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

Autores
Ano, Yoshitaka; Hours, Roque Alberto; Akakabe, Yoshihiko; Kataoka, Naoya; Yakushi, Toshiharu; Matsushita, Kazunobu; Adachi, Osao
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A novel oxidation of D-pentonates to 4-keto-D-pentonates was analyzed with Gluconobacter Thailandicus 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 Ca2+. 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 Gluconobacter species. The reaction versatility of quinoprotein GLDH was notified in this study.
Facultad de Ciencias Exactas
Centro de Investigación y Desarrollo en Fermentaciones Industriales
Materia
Ciencias Exactas
4-keto-D-arabonate production
4-keto-D-pentonate
Acetic acid bacteria
Glycerol dehydrogenase
Oxidative fermentation
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/87580
Acceder
id SEDICI_58b73da26a863f4f7f881bc5b28a8515
oai_identifier_str oai:sedici.unlp.edu.ar:10915/87580
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling 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-psicoseAno, YoshitakaHours, Roque AlbertoAkakabe, YoshihikoKataoka, NaoyaYakushi, ToshiharuMatsushita, KazunobuAdachi, OsaoCiencias Exactas4-keto-D-arabonate production4-keto-D-pentonateAcetic acid bacteriaGlycerol dehydrogenaseOxidative fermentationA 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.Facultad de Ciencias ExactasCentro de Investigación y Desarrollo en Fermentaciones Industriales2017info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf411-418http://sedici.unlp.edu.ar/handle/10915/87580enginfo:eu-repo/semantics/altIdentifier/issn/0916-8451info:eu-repo/semantics/altIdentifier/doi/10.1080/09168451.2016.1254535info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-10-22T16:58:06Zoai:sedici.unlp.edu.ar:10915/87580Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-22 16:58:06.86SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv 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 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
spellingShingle 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
Ano, Yoshitaka
Ciencias Exactas
4-keto-D-arabonate production
4-keto-D-pentonate
Acetic acid bacteria
Glycerol dehydrogenase
Oxidative fermentation
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
dc.creator.none.fl_str_mv Ano, Yoshitaka
Hours, Roque Alberto
Akakabe, Yoshihiko
Kataoka, Naoya
Yakushi, Toshiharu
Matsushita, Kazunobu
Adachi, Osao
author Ano, Yoshitaka
author_facet Ano, Yoshitaka
Hours, Roque Alberto
Akakabe, Yoshihiko
Kataoka, Naoya
Yakushi, Toshiharu
Matsushita, Kazunobu
Adachi, Osao
author_role author
author2 Hours, Roque Alberto
Akakabe, Yoshihiko
Kataoka, Naoya
Yakushi, Toshiharu
Matsushita, Kazunobu
Adachi, Osao
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
4-keto-D-arabonate production
4-keto-D-pentonate
Acetic acid bacteria
Glycerol dehydrogenase
Oxidative fermentation
topic Ciencias Exactas
4-keto-D-arabonate production
4-keto-D-pentonate
Acetic acid bacteria
Glycerol dehydrogenase
Oxidative fermentation
dc.description.none.fl_txt_mv 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.
Facultad de Ciencias Exactas
Centro de Investigación y Desarrollo en Fermentaciones Industriales
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.
publishDate 2017
dc.date.none.fl_str_mv 2017
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/87580
url http://sedici.unlp.edu.ar/handle/10915/87580
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0916-8451
info:eu-repo/semantics/altIdentifier/doi/10.1080/09168451.2016.1254535
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
411-418
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
_version_ 1846783200651640832
score 12.982451

Publicaciones similares