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181.
Toru Nakayama Nobuyoshi Esaki Woon-Joo Lee Izumi Tanaka Hidehiko Tanaka Kenji Soda 《Bioscience, biotechnology, and biochemistry》2013,77(9):2367-2369
Four types of β-xylosidases from a concentrated culture filtrate of Pénicillium wortmanni IFO 7237, designated as xylosidase-1, -2, -3, and -4 were purified to homogeneity on SDS polyacrylamide gel electrophoresis by an alcohol precipitation, DEAE-Sephadex A-25 ion exchange chromatography, and isoelectric focusing. The molecular weights of xylosidase-1, -2, -3, and -4 were estimated to be 110,000, 195,000, 210,000, and 180,000 respectively and their isoelectric points to be 3.7, 4.28, 4.6, and 4.8. The pH optima of β-xylosidase activities were from 3 to 4.5. The optimum temperature for enzyme activities was from 55°C to 65°C. On the enzymic hydrolysis of phenyl ß-d- xyloside, the reaction product of each enzyme was found to be β-d-xylose with retention of configuration. All the four ß-xylosidases were free of α-xylosidase and ß-glucosidase activities. All the enzyme activities of four β-xylosidases were strongly inhibited by Hg2+ and N- bromosuccinimide. With respect to the hydrolysis patterns and HPLC analysis of hydrolyzates from xylooligosaccharides, xylosidase-2 was totally different from other three as a distinct enzyme. Xylosidase-1 was also in a separate group although xylosidase-3 and -4 showed closely related action patterns as a different group. 相似文献
182.
Yoshikazu Izumi Kuninori Sato Yoshiki Tani Koichi Ogata 《Bioscience, biotechnology, and biochemistry》2013,77(11):2683-2684
Vitamin B6 is synthesized by green Cytisus scoparius callus and green Phellodendron amurense callus cultured on Linsmaier and Skoog Agar-medium with 10?5m of ±-naphthaleneacetic acid (NAA) and 10?6 m of 6-benzyladenine (BA). Even when thiamine and inositol were omitted from this medium, the growth and vitamin B6 content of Cytisus scoparius callus did not change. Vitamin B6 contents of clones of the calluses varied and were unstable during long-term subculture. Clonal selection was repeated to obtain stable strains with high vitamin B6 content, and the vitamin B6 content of one strain of green Cytisus scoparius callus became 4-times higher than that of the green leaves. 相似文献
183.
Takuo Sakai Tatsurokuro Tochikura Koichi Ogata 《Bioscience, biotechnology, and biochemistry》2013,77(8):737-741
In this study, the authors developed a simplified method for the separation and the quantitative determination of nucleosides and bases, using paper electraophoretic technique. By this method, nucleosides and bases were well separated and determined in a fairly short time. Thus, this method was expected to be as accurate as the published methods and was believed to be a better method for both quantitative determination and detection of the nucleosides and bases in a large number of samples. 相似文献
184.
185.
Kichitaro Kawaguchi Koichi Ogata Tatsurokuro Tochikura 《Bioscience, biotechnology, and biochemistry》2013,77(6):908-918
Effects of various factors including incubation time, water content of airdried cells, concentration and pH of KH2PO4–K2HPO4 mixture, d-glucose concentration, MgSO4 concentration, GMP concentration, cell concentration, aeration and various kinds of carbohydrates on the fermentative production of GDP-mannose, GDP and GTP from 5′-GMP by air-dried cells of baker’s yeast were investigated. The water content of air-dried cells was the most important factor in the fermentation. When the air-dried cells of baker’s yeast (100 mg/ml) were incubated with 5′-GMP (20 μmoles/ml), d-glucose (800 μmoles/ml), potassium phosphate buffer (360 μmoles/ml, pH 7.0), and MgSO4 (20 μmoles/ml), 2-hr incubation gave GDP in 20% yield and GTP in 61.1% yield, GDP-mannose being produced in 45% yield after 8-hr incubation. The phosphorylation of 5′-AMP, 5′-dAMP, 5′-dGMP 5′-CMP and 5′-UMP was also observed in high yields under the same conditions. 相似文献
186.
Fusako Kawai Kensei Maezato Hideaki Yamada Koichi Ogata 《Bioscience, biotechnology, and biochemistry》2013,77(9):1675-1679
The formation of D-pantothenic acid-α-glucoside (PaA-α-G) was found from D-pantothenic acid (PaA) and maltose in incubation mixtures of microorganisms, especially Saccharomyces yeasts and Sporobolomyces coralliformis IFO 1032. The reaction conditions were investigated for formation of PaA-α-G by resting cells of Spor. coralliformis. The formation of the compound increased with PaA concentration (3~20 mg/ml). The yield was maximum at 5~10 mg/ml of PaA. Cetyl trimethyl ammonium bromide (0.1 %) promoted the formation of PaA-α-G. Sucrose was the optimal α-glucosyl donor. When 30 mg/ml of sucrose was fed to the reaction mixture (initial sucrose, 100 mg/ml; and PaA, 10 mg/ml) at 12-hr intervals, 5.74 mg/ml (3.30 mg/ml as PaA) of PaA-α-G was formed in 48-hr incubation at 28°C with shaking. PaA-α-G was also formed by yeast α-glucosidase, mold maltase and the cell-free extract of Spor. coralliformis. The compound showed approximately 9~10% and 0.1~0.3% (molar ratio) of activity of PaA for Saccharomyces carlsbergensis ATCC 9080 and Lactobacillus plantarum ATCC 8014, respectively. The compound had the same microbiological activity as authentic 4′-O-(α-D-glucopyranosyl)-D-pantothenic acid. 相似文献
187.
Kawai Fusako Yamada Hideaki Ogata Koichi 《Bioscience, biotechnology, and biochemistry》2013,77(11):1660-1667
Some properties of pyridoxine glucoside-synthesizing enzyme were studied using the partially and highly purified enzyme preparations from Micrococcus sp. No. 431.The enzyme was stable at pH 7.0 and between 0°C and 30°C. The maximal activity was obtained at pH 8.0 and 37°C. Besides sucrose, phenyl-α-d-glucoside and maltose served as glucosyl donor. Of vitamin B6 compounds tested, only pyridoxine served as glucosyl acceptor. The enzyme activity was inhibited by PCMB and heavy metal ions, and the inhibition was prevented by 2-mercaptoethanol, indicating the enzyme would be a sulfhydryl enzyme. The activity was not affected by chelating agents and not activated by metal ions. 相似文献
188.
Yoshiki Tani Koichi Ogata Masao Ukita Tsuyoshi Nakamatsu Yoshikazu Izumi 《Bioscience, biotechnology, and biochemistry》2013,77(2):173-197
Escherichia freundii alkaline phosphatase was found in a membrane fraction and was purified by procedures involving spheroplast formation with lysozyme and EDTA, and DEAE-cellulose and Sephadex G-150 column chromatographies. Then this enzyme along with other phosphatases was investigated on the ability to transfer the phosphoryl group from p-nitrophenyl phosphate to pyridoxine. It was found that the ability of the transphosphorylation varied with these phosphatases. The transphosphorylation to hydroxy compounds such as alcohols, sugars and nucleosides was also compared. Escherichia freundii acid phosphatase showed the highest activity of transphosphorylation among phosphatases tested. The mechanism of transphosphorylation was discussed.An enzyme, pyridoxamine 5′-phosphate transaminase, was purified from the cell-free extract of Clostridium kainantoi. The purification procedures involved ammonium sulfate fractionation, protamine sulfate treatment and, DEAE-cellulose, hydroxylapatite, DEAE-Sephadex and Sephadex G-200 column chromatographies. The purified enzyme, which had approximately 2700-fold higher specific activity over the original extract, showed a single schlieren pattern in the ultracentrifuge. From the spectral analysis, it seemed that pyridoxamine 5′-phosphate transaminase did not contain pyridoxal 5′-phosphate as a prosthetic group. It was recognized that the transamination was accelerated by the addition of amino acid and was inhibited by diisopropyl phosphofluoride. Glutamic acid formed in the reaction was identified to be a D-isomer. A study on the substrate specificity showed that the enzyme might be possible to be specific for pyridoxamine 5′-phosphate.The extracellular formation of vitamin B6 was searched in marine and terrestrial microorganisms. Two bacterial strains were selected and were identified as Vibrio and Flavobacterium, respectively. Marine microorganisms showed the considerable formation of vitamin B6 and the presence of vitamin B6 in sea water was also recognized. The cultural and reaction conditions for vitamin B6 formation by these strains were investigated. Glycerol was commonly the most effective compound on vitamin B6 formation among the compounds tested. It was suggested that both bacteria did not have the control system on vitamin B6 biosynthesis by the amount of possible end products. 相似文献
189.
Koichi Ogata Sakayu Shimizu Yoshiki Tani 《Bioscience, biotechnology, and biochemistry》2013,77(1):84-100
The ability of the formation of coenzyme A from pantothenic acid and cysteine in the presence of AMP or ATP was searched in yeasts and bacteria. The result of screening showed that the activity was found in several yeasts and the bacteria belonging to the genera Sarcina, Corynebacterium and Brevibacterium. Particularly, Brevibacterium ammoniagenes IFO 12071 (ATCC 6871) accumulated a large amount of coenzyme A.Isolation of the reaction products, which were synthesized by Brevibacterium ammoniagenes IFO 12071, were carried out. The isolates were identified as coenzyme A, dephosphocoenzyme A and phosphopantothenic acid.The possibility for the formation of coenzyme A in a larger amount from pantothenic acid and cysteine was investigated with baker’s yeast under the condition coupled with ATP-generating system.Effect of various factors affecting the accumulation of coenzyme A was investigated. Among them, glucose concentration and inorganic phosphorus concentration were the most important factors for its accumulation. Coenzyme A was not accumulated without the phosphorylation of AMP to ATP. Several cationic surfactants stimulated the accumulation of coenzyme A.The amount of coenzyme A accumulated reached about 200 μg per ml of the reaction mixture under the suitable reaction conditions employed. 相似文献
190.
Yoshikazu Izumi Kuninori Sato Yoshiki Tani Koichi Ogata 《Bioscience, biotechnology, and biochemistry》2013,77(6):1335-1340
The 7-keto-8-aminopelargonic acid (KAPA) synthetase activities of cell-free extracts from various bacteria were investigated. The experiments on the substrate specificity of KAPA synthetase, using crude cell-free extracts from bacteria having high enzyme activity, showed that l-serine and pyruvic acid could replace l-alanine, but that, when the enzyme was partially purified, these compounds were not effective. Many kinds of amino acids such as l-cysteine, l-serine, d-alanine, glycine, d-histidine, and l-histidine, inhibited the enzyme activity. This inhibition was found to be competitive with l-alanine. Pyridoxal 5′-phosphate, which is a cofactor of the enzyme, also inhibited the enzyme activity at high concentrations. The repression of KAPA synthetase by biotin occurred in Bacillus subtilis and B. sphaericus but not in Micrococcus roseus and Pseudomonas fluorescens, even at a concentration of 1000 mµg per ml of biotin. 相似文献