<scp>D</scp>‐Erythroascorbic acid is an important antioxidant molecule in<i>Saccharomyces cerevisiae</i>

Huh, Won-Ki; Lee, Byung‐Hoon; Kim, Seong-Tae; Kim, Yeon-Ran; Rhie, Gi‐eun; Baek, Yong-Woon; Hwang, Cheol-Sang; Lee, Jung Shin; Kang, Sa-Ouk

doi:10.1046/j.1365-2958.1998.01133.x

Cited by 103 publications

(80 citation statements)

References 51 publications

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“…However, yeast cells naturally lack the ability to produce Lascorbic acid. Instead, erythroascorbic acid, a structurally related compound with chemical properties very similar to those of L-ascorbic acid, is the molecule occurring in yeast cells (11).…”

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confidence: 99%

“…The structural motifs of the molecules changed during this conversion are identical to the structural motifs changed during the conversion of L-galactose via Gal to L-ascorbic acid. The corresponding enzymes have been purified and characterized in more detail (10,11,12,13). It was shown that the arabinono-1,4-lactone oxidases (ALOs) of Candida albicans and S. cerevisiae are able to convert not only L-arabinono-1,4-lactone but also Gal and Gul, among other structurally related lactones, in vitro; for C. albicans, it was shown that upon incubation of the cells with Gal, L-ascorbic acid accumulates in measurable amounts inside the cells (10), as well as in the culture medium (22,23).…”

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confidence: 99%

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Production ofl-Ascorbic Acid by Metabolically EngineeredSaccharomyces cerevisiaeandZygosaccharomyces bailii

Sauer

Branduardi

Valli

et al. 2004

Appl Environ Microbiol

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Production ofl-Ascorbic Acid by Metabolically EngineeredSaccharomyces cerevisiaeandZygosaccharomyces bailii

Sauer

Branduardi

Valli

et al. 2004

Appl Environ Microbiol

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“…These sequences have been identified by a BLAST search of the GenBank sequences as the closest homologues of GLO. There is hardly any information in the literature about the production of ascorbic acid analogues by prokaryotes, and the nonenzymatic defense system against free radicals is believed not to be essential for prokaryotic survival (10,17). It would be very interesting to investigate whether the oxidases of O. iheyensis, S. avermitilis, and B. cereus are indeed aldonic acid lactone specific and do produce ascorbic acid analogues.…”

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confidence: 99%

Cloning and Characterization of Gluconolactone Oxidase of Penicillium cyaneo-fulvum ATCC 10431 and Evaluation of Its Use for Production of d -Erythorbic Acid in Recombinant Pichia pastoris

Salusjärvi¹,

Kalkkinen

Miasnikov³

2004

Appl Environ Microbiol

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A D-erythorbic acid-forming soluble flavoprotein, gluconolactone oxidase (GLO), was purified from Penicillium cyaneo-fulvum strain ATCC 10431 and partially sequenced. Peptide sequences were used to isolate a cDNA clone encoding the enzyme. The cloned gene (accession no. AY576053) exhibits high levels of similarity with the genes encoding other known eukaryotic lactone oxidases and also with the genes encoding some putative prokaryotic lactone oxidases. Analysis of the coding sequence of the GLO gene indicated the presence of a typical secretion signal sequence at the N terminus of GLO. No other targeting or anchoring signals were found, suggesting that GLO is the first known lactone oxidase that is secreted rather than targeted to the membranes of the endoplasmic reticulum or mitochondria. Experimental evidence, including the N-terminal sequence of mature GLO and data on glycosylation and localization of the enzyme in native and recombinant hosts, supports this analysis. The GLO gene was expressed in Pichia pastoris, and recombinant GLO was produced by using the strong methanol-induced AOX1 promoter. In order to evaluate the suitability of purified GLO for production of D-erythorbic acid, we immobilized it on N-hydroxysuccinimide-activated Sepharose and found that the immobilized GLO retained full activity during immobilization but was rather unstable under reaction conditions. Our results show that both soluble and immobilized forms of GLO can, in principle, be used for production of D-erythorbic acid from D-glucono-␦-lactone or (in combination with glucose oxidase and catalase) from glucose. We also demonstrated the feasibility of glucose-D-erythorbic acid fermentation with recombinant strains coexpressing GLO and glucose oxidase genes, and we analyzed problems associated with construction of efficient D-erythorbic acid-producing hosts.D-Erythorbic acid (D-EA) (D-araboascorbic acid, isovitamin C) is a C-5 epimer of L-ascorbic acid. It has chemical properties very similar to those of ascorbic acid but very low vitamin C activity. D-EA and erythorbates have been used as food antioxidants for many years, particularly in processed meat and soft drinks. Currently, D-EA is manufactured by a two-step process; glucose is first converted into D-2-ketogluconic acid by fermentation, and this is followed by chemical lactonization similar to the lactonization of L-2-ketogulonic acid in the Reichstein process. In the early 1960s, direct conversion of glucose into D-EA by Penicillium fungi was discovered (48). This discovery was followed by an extensive mutagenesis and selection program that resulted in strains capable of converting glucose into D-EA with a yield of approximately 40% over a week-long fermentation (44, 56). These process parameters are still not sufficient to make the direct fermentation of glucose into D-EA economically feasible. In the last decade, much research effort has been spent on development of biotechnology-based processes for L-ascorbic acid manufacture (12,40). Most of the studies aimed at a two-s...

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“…11) These have been purified and well characterized in S. cerevisiae. ARA in S. cerevisiae has been reported to be a heterodimeric, cytosolic protein with a large subunit encoded by ARA1 (YBR149w), and a small subunit encoded by a yet-unidentified gene.…”

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“…10) ALO is a monomeric mitochondrial membrane protein encoded by ALO1 (YML086c). 11) Mutants deprived of either ara1 10) or alo1 11) have been reported to lack intracellular eAsA completely, so they are believed to be important exclusively in eAsA biosynthesis.…”

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NADP⁺-DependentD-Arabinose Dehydrogenase Shows a Limited Contribution to Erythroascorbic Acid Biosynthesis and Oxidative Stress Resistance inSaccharomyces cerevisiae

Amako

Fujita

Iwamoto

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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D‐Erythroascorbic acid is an important antioxidant molecule inSaccharomyces cerevisiae

Cited by 103 publications

References 51 publications

Production ofl-Ascorbic Acid by Metabolically EngineeredSaccharomyces cerevisiaeandZygosaccharomyces bailii

Production ofl-Ascorbic Acid by Metabolically EngineeredSaccharomyces cerevisiaeandZygosaccharomyces bailii

Cloning and Characterization of Gluconolactone Oxidase of Penicillium cyaneo-fulvum ATCC 10431 and Evaluation of Its Use for Production of d -Erythorbic Acid in Recombinant Pichia pastoris

NADP⁺-DependentD-Arabinose Dehydrogenase Shows a Limited Contribution to Erythroascorbic Acid Biosynthesis and Oxidative Stress Resistance inSaccharomyces cerevisiae

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D‐Erythroascorbic acid is an important antioxidant molecule inSaccharomyces cerevisiae

Cited by 103 publications

References 51 publications

Production ofl-Ascorbic Acid by Metabolically EngineeredSaccharomyces cerevisiaeandZygosaccharomyces bailii

Production ofl-Ascorbic Acid by Metabolically EngineeredSaccharomyces cerevisiaeandZygosaccharomyces bailii

Cloning and Characterization of Gluconolactone Oxidase of Penicillium cyaneo-fulvum ATCC 10431 and Evaluation of Its Use for Production of d -Erythorbic Acid in Recombinant Pichia pastoris

NADP+-DependentD-Arabinose Dehydrogenase Shows a Limited Contribution to Erythroascorbic Acid Biosynthesis and Oxidative Stress Resistance inSaccharomyces cerevisiae

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NADP⁺-DependentD-Arabinose Dehydrogenase Shows a Limited Contribution to Erythroascorbic Acid Biosynthesis and Oxidative Stress Resistance inSaccharomyces cerevisiae