Purification and Some Properties of an Erythrose Reductase from an<i>Aureobasidium</i>sp. Mutant

Ishizuka, Hiroaki; Tokuoka, Keiko; Sasaki, Takashi; Taniguchi, Hajime

doi:10.1271/bbb.56.941

Cited by 21 publications

(29 citation statements)

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“…Purification of ER-I and ER-III was achieved as described previously. 1,2) Before proteolytic digestion, the cysteinyl residues were reduced and alkylated. ER-I (1 nmole) and ER-III (3 nmole) were dissolved in 200 ml of deoxygenated 10 mM Tris-HCl/6 M urea (pH 8.0).…”

Section: Methodsmentioning

confidence: 99%

“…We characterized three isozymes of erythrose reductases (ER-I, ER-II, and ER-III) biochemically from Trichosporonoides megachiliensis SNG-42, one of the strains used for commercial production of erythritol. 1,2) In Candida magnoliae, partial amino acid sequences of the enzyme, which had erythrose reductase activity, have been reported, 3) but the entire primary structures and the corresponding cDNAs for ERs remain unknown. In this paper, we report the primary structure, cDNA isolation, and functional expression of erythrose reductases in Escherichia coli.…”

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confidence: 99%

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Primary Structure Analysis and Functional Expression of Erythrose Reductases from Erythritol-Producing Fungi (Trichosporonoides megachiliensisSNG-42)

Ookura

Azuma

Isshiki

et al. 2005

Bioscience, Biotechnology, and Biochemistry

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Section: Methodsmentioning

confidence: 99%

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confidence: 99%

Primary Structure Analysis and Functional Expression of Erythrose Reductases from Erythritol-Producing Fungi (Trichosporonoides megachiliensisSNG-42)

Ookura

Azuma

Isshiki

et al. 2005

Bioscience, Biotechnology, and Biochemistry

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“…Assay conditions used are exactly the same as those used in the previous paper (7). Briefly, the reductive activity was assayed by measuring the decrease in absorbance at 340 nm due to the oxidation of NADPH.…”

Section: Methodsmentioning

confidence: 99%

“…Protein on the electrophoresed gels was stained using a PhastGel Silver Kit from Pharmacia. Activity staining was carried out as shown in the previous paper (7).…”

Section: Methodsmentioning

confidence: 99%

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Comparison of three forms of erythrose reductase from an Aureobasidium sp. mutant.

Tokuoka

Ishizuka

Wako

et al. 1992

J. Gen. Appl. Microbiol.

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Two forms of erythrose reductave (ER-1 and ER-2) were purified from an Aureobasidium sp. mutant having high erythritol-producing activity besides the one (ER-3) reported previously. They were purified by chromatofocusing or hydrophobic chromatography after being separated from ER-3 on affinity chromatography. Physicochemical and enzymatic properties of the three forms were compared.Molecular weights were estimated to be 38,000 for ER-1 and 37,000 for ER-2 and ER-3 by SDS-PAGE. Isoelectric points of ER-1, ER-2, and ER-3 were 5.2, 5.0, and 4.8, respectively. All three forms behaved similarly toward pH and temperature, and showed maximum activity at pH 6.5 and 45°C. They showed essentially the same pH-and temperature-stability. D-Erythrose was the best substrate and D-glyceraldehyde, L-erythrulose, and dihydroxyacetone followed. No other aldose and ketose were reduced. There was no significant difference in the substrate specificity of the three forms. Their Km and Vmax for D-erythrose were found to be around 8 mM and 0.38-0.63 ,umol/min/mg, respectively. Significant differences were observed in the behavior of the three forms toward metal ions such as Ag+, Fe3+, and A13+. They showed no oxidative activity at neutral pH but showed some activity at alkaline conditions. Although the activity toward erythritol was much lower (less than 0.1%) compared with the reductive activity, the three forms showed remarkable diversity in pH-activity profile and substrate specificity.Aureobasidium sp. SN-G42 (6), a mutant isolated from Aureobasidium sp. SN-124A, is one of the strains used for commercial production of erythritol. This strain

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Erythritol production by yeasts: a snapshot of current knowledge

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Purification and Some Properties of an Erythrose Reductase from anAureobasidiumsp. Mutant

Cited by 21 publications

References 3 publications

Primary Structure Analysis and Functional Expression of Erythrose Reductases from Erythritol-Producing Fungi (Trichosporonoides megachiliensisSNG-42)

Primary Structure Analysis and Functional Expression of Erythrose Reductases from Erythritol-Producing Fungi (Trichosporonoides megachiliensisSNG-42)

Comparison of three forms of erythrose reductase from an Aureobasidium sp. mutant.

Erythritol production by yeasts: a snapshot of current knowledge

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