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Titolo:
Membrane-bound sugar alcohol dehydrogenase in acetic acid bacteria catalyzes L-ribulose formation and NAD-dependent ribitol dehydrogenase is independent of the oxidative fermentation
Autore:
Adachi, O; Fujii, Y; Ano, Y; Moonmangmee, D; Toyama, H; Shinagawa, E; Theeragool, G; Lotong, N; Matsushita, K;
Indirizzi:
Yamaguchi Univ, Fac Agr, Dept Biol Chem, Appl Microbiol Lab, Yamaguchi 7538515, Japan Yamaguchi Univ Yamaguchi Japan 7538515 iol Lab, Yamaguchi 7538515, Japan Ube Natl Coll Technol, Dept Biol & Chem Engn, Ube, Yamaguchi 7558555, Japan Ube Natl Coll Technol Ube Yamaguchi Japan 7558555 amaguchi 7558555, Japan Kasetsart Univ, Fac Sci, Dept Microbiol, Bangkok 10900, Thailand KasetsartUniv Bangkok Thailand 10900 Microbiol, Bangkok 10900, Thailand
Titolo Testata:
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
fascicolo: 1, volume: 65, anno: 2001,
pagine: 115 - 125
SICI:
0916-8451(200101)65:1<115:MSADIA>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
D-SORBITOL DEHYDROGENASE; D-MANNITOL DEHYDROGENASE; GLUCONOBACTER-SUBOXYDANS; PURIFICATION; CRYSTALLIZATION;
Keywords:
acetic acid bacteria; Gluconobacter suboxydans; oxidative fermentation; pentitol oxidation; ribitol dehydrogenase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Adachi, O Yamaguchi Univ, Fac Agr, Dept Biol Chem, Appl Microbiol Lab, Yamaguchi 7538515, Japan Yamaguchi Univ Yamaguchi Japan 7538515 amaguchi 7538515, Japan
Citazione:
O. Adachi et al., "Membrane-bound sugar alcohol dehydrogenase in acetic acid bacteria catalyzes L-ribulose formation and NAD-dependent ribitol dehydrogenase is independent of the oxidative fermentation", BIOS BIOT B, 65(1), 2001, pp. 115-125

Abstract

To identify the enzyme responsible for pentitol oxidation by acetic acid bacteria, two different ribitol oxidizing enzymes, one in the cytosolic fraction of NAD(P)-dependent and the other in the membrane fraction of NAD(P)-independent enzymes, were examined with respect to oxidative fermentation. The cytoplasmic NAD-dependent ribitol dehydrogenase (EC 1.1.1.56) was crystallized from Gluconobacter suboxydans IFO 12528 and found to be an enzyme having 100 kDa of molecular mass and 5s as the sedimentation constant, composed of four identical subunits of 25 kDa, The enzyme catalyzed a shuttle reversible oxidoreduction between ribitol and D-ribulose in the presence of NAD and NADH, respectively. Xylitol and L-arabitol were well oxidized by the enzyme with reaction rates comparable to ribitol oxidation, D-Ribulose, L-ribulose, and L-xylulose were well reduced by the enzyme in the presence of NADH as cosubstrates. The optimum pH of pentitol oxidation was found at alkaline pH such as 9.5-10.5 and ketopentose reduction was found at pH 6.0. NAD-Dependent ribitol dehydrogenase seemed to be specific to oxidoreduction between pentitols and ketopentoses and D-sorbitol and D-mannitol were not oxidized by this enzyme. However, no D-ribulose accumulation was observed outside the cells during the growth of the organism on ribitol, L-Ribulose wasaccumulated in the culture medium instead, as the direct oxidation productcatalyzed by a membrane-bound NAD(P)-independent ribitol dehydrogenase. Thus, the physiological role of NAD-dependent ribitol dehydrogenase was accounted to catalyze ribitol oxidation to D-ribulose in cytoplasm, taking D-ribulose to the pentose phosphate pathway after being phosphorylated, L-Ribulose outside the cells would be incorporated into the cytoplasm in several ways when need for carbon and energy sources made it necessary to use L-ribulose for their survival. From a series of simple experiments, membrane-boundsugar alcohol dehydrogenase was concluded to be the enzyme responsible forL-ribulose production in oxidative fermentation by acetic acid bacteria.

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Documento generato il 28/11/20 alle ore 23:03:02