Project/Area Number |
60304027
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Research Category |
Grant-in-Aid for Co-operative Research (A)
|
Allocation Type | Single-year Grants |
Research Field |
発酵・醸造
|
Research Institution | Yamaguchi University |
Principal Investigator |
AMEYAMA Minoru Faculty of Agriculture, Yamaguchi University, Professor, 農学部, 教授 (90022053)
|
Co-Investigator(Kenkyū-buntansha) |
OHSHIRO Yoshiki Faculty of Engineering, Osaka University, Professor, 工学部, 教授 (70028984)
YAMANAKA Kei Institute of Applied Biochemistry, University of Tsukuba, Professor, 応用生物化学系, 教授 (30035951)
IMANAGA Yujiro Faculty of Science, Nara Women's University, Professor, 理学部, 教授 (60031613)
KAWAI Fusako School of Economics and Business Administeration, Kobe University of Commerce, A, 商経学部, 助教授 (60118007)
KATO Nobuo Faculty of Engineering, Tottori University, Associate Prof., 工学部, 助教授 (50026556)
|
Project Period (FY) |
1985 – 1986
|
Project Status |
Completed (Fiscal Year 1986)
|
Budget Amount *help |
¥7,100,000 (Direct Cost: ¥7,100,000)
Fiscal Year 1986: ¥3,200,000 (Direct Cost: ¥3,200,000)
Fiscal Year 1985: ¥3,900,000 (Direct Cost: ¥3,900,000)
|
Keywords | pyrroloquinoline quinone / glucose dehydrogenase / proteoliposome / PVA dehydrogenase / PEG dehydrogenase / enzyme model / diamine oxidase / ジアミン酸化酵素 |
Research Abstract |
AMEYAMA has established a new method for enzymatic determination of PQQ, purified apo-glucose dehydrogenase, determined the distribution of PQQ in nature, reconstituted a proteoliposome consisting of glucose dehydrogenase, terminal oxidase and ubiquinone, and disclosed the mechanism of growth promoting activity of PQQ for various microorganisms. IMANAGA studied the binding specificity of PQQ to PQQ-dependent glucose dehydrogenase from Pseudomonas fluorescens and Gluconobacter suboxydans. OHSHIRO examined the oxidation of various compounds including amino acids, amines, thiol compounds and alcohols, in a mixed micelle system with CTAB and proposed a model system of PQQ-dependent oxidation system. KATO reported a symbiotic degradation of polyvinyl alcohol and indicated the importance of PQQ. He also purified a novel enzyme, polyvinyl alcohol dehydrogenase, which requaires PQQ as the prosthetic group. KAWAI reported the purification and identification of polyethyleneglycol dehydrogenase a
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nd indicated the presence of PQQ as the prosthetic group of the enzyme. She also reported a novel enzyme, ether-bond cleaving enzyme, in a symbiotic microorganisms and suggested the presence of PQQ in such degradation system. SUZUKI isolated a peptide fraction containing PQQ from a highly purified human kidney diamine oxidase. SODA indicated the presence of a covalent bound PQQ in a highly purified nitroalkane oxidase, with deflavonated apo-enzyme. He concluded the flow of electron during enzyme activity to be from enzyme to PQQ and then to FAD to oxygen. TAKIMOTO reported that a trace amount of PQQ facilitated acetic acid fermentation. NAKASHIMA established a method in diagnostic test using PQQ-enzymes. He reported the use of alcohol dehydrogenase for alcoholism, fructose dehydrogenase for infertility of man, and amine dehydrogenase for a cancer. YAMANAKA reported novel enzymes, aromatic alcohol dehydrogenase and aromatic aldehyde dehydrogenase, in a photosynthesizing bacteria, Rhodopseudomonas acidophila, and confirmed the presence of PQQ as the prosthetic group. Less
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