• Journal of the Korean Society of Food Science and Nutrition
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• v.27 no.4
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• pp.693-697
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• 1998

The influence of flavonols from onion skin on xanthine oxidase was investigated. Methanol extract was showed 12.8% of yield, 661.3mg% of flavonoids contents and 88.7% of inhibitory effect on xanthine oxidase F1 and F2 fractions were obtained from the methanol extract by ODS and Sephadex LH-20 chromatography. F1 and F2 fractions flavonols(3-OH free) identified by UV/visible spectroscopy. Inhibitory effect of F1 and F2 on xanthine oxidase were increased with increasing concentration. IC50s of F1 and F2 were 0.95$\mu\textrm{g}$ and 0.67$\mu\textrm{g}$, respectively. To confirm the specificity of F1 and F2 against xanthine oxidase, albumin was added to the reaction mixture. The inhibition of F1 and F2 may be due to specific binding to xanthine oxidase. The modes of their inhibitions were of mixed type with respect to xanthine as a substrate.

• Korean Journal of Microbiology
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• v.24 no.2
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• pp.141-146
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• 1986

To find the role of polyphenol oxidase in lignin biodegradation, chracteristics of extracellular polyphenol oxidase activity from Lentinus edodes JA01 was investigated. Polyphenol oxidase had its optimum activity at pH 4.5 and $45^{\circ}C$ respectively. Also, the enzyme was very unstable in various pHs and comparatively heat stable up to $60^{\circ}C$. In $lignosulfonate-NH_4$ salts medium, the growth rate of L.edodes JA 01 was relatively slow and polyphenol oxidase activity appeared 2 and 14 days after inoculation. No significant relationships were found between polyphenol oxidase activity and the amounts of lignosulfonate present in the culture medium.

• Journal of the Korean Society of Food Science and Nutrition
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• v.12 no.2
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• pp.57-61
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• 1983

The present study was undertaken to elucidate the effect of Serotonin and Norepinephrine on Aldehyde Oxidase activity in rabbit liver, in vitro. The results were as follows; 1. Aldehyde Oxidase was measured optimum substrate concentration at $5{\times}10^{-4}M$ and incubation time for 10 minutes. 2. Aldehyde Oxidase were inhibited by Serotonin and Norepinephrine. 3. It was observed that relationship between biogenic amines and substrate were competitive inhibition on Aldehyde Oxidase.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.6
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• pp.792-796
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• 1993

The synthesis alcohol-oxidase[EC 1.1.3.13] was investigated in the yeasts, Candida boidinii CBS 8106 and C. boidinii CBS 2428, during growth on different carbon sources. Alcohol-oxidase was undetectable in all strains submitted to the test in the mineral salts medium containing 1.0% glucose, but its production was rapidly increased when the carbon source was changed glucose to 1.0% methanol after 24hrs of incubation. When cells were grown on the various carbon sources (glucose, xylose, lactose, glycerol, galactose, saccharose, sorbose, lactic acid or acetic acid), the alcohol-oxidase activity was undetected. These carbon sources together with methanol yielded far better synthesis of alcohol-oxidase than in the case of carbon sources alone. Alcohol-oxidase was active towards alcohol of shorter alkyl-chain length than C5 and unsaturated alcohols. Its affinity for these alcohols decreased with the increasing length of the alkyl-chain. The apparent Km values for the methanol of Candida boidinii CBS 8106 and C. boidinii CBS 2428 were 1.96 and 1.21, respestively.

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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• 1999.11a
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• pp.147-150
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• 1999

In the case of immobilizing of glucose oxidase in organic polymer using electrosynthesis, the glucose oxidase obstructs charge transfer and mass transport during the film growth. This may lead to short chained polymer and/or make charge-coupling weak between the glucose oxidase and the backbone of the polymer. That is mainly due to insulating property and net chain of the glucose oxidase. Since being the case, it is useless to increase in amount of glucose oxidase more than reasonable in the synthetic solution. We establish qualitatively that amount of immobilization can be improved by adding a little ethanol in the synthetic solution. As ethanol was added by 0.1 rnol dm" in the synthetic solution, Michaelis-Menten constants of the resulting enzyme electrode decreased from 30.7 mmol $dm^{-3}$ to about 2 mmol $dm^{-3}$. That suggests increase in affinity of the enzyme electrode for glucose and in amount of the immobilized enzyme.zyme.

• Journal of Nutrition and Health
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• v.18 no.4
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• pp.312-317
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• 1985

This study was attempted to investigate the occurrence and the characteristics of ascorbic oxidase in cucumbers. Ascorbic acid oxidase was isolated from cucumbers and concentrated using ammonium sulfate precipitation. The results of this study are as follows ; 1) Ascorbic acid oxidase activity was detected in whole cucumber homogenate. 2) Highest amounts of ascorbic acid destroyed after 10 minutes' incubation of ascorbic acid oxidase with its substrate. 3) The optimum pH and temperature of this enzyme were found to be pH 6.5 and $40^{\circ}C$, respectively. 4) Ascorbic acid content in cucumber juice prepared using the cold water $(4^{\circ}C)$ was higher than that made with water at $30^{\circ}C$. 5) When orange juice ( pH 3.4 )was added, ascorbic acid destruction was completely ceased. (The ascorbic acid oxidase was inactivated at pH 3.9) Decreasing the temperature and pH are recommended to achieve maximum stability of ascorbic acid in preparing cucumber juice.

• Journal of the Korean Society of Food Science and Nutrition
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• v.25 no.6
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• pp.1069-1073
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• 1996

Inhibition of xanthine oxidase by seaweed extracts obtained from Undaria pinnatifida, Ecklonia stolonifera, Ecklonia cava, Laminaria japonica, Sargassum, Codiumfragile, Enteromorpha compressa and Porphyra tenera were investigated. Extracts of E. stolonifera and E. mua remarkably inhibited xanthine oxidase activity compared to those of other seaweed. The xanthine oxidase inhibitory activity of E. cava was higher than that of E. stolonifera. Diethyl ether extract from E. cava was more effective in the inhibition of xanthine oxidase than other solvent extracts. Two xanthine oxidase inhibitors(A-1 and A-2) from diethyl ether extract were isolated and purified by silica gel column chromatography, thin layer chromatography and high performance liquid chromatography. Xanthine oxidase inhibitory activities of these compounds were 27.8 and 48.1% per 0.4mg, respectively. The active compound A-2 had absorption peak at 420nm, 456nm and 467nm, which can be considered as siphonaxanthine.

• Korean Journal of Food Science and Technology
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• v.17 no.1
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• pp.37-40
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• 1985

The reactor performance of a coimmobilized glucose oxidase and catalase enzyme system was investigated. In the determination of efficiencies of glucose oxidase and catalase of dual, mixed and soluble systems, the dual type immobilized one was superior to either the soluble or to the mixed system. In the continuous plugflow bed reactor system of glucose oxidase and catalase, $k-d$, deactivation rare constant of glucose oxidase only and catalase/glucose oxidase = 10 were $1.12\;{\times}\;10^{-2}\;and\;2.17\;{\times}10^{-3}\;hr^{-1}$, respectively. In the effect of ${\tau}$, space time, the point of $O_2$ limitation is $5.5\;g{\cdot}hr/l$ in both catalase/glucose oxidase = 1 and 10. In the effect of $O_2$ concentration to reduce the $O_2$ diffusion limitation, it appeared that ${\tau}\;=\;8.3g{\cdot}r/l$ is the maximum point of $O_2$ concentration in both catalase/glucose oxidase = 1 and 10.

• Microbiology and Biotechnology Letters
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• v.21 no.4
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• pp.329-335
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• 1993

Ascorbate oxidase activity in various cucumber tissue extracts was highest in young fruit peeling. Cucumber callus was induced from young fruit peeling and callus cell lines were selected for more than 7 months, which porduced high levels of ascorbate oxidase and had a high growth rate. Induction of callus was optimized with Linsmaier-Skoog(LS) medium at 25$^{\circ}C$ in dark phase. Ascorbate oxidase activity reached a maximum at 5 days after transfer to LS basal liquid-medium ant then declined. The enzyme activity in callus cells was stimulated by addition of 10${\mu}$M $CuSO_4$ in the early logarithmic phase of growth. And also, adding 10${\mu}$M $CuSO_4$ at 3rd day 7th day of culture period, ascorbate oxidase activity in callus cells was maintained to high level. Maximum yield of ascorbate oxidase was found at the 25th day by flask shaking culture, but three-fold of ascorbate oxidase activity was obtained at the 16th day by jar fermentation.

• Microbiology and Biotechnology Letters
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• v.28 no.2
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• pp.92-96
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• 2000

Aspergillus sp. F184 was isolated from soil for the development of new xanthine oxidase inhibitor. This xanthine oxidase inhibitor was sequentially purified by filtration, HP-20 adsorption column chromatography, ethyl acetate extraction, silica gel column chromatography and crystallization, and was named as YUX 104. YUX 104 was identified to be 5,6-epoxy-2-hydroxy-3-methyl-2-cyclohexene-1,4-dione(terreic acid) by NMR and mass spectroscopic sudies.