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Distribution and solubilization of particulate gluconate dehydrogenase and particulate 2-ketogluconate dehydrogenase in acetic acid bacteria.
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- SHINAGAWA Emiko
- Department of Agricultural Chemistry, Yamaguchi University
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- CHIYONOBU Toshikazu
- Department of Agricultural Chemistry, Yamaguchi University
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- ADACHI Osao
- Department of Agricultural Chemistry, Yamaguchi University
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- AMEYAMA Minoru
- Department of Agricultural Chemistry, Yamaguchi University
Bibliographic Information
- Other Title
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- Distribution and solubilization of particulate gluconate dehyrdogenase and paticulate 2-ketogluconate dehydrogenase in acetic acid bacteria
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Description
The distribution of two particulate enzymes, gluconate dehydrogenase (GDH) and 2-ketogluconate dehydrogenase (2 KGDH), was investigated with cell free extract through 26 strains of genus Acetobacter and genus Ghrconobacter. GDH activity was found in the cell free extracts from all strains of genus Gluconobacter and two species of genus Acetobacter, A. aceti and A. aurantium. High activity of 2KGDH was also found in the pigment-producing strains of genus Gluconobacter.<br> Best solubilization of particulate enzymes was attained with the highest recovery when 10mg of Triton X-100 and 30mg of protein of particulate fractions in 1ml of 0.01M phosphate buffer, pH 6.0, are incubated for 9 hr at 5°C with continuous stirring.<br> By comparison of the total, enzyme activity of particulate enzymes with that of NAD (P)-linked enzymes in the cell free extract, it was obvious that the formation of ketogluconates by particulate enzymes was much more predominant, roughly over 100 times higher, as that of NAD (P)-linked enzymes.
Journal
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- Agricultural and Biological Chemistry
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Agricultural and Biological Chemistry 40 (3), 475-483, 1976
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Keywords
Details 詳細情報について
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- CRID
- 1390282681442580864
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- NII Article ID
- 130003415887
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- COI
- 1:CAS:528:DyaE28XhslGlu7g%3D
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- ISSN
- 18811280
- 00021369
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- Text Lang
- en
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- Data Source
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- JaLC
- Crossref
- CiNii Articles
- OpenAIRE
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- Abstract License Flag
- Disallowed