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Kazuya, Tanioka. Functional analysis of membrane-bound alcohol dehydrogenase of Gluconobacter oxydans, a member of Acetic acid bacteria. Master's Degree(Life Sciences). Kasetsart University. Office of the University Library. : Kasetsart University, 2021.
Functional analysis of membrane-bound alcohol dehydrogenase of Gluconobacter oxydans, a member of Acetic acid bacteria
Name: Kazuya, Tanioka
Classification :.LCCS: QR82.P78
LCSH:
Acetobacter
LCSH:
Acetic acid
LCSH:
Alcohol dehydrogenase
Abstract:
Acetic acid fermentation from ethanol by acetic acid bacteria is carried out by two successive reactions of membrane-bound alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). ADH catalyzes the first step in acetic acid production and is composed of three subunits, AdhA, AdhB, and AdhS. In this study, to analyze the function of each ADH, the gene disruption strains (ΔadhB, ΔadhS, ΔadhBS, ΔadhA) were constructed using the conjugation method from Gluconobacter oxydans NBRC 3293 and measured activities (mADH, Q1, O2 consumption) and performed SDS-PAGE. In addition, mADH, GDH, GLDH activities of Gluconobacter frateurii CHM43 and their transformants were measured. Since TANI3 (ΔadhB) lacks the B subunit, it showed only ferricyanide reduction activity at pH 5.0. TANI4 (ΔadhS) showed a decrease in each activity compared to the wild strain. In TANI4, each activities (mADH, Q1, O2 consumption)were decreased compared with the wild-type strain, however, the difference in activity phenomenon was generated depending on the type of activity. I also confirmed that TANI4 was not involved in the binding of PQQ to ADH in the 1-week activity assay. It was suggested that another method be used to investigate the relationship between PQQ and the S subunit. In TANI8(ΔadhBS), heme staining showed that the A subunit band was thinner than those others, suggesting that ADH is unstable only in the A subunit. In addition, adhAB(S)-expressing TORI4 showed mADH activity. The results of the present study and those of Habe et al. suggest that the ADH from Acetobacter tropicalis can function as ADH with or without AdhS.
Kasetsart University. Office of the University Library
Address:
Bangkok
Email:
tdckulib@ku.ac.th
Name: Toshiharu Yakushi
Role:
Thesis Advisor
Name: Gunjana Theeragool
Role:
Thesis CO-Advisor
Created:
2021
Modified:
2025-07-18
Issued:
2025-07-18
วิทยานิพนธ์/Thesis
application/pdf
URL: https://www.lib.ku.ac.th/KUthesis/2564/kazuya-tan-all.pdf
CallNumber:
QR82.P78 .K39
eng
DegreeName: Master of Science
Level: Master's Degree
Descipline: Life Sciences
Grantor: Kasetsart University
©copyrights Kasetsart University
RightsAccess:
ใช้เวลา
0.034096 วินาที
Kazuya, Tanioka
| Title | Contributor | Type |
|---|---|---|
| Functional analysis of membrane-bound alcohol dehydrogenase of Gluconobacter oxydans, a member of Acetic acid bacteria
มหาวิทยาลัยเกษตรศาสตร์ Kazuya, Tanioka | Toshiharu Yakushi | วิทยานิพนธ์/Thesis |
Toshiharu Yakushi
| Title | Creator | Type and Date Create |
|---|---|---|
| Periplasmic metabolic engineering to produce protocatechuic acid from quinic acid with gluconobacter oxydans
มหาวิทยาลัยเกษตรศาสตร์ Toshiharu Yakushi | Nagaki, Kakeru | วิทยานิพนธ์/Thesis |
| Functional analysis of membrane-bound alcohol dehydrogenase of Gluconobacter oxydans, a member of Acetic acid bacteria
มหาวิทยาลัยเกษตรศาสตร์ Toshiharu Yakushi | Kazuya, Tanioka | วิทยานิพนธ์/Thesis |
Gunjana Theeragool