Membrane-bound glycerol dehydrogenase catalyzes oxidation of D-pentonates to 4-keto-D-pentonates, D-fructose to 5-keto-D-fructose, and D-psicose to 5-keto-D-psicose
A novel oxidation of D-pentonates to 4-keto-D-pentonates was analyzed with <i>Gluconobacter Thailandicus</i> NBRC 3258. D-Pentonate 4-dehydrogenase activity in the membrane fraction was readily inactivated by EDTA and it was reactivated by the addition of PQQ and Ca<sup>2+</sup&...
Autores principales: | , , , , , , |
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Formato: | Articulo |
Lenguaje: | Inglés |
Publicado: |
2017
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Acceso en línea: | http://sedici.unlp.edu.ar/handle/10915/87580 |
Aporte de: |
id |
I19-R120-10915-87580 |
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record_format |
dspace |
institution |
Universidad Nacional de La Plata |
institution_str |
I-19 |
repository_str |
R-120 |
collection |
SEDICI (UNLP) |
language |
Inglés |
topic |
Ciencias Exactas 4-keto-D-arabonate production 4-keto-D-pentonate Acetic acid bacteria Glycerol dehydrogenase Oxidative fermentation |
spellingShingle |
Ciencias Exactas 4-keto-D-arabonate production 4-keto-D-pentonate Acetic acid bacteria Glycerol dehydrogenase Oxidative fermentation Ano, Yoshitaka Hours, Roque Alberto Akakabe, Yoshihiko Kataoka, Naoya Yakushi, Toshiharu Matsushita, Kazunobu Adachi, Osao Membrane-bound glycerol dehydrogenase catalyzes oxidation of D-pentonates to 4-keto-D-pentonates, D-fructose to 5-keto-D-fructose, and D-psicose to 5-keto-D-psicose |
topic_facet |
Ciencias Exactas 4-keto-D-arabonate production 4-keto-D-pentonate Acetic acid bacteria Glycerol dehydrogenase Oxidative fermentation |
description |
A novel oxidation of D-pentonates to 4-keto-D-pentonates was analyzed with <i>Gluconobacter Thailandicus</i> NBRC 3258. D-Pentonate 4-dehydrogenase activity in the membrane fraction was readily inactivated by EDTA and it was reactivated by the addition of PQQ and Ca<sup>2+</sup>. D-Pentonate 4-dehydrogenase was purified to two different subunits, 80 and 14 kDa. The absorption spectrum of the purified enzyme showed no typical absorbance over the visible regions. The enzyme oxidized D-pentonates to 4-keto-D-pentonates at the optimum pH of 4.0. In addition, the enzyme oxidized D-fructose to 5-keto-D-fructose, D-psicose to 5-keto-D-psicose, including the other polyols such as, glycerol, D-ribitol, D-arabitol, and D-sorbitol. Thus, D-pentonate 4-dehydrogenase was found to be identical with glycerol dehydrogenase (GLDH), a major polyol dehydrogenase in <i>Gluconobacter</i> species. The reaction versatility of quinoprotein GLDH was notified in this study. |
format |
Articulo Articulo |
author |
Ano, Yoshitaka Hours, Roque Alberto Akakabe, Yoshihiko Kataoka, Naoya Yakushi, Toshiharu Matsushita, Kazunobu Adachi, Osao |
author_facet |
Ano, Yoshitaka Hours, Roque Alberto Akakabe, Yoshihiko Kataoka, Naoya Yakushi, Toshiharu Matsushita, Kazunobu Adachi, Osao |
author_sort |
Ano, Yoshitaka |
title |
Membrane-bound glycerol dehydrogenase catalyzes oxidation of D-pentonates to 4-keto-D-pentonates, D-fructose to 5-keto-D-fructose, and D-psicose to 5-keto-D-psicose |
title_short |
Membrane-bound glycerol dehydrogenase catalyzes oxidation of D-pentonates to 4-keto-D-pentonates, D-fructose to 5-keto-D-fructose, and D-psicose to 5-keto-D-psicose |
title_full |
Membrane-bound glycerol dehydrogenase catalyzes oxidation of D-pentonates to 4-keto-D-pentonates, D-fructose to 5-keto-D-fructose, and D-psicose to 5-keto-D-psicose |
title_fullStr |
Membrane-bound glycerol dehydrogenase catalyzes oxidation of D-pentonates to 4-keto-D-pentonates, D-fructose to 5-keto-D-fructose, and D-psicose to 5-keto-D-psicose |
title_full_unstemmed |
Membrane-bound glycerol dehydrogenase catalyzes oxidation of D-pentonates to 4-keto-D-pentonates, D-fructose to 5-keto-D-fructose, and D-psicose to 5-keto-D-psicose |
title_sort |
membrane-bound glycerol dehydrogenase catalyzes oxidation of d-pentonates to 4-keto-d-pentonates, d-fructose to 5-keto-d-fructose, and d-psicose to 5-keto-d-psicose |
publishDate |
2017 |
url |
http://sedici.unlp.edu.ar/handle/10915/87580 |
work_keys_str_mv |
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bdutipo_str |
Repositorios |
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1764820490219683840 |