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K Izumori

Publications and source records attributed to K Izumori.

At least 19 recordsLinked to original sources
PubMed2001

Cloning and characterization of a novel gene encoding L-ribose isomerase from Acinetobacter sp. strain DL-28 in Escherichia coli.

The gene encoding a novel L-ribose isomerase (L-RI) from Acinetobacter sp. was cloned into Escherichia coli and nucleotide sequence was determined. The gene corresponded to an open reading frame of 747 bp that codes for a deduced protein of 249 amino acids, which showed no amino acid sequence similarity with any other sugar isomerases. After expression of the gene in E. coli using pUC118 the recombinant L-RI was purified to homogeneity using different chromatographic methods. The overall enzymatic properties of the purified recombinant L-RI were the same as those of the authentic L-RI. To our knowledge, this is the first time report concerning the L-RI gene.

Acinetobacter↗
PubMed2001

Dietary D-psicose, a C-3 epimer of D-fructose, suppresses the activity of hepatic lipogenic enzymes in rats.

D-Psicose (D-ribo-2-hexulose), a C-3 epimer of D-fructose, is present in small quantities in commercial carbohydrate complexes or agricultural products. Wistar male rats were fed experimental diets which consisted of 5% D-psicose, cellulose, D-fructose or D-glucose for 28 days. Abdominal adipose tissue weight was significantly lower (P < 0.05) in rats fed the D-psicose diet than in rats fed a D-fructose and D-glucose diets, even though the four dietary groups were offered the same amount throughout the experimental period. Fatty acid synthase and glucose 6-phosphate dehydrogenase activities in the liver were significantly lower (P < 0.05) in rats fed the D-psicose diet than in rats fed the D-fructose and D-glucose diets. However, lipoprotein lipase activities in the heart, soleus muscle and perirenal adipose tissue were the same. These results suggest that a supplement of D-psicose in the diet suppresses hepatic lipogenic enzyme activities. The lower abdominal fat accumulation in rats fed a D-psicose diet might result from lower lipogenesis in the liver.

Abdomen↗
PubMed2001

Production of L-erythrose via L-erythrulose from erythritol using microbial and enzymatic reactions.

A rare aldotetrose, L-erythrose, was produced from erythritol via a two-step reaction. In the first step, complete oxidation of erythritol to L-erythrulose was achieved by using Gluconobacter frateurii IFO 3254. Washed cell suspension of the strain grown on tryptic soy broth (TSB) supplemented with 1% d-sorbitol was used to carry out the transformation reaction at 30 degrees C with shaking at 170 rpm. At 10% substrate concentration, 98% erythritol was converted to L-erythrulose within 48 h. The produced L-erythrulose was then used as a substrate for the production of L-erythrose. The isomerization of L-erythrulose to L-erythrose was carried out using constitutively produced L-ribose isomerase (l-RI) from the mutant strain Acinetobacter sp. DL-28 grown on D-lyxose mineral salt medium. At equilibrium, the yield of L-erythrose from L-erythrulose was 18% and finally 1.7 g L-erythrose was obtained from 10 g erythritol. After a number of simple purification steps, the product was isolated from the reaction mixture by ion-exchange column chromatography (Dowex 50W-X2, Ca2+). The structure of the product was determined after NaBH4 reduction from Infrared (IR) and 13C nuclear magnetic resonance (NMR) spectra.

Journal Article↗
PubMed2000

Mass production of D-psicose from d-fructose by a continuous bioreactor system using immobilized D-tagatose 3-epimerase.

An improved process for the mass production of D-psicose from D-fructose was developed. A D-fructose solution (60%, pH 7.0) was passed at 45 degrees C through a column filled with immobilized D-tagatose 3-epimerase (D-TE) which was produced using recombinant Escherichia coli, and 25% of the substrate was converted to D-psicose. After epimerization, the substrate, D-fructose, was removed by treatment with baker's yeast. The supernatant was concentrated to a syrup by evaporation under vacuum and D-psicose was crystallized with ethanol. Approximately 20 kg of pure crystal D-psicose was obtained in 60 d.

Journal Article↗
PubMed2000

Direct production of allitol from D-fructose by a coupling reaction using D-tagatose 3-epimerase, ribitol dehydrogenase and formate dehydrogenase.

Allitol was produced from D-fructose via a new NADH-regenerating enzymatic reaction system using D-tagatose 3-epimerase (D-TE), ribitol dehydrogenase (RDH), and formate dehydrogenase (FDH). D-fructose was epimerized to D-psicose by the D-TE of Pseudomonas cichorii ST-24 and the D-psicose was subsequently reduced to allitol by the RDH of an RDH-constitutive mutant, X-22, derived from Klebsiella pneumoniae IFO 3321. NADH regeneration for the reduction of D-psicose by the RDH was achieved by the irreversible formate dehydrogenase reaction, which allowed the D-psicose produced from d-fructose to be successively transformed to allitol with a production yield from D-fructose of almost 100%. The reactions progressed without any by-product formation. After separation of the product from the reaction mixture by a simple procedure, a crystal of allitol was obtained in a yield exceeding 90%. This crystal was characterized and determined to be allitol by HPLC analysis, its IR and NMR spectra, its melting point, and optical rotation measurement.

Journal Article↗
PubMed1999

Production of D-lyxose from D-glucose by microbial and enzymatic reactions.

D-arabitol was first prepared from D-glucose using Candida famata R28. The reaction gave 5.0% D-arabitol from 10.0% D-glucose. D-arabitol was then almost completely converted to D-xylulose using Acetobacter aceti IFO 3281. Finally, D-lyxose was prepared from D-xylulose enzymatically using L-ribose isomerase from toluene-treated cells of Acinetobacter sp. strain DL-28. The isomerization reaction progressed steadily and the concentration of D-xylulose increased from 1.0 to 10.0%. About 70% of D-xylulose was converted to D-lyxose in all cases. Separation of residual D-xylulose from the reaction mixture is very difficult to achieve by column chromatography, but D-xylulose could be selectively degraded easily using Saccharomyces cerevisiae IFO 0841. The product was crystallized and was confirmed to be D-lyxose by HPLC, 13C-NMR spectra, IR spectra analysis, and optical rotation measurement.

Journal Article↗
PubMed1999

Preparation of L-talose and D-gulose from L-tagatose and D-sorbose, respectively, using immobilized L-rhamnose isomerase.

L-rhamnose isomerase of Pseudomonas sp. LL172 immobilized on BCW 2603 Chitopearl beads was used to produce L-talose and D-gulose. At equilibrium, the production yields of L-talose and D-gulose were determined to be 12 and 10% from L-tagatose and D-sorbose, respectively. The crystallized products were confirmed by HPLC, IR and NMR spectra, and optical rotation measurement analyses.

Journal Article↗
PubMed1999

Production of D-iditol from D-sorbose by Rhodotolura rubra RY10 isolated from miso paste.

The yeast strain RY10 that can convert D-sorbose to D-iditol was isolated from miso paste and identified as Rhodotolura rubra. The cells grown on D-fructose were found to have relatively high conversion potential. Addition of ethanol to the reaction mixture significantly accelerated the conversion rate of D-sorbose to D-iditol. During the conversion reaction, ethanol was added to the reaction mixture at 48 h intervals to maintain the concentration of ethanol at 1.0%. The final conversion ratios were 82.7%, 95.0%, 93.7%, and 78.0% using washed cells when the concentration D-sorbose were 1.0%, 2.0%, 3.0% and 5.0%, respectively. The product produced from D-sorbose was identified as D-iditol by high performance liquid chromatography analysis, infrared spectrum, optical rotation and melting point measurements.

Journal Article↗
PubMed1999

Biochemical preparation of L-ribose and L-arabinose from ribitol: a new approach.

L-ribose and L-arabinose were prepared biochemically from ribitol via a two-step reaction, by which the complete oxidation of ribitol to L-ribulose (approximately 98%) was achieved by the reaction of washed cells of Acetobacter aceti IFO 3281. The produced L-ribulose was then used as a substrate for the production of L-ribose and L-arabinose. The isomerization of L-ribulose to L-ribose and L-arabinose was carried out using L-ribose isomerase (L-RI) of Acinetobacter sp. strain DL-28 and L-arabinose isomerase (L-AI) of Mycobacterium smegmatis, respectively. At equilibrium, the ratio of L-ribose: L-ribulose was 70:30 and that of L-arabinose: L-ribulose was 90: 10. After a simple purification treatment, both pentoses could be crystallized without the use of column chromatography. The crystals were confirmed as L-ribose and L-arabinose by High-performance liquid chromatography (HPLC), Infrared (IR), Nuclear magnetic resonance (NMR) and optical rotation measurements.

Journal Article↗
PubMed1996

Inhibition of glycoprotein processing by L-fructose and L-xylulose.

A number of unusual and rare carbohydrates were tested as potential inhibitors of various glycosidases, as well as inhibitors of N-linked oligosaccharide processing. The best inhibitors of several arylglycosidases and of glucosidase I were L-xylulose and L-fructose. Both of these sugars showed some inhibitory activity towards yeast alpha-glucosidase but were inactive against beta-glucosidase and other arylglycosidases. The inhibition of yeast alpha-glucosidase by L-xylulose was of a competitive nature and required a concentration of 1 x 10(-5) M for 50% inhibition. Both L-xylulose and L-fructose also inhibited the purified soybean glucosidase I, with 50% inhibition occurring at about 1 x 10(-4) M, but showed no inhibitory activity against soybean glucosidase II. When influenza virus-infected MDCK cells were raised in the presence of L-xylulose, there was a dose-dependent inhibition in the formation of complex types of oligosaccharides on the viral glycoproteins consistent with the inhibition of the processing glucosidase I. This inhibition resulted in the occurrence of oligosaccharides on the viral glycoproteins that were characterized as Glc3Man9(GlcNAc)2 structures. L-Fructose also inhibited glycoprotein processing in cell culture, and the inhibition resulted in the formation of similar oligosaccharides to those seen with L-xylulose. However, L-fructose was a poorer inhibitor than L-xylulose and required much higher concentrations for the same degree of inhibition. Neither of these compounds inhibited protein synthesis or the formation of lipid-linked saccharides in culture MDCK cells, even when tested at concentrations of 5 mg/ml (about 30 mM) of culture media.

Animals↗
PubMed1984

Production of d-Tagatose from Dulcitol by Arthrobacter globiformis.

A process for the bacterial oxidation of dulcitol to d-tagatose has been developed. The strain Arthrobacter globiformis ST48 used in this fermentation was isolated from soil. The yield of d-tagatose accumulated in the medium from dulcitol was as high as 85%. About 14 g of d-tagatose crystals was isolated from 1 liter of 2% dulcitol medium.

Journal Article↗
PubMed1982

D-Ribose isomerase.

Explore the source record for details and available documents.

Aldose-Ketose Isomerases↗
PubMed1978

Pentose metabolism in Mycobacterium smegmatis: comparison of L-arabinose isomerases induced by L-arabinose and D-galactose.

D-Galactose, which did not serve as a growth substrate, was found to induce an L-arabinose isomerase of similar properties to the L-arabinose-induced L-arabinose isomerase. In both cases the pH profiles, pH stability, optimum temperature, heat stability, substrate specificity, metal ion requirements, mobility on polyacrylamide gel electrophoresis, and kinetic properties of the induced isomerases were identical. It appears possible that D-galactose was incorporated into the cells by an L-arabinose permease system that was alos induced by D-galactose.

Arabinose↗
PubMed1978

Selective inhibition of Klebsiella aerogenes growth on pentoses by pentitols.

Selective inhibition of growth by pentitols was observed when Klebsiella aerogenes M-7 which could not utilize pentitols was grown on pentoses. D-Arabitol inhibited the growth on D-arabinose as a sole carbon source, but had no effect on the growth on L-arabinose, D-xylose, and D-ribose. Similarly, L-arabitol inhibited the growth on D-arabinose and L-arabinose, ribitol inhibited the growth on D-arabinose and L-arabinose, and xylitol inhibited the growth on D-xylose. From the following reasons, we postulated that the selective growth inhibition by pentitols was due to the competitive inhibition of pentose isomerase reaction by the cell by pentitols. (i) D-Arabinose transport activity was not inhibited by pentitols. (ii) Induction of D-arabinose and L-arabinose isomerases was not inhibited by D- and L-arabitol, respectively. (iii) The specificity of growth inhibition by pentitols was the same as that of competitive inhibition of pentose isomerases by pentitols.

Arabinose↗
PubMed1976

Evidence that the isomerization of D-ribose and L-rhamnose is catalyzed by the same enzyme in Mycobacterium smegmatis.

D-Ribose isomerase was purified and crystallized from cells of Mycobacterium smegmatis grown on either D-ribose or L-rhamnose. Isomerase activity for both of these sugars remained together throughout the purification. The isomerase from L-rhamnose-grown cells had the same chemical and physical properties as the enzyme isolated from D-ribose grown cells. In addition, immunological studies indicated that both activities were in the same protein since antisera prepared against either of the crystals cross-reacted with the other and gave lines of symmetry by the agar gel diffusion method.

Carbohydrate Epimerases↗
PubMed1976

Pentose metabolism in Mycobacterium smegmatis: specificity of induction of pentose isomerases.

The induction of D-xylose, D-ribose, L-arabinose, and D-lyxose isomerases by various sugars was studied to determine the configuration necessary for induction. D-Xylose isomerase was only induced by D-xylose, whereas D-ribose isomerase was induced by D-ribose, L-rhamnose, and L-lyxose. L-arabinose isomerase was induced by L-arabinose, D-galactose, L-arabitol, D-fucose, and dulcitol, whereas D-lyxose isomerase was induced by D-lyxose, D-mannose, D-ribose, dulcitol, and myoinositol. Some compounds such as dulcitol, D-galactose, and D- or L-fucose which do not support growth are still able to serve as inducers for various pentose isomerases.

Arabinose↗
PubMed1975

Purification, crystallization, and properties of D-ribose isomerase from Mycobacterium smegmatis.

D-Ribose isomerase, which catalyzes the conversion of D-ribose to D-ribulose, was purified from extracts of Mycobacterium smegmatis grown on D-ribose. The purified enzyme crystalized as hexagonal plates from a 44% solution of ammonium sulfate. The enzyme was homogenous by disc gel electrophoresis and ultracentrifugal analysis. The molecular weight of the enzyme was between 145,000 and 174,000 by sedimentation equilibrium analysis. Its sedimentation constant of 8.7 S indicates it is globular. On the basis of sodium dodecyl sulfate gel electrophoresis in the presence of Mn2+, the enzyme is probably composed of 4 identical subunits of molecular weight about 42,000 to 44,000. The enzyme was specific for sugars having the same configuration as D-ribose at carbon atoms 1 to 3. Thus, the enzyme could also utilize L-lyxose, D-allose, and L-rhamnose as substrates. The Km for D-ribose was 4 mM and for L-lyxose it was 5.3 mM. The enzyme required a divalent cation for activity with optimum activity being shown with Mn2+. the Km for the various cations was as follows: Mn2+, 1 times 10(-7) M, Co2+, 4 times 10(-7) M, and Mg2+, 1.8 times 10(-5) M. The pH optimum for the enzyme was 7.5 to 8.5. Polyols did not inhibit the enzyme to any great extent. The product of the reaction was identified as D-ribulose by thin layer chromatography and by preparation of the O-nitrophenylhydrazone derivative.

Aldose-Ketose Isomerases↗