| 학회 | 한국화학공학회 |
| 학술대회 | 2008년 가을 (10/23 ~ 10/24, 부산 BEXCO) |
| 권호 | 14권 2호, p.2696 |
| 발표분야 | 생물화공 |
| 제목 | Cloning, Expression, and Characterization of a Novel Putative Aldehyde Dehydrogenase from Escherichia coli K-12 Which is Highly Active on3-Hydroxypropionaldehyde |
| 초록 | Our interest in 3-hydroxypropionic acid (3-HP) production from glycerol, which involves the oxidation of 3-hydroxypropionaldehyde (3-HPA) to 3-HP. Among the ALDHs tested in our laboratory, the putative aldehyde dehydrogenase (AldH) from Escherichia coli K-12 exhibited the highest activity on 3-HPA. To asses and characterize its specific function on 3-HPA, the gene aldH has been cloned in E. coli BL21 under the strong T5 promoter with pQE80L vector. Upon characterizing the purified AldH protein, we observed that this enzyme is highly specific to NAD+ over NADP+ as hydrogen acceptors. The enzyme activity was significantly high (38.1 U mg-1 protein) with 3-hydroxypropionaldehyde (3-HPA) in pH 8.0 at 37 oC. The low activation energy (E a ) of 20.4 kJ mol-1 for its oxidation of 3-HPA is advantageous in use of this enzyme for commercial applications. The kinetic properties of AldH on 3-HPA and 3-HP indicated that it mostly involved in oxidation reactions and the ratio (%) of oxidation/reduction is 96:4. The enzyme AldH can effectively be utilized for the biological production of 3-HP. |
| 저자 | 조지은 , 박성훈 |
| 소속 | 부산대 |
| 키워드 | 3-hydroxypropionic acid ; aldehyde dehydrogenases (ALDHs) ; Escherichia coli K-12 |
| VOD | VOD 보기 |
| 원문파일 | 초록 보기 |
