
/
Aldehyde Reductase
/
Aerobiosis
/
Escherichia coli Proteins
/
Alcohol Oxidoreductases
/
Escherichia coli
/
Genetics
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2005
Type:
Article
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