Solubilization, Purification, and Properties of Membrane-Bound<scp>D</scp>-Glucono-δ-lactone Hydrolase from<i>Gluconobacter oxydans</i>

Shinagawa, Emiko; Ano, Yoshitaka; Yakushi, Toshiharu; Adachi, Osao; Matsushita, Kazunobu

doi:10.1271/bbb.80554

Cited by 18 publications

(11 citation statements)

References 22 publications

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“…D -GalA reductase, which catalyses the conversion of D -GalA to L -galactonic acid, is a soluble enzyme in non-climacteric strawberry fruits ( Agius et al , 2003 ) and Euglena ( Ishikawa et al , 2006 b ). On the other hand, though there is no report on aldonolactonase, which reversibly converts L -galactonic acid to L -galactono-1,4-lactone, in higher plants, similar enzymes exist in soluble fraction of rat ( Kondo et al , 2006 ) and Euglena ( Ishikawa et al , 2008 ), and in the membrane fraction of Gluconobacter ( Shinagawa, et al , 2009 ). Therefore, experiments were carried out to examine whether climacteric tomato fruit possesses D -GalA reductase and aldonolactonase activities in the soluble or insoluble fractions.…”

Section: Resultsmentioning

confidence: 99%

Translocation and the alternative D-galacturonate pathway contribute to increasing the ascorbate level in ripening tomato fruits together with the D-mannose/L-galactose pathway

Badejo

Wada

Gao

et al. 2011

Journal of Experimental Botany

150

114

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The D-mannose/L-galactose pathway for the biosynthesis of vitamin C (L-ascorbic acid; AsA) has greatly improved the understanding of this indispensable compound in plants, where it plays multifunctional roles. However, it is yet to be proven whether the same pathway holds for all the different organs of plants, especially the fruit-bearing plants, at different stages of development. Micro-Tom was used here to elucidate the mechanisms of AsA accumulation and regulation in tomato fruits. The mRNA expression of the genes in the D-mannose/L-galactose pathway were inversely correlated with increasing AsA content of Micro-Tom fruits during ripening. Feeding L-[6-14C]AsA to Micro-Tom plants revealed that the bulk of the label from AsA accumulated in the source leaf was transported to the immature green fruits, and the rate of translocation decreased as ripening progressed. L-Galactose feeding, but neither D-galacturonate nor L-gulono-1,4-lactone, enhanced the content of AsA in immature green fruit. On the other hand, L-galactose and D-galacturonate, but not L-gulono-1,4-lactone, resulted in an increase in the AsA content of red ripened fruits. Crude extract prepared from insoluble fractions of green and red fruits showed D-galacturonate reductase- and aldonolactonase-specific activities, the antepenultimate and penultimate enzymes, respectively, in the D-galacturonate pathway, in both fruits. Taken together, the present findings demonstrated that tomato fruits could switch between different sources for AsA supply depending on their ripening stages. The translocation from source leaves and biosynthesis via the D-mannose/L-galactose pathway are dominant sources in immature fruits, while the alternative D-galacturonate pathway contributes to AsA accumulation in ripened Micro-Tom fruits.

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Section: Resultsmentioning

confidence: 99%

Translocation and the alternative D-galacturonate pathway contribute to increasing the ascorbate level in ripening tomato fruits together with the D-mannose/L-galactose pathway

Badejo

Wada

Gao

et al. 2011

Journal of Experimental Botany

150

114

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“…A membrane-bound pyrroloquinoline quinone (PQQ)-dependent glucose dehydrogenase (mGDH) catalyzes the initial reaction linked to the generation of a proton motive force (25). The direct oxidation product, glucono-␦-lactone, is converted to gluconate, either spontaneously or enzymatically catalyzed by glucono-␦-lactonase (39). Further oxidation of gluconate by membrane-bound and respiratory-chain-coupled quinoprotein or flavoprotein dehydrogenases leads to the formation of 5-ketogluconate (5-KGA), 2-ketogluconate (2-KGA), and 2,5-diketogluconate (2,5-DKGA) (25).…”

Section: And N-formyl-1-amino-1-deoxy-d-sorbitolmentioning

confidence: 99%

Metabolic Engineering of Gluconobacter oxydans for Improved Growth Rate and Growth Yield on Glucose by Elimination of Gluconate Formation

Krajewski

Šimić²,

Mouncey³

et al. 2010

Appl Environ Microbiol

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Gluconobacter oxydans N44-1, an obligatory aerobic acetic acid bacterium, oxidizes glucose primarily in the periplasm to the end products 2-ketogluconate and 2,5-diketogluconate, with intermediate formation of gluconate. Only a minor part of the glucose (less than 10%) is metabolized in the cytoplasm after conversion to gluconate or after phosphorylation to glucose-6-phosphate via the only functional catabolic routes, the pentose phosphate pathway and the Entner-Doudoroff pathway. This unusual method of glucose metabolism results in a low growth yield. In order to improve it, we constructed mutants of strain N44-1 in which the gene encoding the membrane-bound glucose dehydrogenase was inactivated either alone or together with the gene encoding the cytoplasmic glucose dehydrogenase. The growth and product formation from glucose of the resulting strains, N44-1 mgdH::kan and N44-1 ⌬mgdH sgdH::kan, were analyzed. Both mutant strains completely consumed the glucose but produced neither gluconate nor the secondary products 2-ketogluconate and 2,5-diketogluconate. Instead, carbon dioxide formation of the mutants increased by a factor of 4 (N44-1 mgdH::kan) or 5.5 (N44-1 ⌬mgdH sgdH::kan), and significant amounts of acetate were produced, presumably by the activities of pyruvate decarboxylase and acetaldehyde dehydrogenase. Most importantly, the growth yields of the two mutants increased by 110% (N44-1 mgdH::kan) and 271% (N44-1 ⌬mgdH sgdH::kan). In addition, the growth rates improved by 39% (N44-1 mgdH::kan) and 78% (N44-1 ⌬mgdH sgdH::kan), respectively, compared to the parental strain. These results show that the conversion of glucose to gluconate and ketogluconates has a strong negative impact on the growth of G. oxydans.As the Gram-negative acetic acid bacterium Gluconobacter oxydans is able to oxidize sugars and sugar alcohols regioselectively, it is a valuable and versatile biocatalyst and has been used in industry for a long time, e.g., for the production of vitamin C via Reichstein synthesis (32) and of 1-deoxynojirimycin, a precursor of the antidiabetic drug miglitol (35). Both processes are combined biotechnological-chemical syntheses carried out on a large scale (10,35). The key biotechnological reactions in these two examples are the regioselective oxidation of D-sorbitol to L-sorbose and N-formyl-1-amino-1-deoxy-D-sorbitol to N-formyl-6-amino-6-deoxy-L-sorbose, respectively. The latter conversion is performed in whole-cell biotransformations with resting cells of G. oxydans as a catalyst.A characteristic trait of G. oxydans is the presence of parallel but spatially separated pathways for the oxidation of nonphosphorylated substrates and intermediates in both the periplasmic and cytoplasmic compartments (Fig.

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“…It can be oxidized further to either 2-keto-D-gluconate (2KGA) by an FAD-containing gluconate dehydrogenase (FAD-GADH) or 5-keto-D-gluconate (5KGA) by PQQ-glycerol dehydrogenase (PQQ-GLDH). In some AAB strains, 2KGA is later converted to 2,5-diketogluconate (2,5-diKGA) by FAD-containing 2KGA dehydrogenase (FAD-2KGADH) (Shinagawa, Ano, Yakushi, Adachi, & Matsushita, 2009;Toyama et al, 2007). Conversion of GA to its associated ketogluconates is both strain-and growth condition-dependent.…”

Section: Oxidative Fermentationmentioning

confidence: 99%

Physiology of Acetic Acid Bacteria and Their Role in Vinegar and Fermented Beverages

Lynch

Zannini

Wilkinson

et al. 2019

Comp Rev Food Sci Food Safe

152

139

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Acetic acid bacteria (AAB) have, for centuries, been important microorganisms in the production of fermented foods and beverages such as vinegar, kombucha, (water) kefir, and lambic beer. Their unique form of metabolism, known as “oxidative” fermentation, mediates the transformation of a variety of substrates into products, which are of importance in the food and beverage industry and beyond; the most well‐known of which is the oxidation of ethanol into acetic acid. Here, a comprehensive review of the physiology of AAB is presented, with particular emphasis on their importance in the production of vinegar and fermented beverages. In addition, particular reference is addressed toward Gluconobacter oxydans due to its biotechnological applications, such as its role in vitamin C production. The production of vinegar and fermented beverages in which AAB play an important role is discussed, followed by an examination of the literature relating to the health benefits associated with consumption of these products. AAB hold great promise for future exploitation, both due to increased consumer demand for traditional fermented beverages such as kombucha, and for the development of new types of products. Further studies on the health benefits related to the consumption of these fermented products and guidelines on assessing the safety of AAB for use as microbial food cultures (starter cultures) are, however, necessary in order to take full advantage of this important group of microorganisms.

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Solubilization, Purification, and Properties of Membrane-BoundD-Glucono-δ-lactone Hydrolase fromGluconobacter oxydans

Cited by 18 publications

References 22 publications

Translocation and the alternative D-galacturonate pathway contribute to increasing the ascorbate level in ripening tomato fruits together with the D-mannose/L-galactose pathway

Translocation and the alternative D-galacturonate pathway contribute to increasing the ascorbate level in ripening tomato fruits together with the D-mannose/L-galactose pathway

Metabolic Engineering of Gluconobacter oxydans for Improved Growth Rate and Growth Yield on Glucose by Elimination of Gluconate Formation

Physiology of Acetic Acid Bacteria and Their Role in Vinegar and Fermented Beverages

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