Properties of sorbitol dehydrogenase from Pseudomonas sp. KS-E1806 and comparison with other sorbitol dehydrogenases

Minamihara, Tomoyuki; Suzuki, Masaru

doi:10.1016/s0922-338x(97)82064-8

Cited by 9 publications

(6 citation statements)

References 13 publications

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“…This enzyme was stable from pH 5´5 to 10´5, and showed strict substrate speci®city at pH 9´0. 18 Furthermore, we modi®ed the method of deproteinization by using NaOH and ZnSO 4 , as shown by Shinohara et al 20 In our assay system we speeded the sample preparation by washing once with physiological saline and performed cell lysis with distilled water. In addition, we facilitated the step of deproteinization by using NaOH and ZnSO 4 instead of HClO 4 and K 2 CO 3 .…”

Section: Discussionmentioning

confidence: 99%

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Determination of D-sorbitol in human erythrocytes by an enzymatic fluorometric method with an improved deproteinization procedure

Umeda

Otsuka²,

Li³

et al. 2001

Ann Clin Biochem

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SUMMARY.We developed an improved enzymatic assay of D-sorbitol in human erythrocytes by employing highly speci®c D-sorbitol dehydrogenase from Pseudomonas sp. (EC 1.1.1.14) and replacing perchloric acid (HClO 4 ) and potassium carbonate (K 2 CO 3 ), generally used for deproteinization, with sodium hydroxide (NaOH) and zinc sulphate (ZnSO 4 ). In this assay, erythrocytes were separated from plasma by centrifugation and washed once with physiological saline. Subsequently, the erythrocytes were lysed with distilled water and proteins precipitated with NaOH and ZnSO 4 . After centrifugation, the resulting colourless supernatant was mixed with a glycine buffer (pH 9´0) containing NAD + and D-sorbitol dehydrogenase. After incubation for 30 min at 37°C, the NADH produced was measured uorimetrically. The¯uorescence intensities were corrected for sample blanks, and the values of D-sorbitol were normalized for haemoglobin content.The method had an analytical range of 1±180 mmol/L. The intra-and inter-assay precisions were < 3´3% and < 5´8%, respectively. The detection limit was 0´65 mmol/ L. In terms of the linearity, precision and sensitivity, the improved method using NaOH and ZnSO 4 was superior to the conventional method using HClO 4 and K 2 CO 3 .

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Section: Discussionmentioning

confidence: 99%

“…D-Sorbitol dehydrogenase (EC 1.1.1.14) 18 and NAD + (b-nicotinamide adenine dinucleotide) were purchased from Kikkoman Corporation (Noda, Japan) and Oriental Yeast Co. (Tokyo, Japan), respectively. D-Sorbitol and other chemicals (reagent grade) were obtained from Wako Pure Chemicals Industries Ltd (Osaka, Japan).…”

Section: Chemicalsmentioning

confidence: 99%

Determination of D-sorbitol in human erythrocytes by an enzymatic fluorometric method with an improved deproteinization procedure

Umeda

Otsuka²,

Li³

et al. 2001

Ann Clin Biochem

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“…specificity. 40 The novel approach presented here uses functionalized polyelectrolytes to fabricate bioelectronic interfaces that can be removed by a simple pH change and then reconstituted. For the enzymes tested, 2°ADH and SDH, the I cat sat , sensitivity, and TR max values of the reconstituted interface were comparable to those of the original.…”

Section: Resultsmentioning

confidence: 99%

“…KS-E1806 was provided by the Kikkoman Corp. (Chiba, Japan). 40 Chemicals. Tryptone, yeast extract, dithiothreitol (DTT), kanamycin, and ampicillin were purchased from Fisher Scientific (Pittsburgh, PA).…”

Section: Methodsmentioning

confidence: 99%

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Renewable Dehydrogenase-Based Interfaces for Bioelectronic Applications

et al. 2007

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Bioelectronic interfaces that establish electrical communication between redox enzymes and electrodes have potential applications as biosensors, biocatalytic reactors, and biological fuel cells. However, these interfaces contain labile components, including enzymes and cofactors, which have limited lifetimes and must be replaced periodically to allow long-term operation. Current methods to fabricate bioelectronic interfaces do not allow facile replacement of these components, thus limiting the useful lifetime of the interfaces. In this paper we describe a versatile new fabrication approach that binds the enzymes and cofactors using reversible ionic interactions. This approach allows the interface to be removed via a simple pH change and then replaced to fully regenerate the biocatalytic activity. The positively charged polyelectrolyte poly(ethylenimine) was used to ionically bond a dehydrogenase enzyme and its cofactor to a gold electrode that was functionalized with 3-mercaptopropionic acid and the electron mediator toluidine blue O. By reducing the pH, the surface-bound 3-mercaptopropionic acid was protonated, disrupting the ionic bonds and releasing the enzyme-modified polyelectrolyte. After neutralization, fresh enzyme and cofactor were bound, regenerating the bioelectronic interface. Cyclic voltammetry, chronoamperometry, constant potential amperometry, electrochemical impedance spectroscopy, and Fourier transform infrared spectroscopy analyses were used to characterize the bioelectronic interfaces. For the two enzymes tested (secondary alcohol dehydrogenase and sorbitol dehydrogenase) and their respective cofactors (beta-nicotinamide adenine dinucleotide phosphate and beta-nicotinamide adenine dinucleotide), the reconstituted interface exhibited a surface coverage, an electron-transfer coefficient, and a turnover rate similar to those of the original interface.

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Functional assignment of gene AAC16202.1 from Rhodobacter capsulatus SB1003: New insights into the bacterial SDR sorbitol dehydrogenases family

et al. 2012

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Properties of sorbitol dehydrogenase from Pseudomonas sp. KS-E1806 and comparison with other sorbitol dehydrogenases

Cited by 9 publications

References 13 publications

Determination of D-sorbitol in human erythrocytes by an enzymatic fluorometric method with an improved deproteinization procedure

Determination of D-sorbitol in human erythrocytes by an enzymatic fluorometric method with an improved deproteinization procedure

Renewable Dehydrogenase-Based Interfaces for Bioelectronic Applications

Functional assignment of gene AAC16202.1 from Rhodobacter capsulatus SB1003: New insights into the bacterial SDR sorbitol dehydrogenases family

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