• Food Science and Preservation
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• v.9 no.4
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• pp.369-374
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• 2002

This study was performed to investigate the effects of tyrosinase inhibition, xanthine oxidase inhibition and nitrite-scavenging effects of gamma-irradiated Schizandrae Fructus extracts from different solvents. Schizandrae Fructus was extracted by hot water, ethanol, acetone and methanol, and the extracts were irradiated 10, 20 and 30 kGy with gamma rays. All extracts from Schizandrae Fructus showed inhibition effect against tyrosinase. Tyrosinase inhibition effect of Schizandrae Fructus were higher in solvent extracts than hot water extracts by irradiation. The Schizandrae Fructus extracts had a higher inhibitory effect against xanthine oxidase, and the effect was not changed by irradiation. Nitrite scavenging activity, which was measured at various pH conditions (1.2, 3.0, 6.0), was the highest in Schizandrae Fructus extracts at pH 1.2 and 3.0. Hot water extracts provided higher nitrite scavenging effect than those of the methanol, ethanol and acetone extracts. Gamma-Irradiation may not influence on biological activites of the extracts when irradiated up to 30 kGy.

• Korean Journal of Food Science and Technology
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• v.29 no.6
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• pp.1075-1081
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• 1997

The objective of this research was to develop a glutamate enzyme sensor for rapid determinations of glutamate in samples. Glutamate oxidase was immobilized onto activated nylon, chitosan and other membranes. The enzymic and nonactin membranes were attached to an ammonia electrode to detect ammonia generated by the reaction between glutamate oxidase and glutamate. The enzyme immobilized on activated nylon membrane was stable for 2 months, and was able to perform about 250 glutamate determinations without losing activities. The enzyme immobilized on chitosan membrane had higher enzyme activity, but was not as much stable as that immobilized on nylon. The glutamate biosensor was able to accurately determine $0.1{\sim}5\;mM$ of glutamate in samples.

• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.1
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• pp.154-159
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• 1995

Inhibition of xanthine oxidase by tea extracts obtained from non-fermented tea(steamed green tea and roasted green tea), semi-fermented tea(oolong tea) and fermented tea(black tea) were investigated. The crude catechin fraciton had a hgher inhibitory effect against xanthine oxidase, and the effect was increased with the addition of tea extracts. Their inhibitory effect were hardly influenced until extracted three times with hot water. According to the investigation of catechins in the crude catechin fraction obtained from tea extracts, (-)-epicatechin-(EC), (-)-epicatechin gallate(ECg). (-)-epigallocatechin(EGC) and (-)-epigallocatechin gallate(EGCg) were 80.1$\mu\textrm{g}$/mg 113.5$\mu\textrm{g}$ /mg, 186.3$\mu\textrm{g}$/mg and 367.7$\mu\textrm{g}$/mg in steamed green tea, and 75.6$\mu\textrm{g}$/mg, 114.7$\mu\textrm{g}$/mg, 193.7 $\mu\textrm{g}$/mg and 381.9$\mu\textrm{g}$/mg in roasted green tea, and 69.4$\mu\textrm{g}$/mg, 110.0$\mu\textrm{g}$/mg, 127.1$\mu\textrm{g}$.mg and 464.9$\mu\textrm{g}$/mg in oolong tea, and 78.1$\mu\textrm{g}$/mg, 171.8$\mu\textrm{g}$/mg, 80.7$\mu\textrm{g}$/mg and 51.4$\mu\textrm{g}$/mg in black tea, respectively. Order of the content of these catechins was (-)-EGCg>(-)-EGC>(-)-ECg>(-)-EC in steamed green tea, roasted green tea and oolong tea, and was (-)-ECg>(-)-EGC>(-)-EC>(-)-EGCg in black tea. Also the concentration of catechins was hardly influeced until extracted three times. The inhibition ratio of xanthine oxidase by autherntic catechins was hardly influenced until extracted three times. The inhibition ratio of xanthine oxidase by authentic catechins was 94.9% and 87.6% by addition of 5.0$\mu\textrm{g}$/ml of (-)-EGCg and (-)-ECg, respectively. the inhibitors of xanthine oxidase were supposed to be due to (-)-ECg and (-)-EGCg in tea polyphenol compounds.

• Journal of the Korean Society of Food Science and Nutrition
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• v.17 no.3
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• pp.198-204
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• 1988

This study was aimed at obtaining elementary data on enzymatic browning of potato and potato products and examining the inhibitory method of browning. Therefore, we extracted polyphenol oxidase from potatoes(Solanum tubersum L.), and investigates its general properties and inhibiting effects of its activity with the different concentrations of sulfites($Na_2S_2O_4,\;Na_2SO_3{\cdot}7H_2O,\;NaHSO_3$). The optimum pH and temperature of polyphenol oxidase were observed to be 6.5 and $37^{\circ}C$ respectively. The polyphenol oxidase at PH5 was very stable, and the activity of polyphenol oxidase between pH $5.0{\sim}9.0$ was estimated to be relatively high, showing $72{\sim}75%$ of its activity at pH5. The polyphenol oxidase was very stable when heated at $40^{\circ}C$ for one hour, and almost 50% of enzyme activity was decreased when heated at $70^{\circ}C$ for twelve minutes. At 0.1mM concentrating of sulfites the relative activity of polyphenol oxidase was 98% in all the three cases of sulfites. Thus sulfites at 0.1mM concentration was found to have little inhibiting effect on polyphenol oxidase activity. At 1mM concentration of sulfites $NaHSO_3$ showed the lowest 36% relative activity among the three. At 5mM concentration of sulfites, the relative activity of $Na_2SO_3{\cdot}7H_2O$ was the lowest 14%.

• Archives of Pharmacal Research
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• v.10 no.1
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• pp.36-41
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• 1987

The conversion of xanthine dehydrogenase (type D) into xanthine oxidase (type D) was significantly increased in serum and liver of all $CCI_4$ treated rats on the necrosis and early cirrhosis stage of liver tissue. In the pretreatment of prednisolone, the ratio of type O per type O + D showed the decreasing tendency in serum, but the significant decrease in liver. In vitro, the conversion of liver xanthine oxidase from type D into type O was markedly increased by following preincubation with lysosomal fraction. The type conversion of xanthine oxidase may be caused by protelytic enzymes in lysosome.

• KSBB Journal
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• v.14 no.2
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• pp.235-240
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• 1999

Simple and rapid screening methods were developed to screen mutant strains of Trigonopsis variabilis ATCC10679 (TW). D-amino acid oxidase (D-AAO) from a mutant strain, T26, showed about 30% higher specific activity against cephalosporin C than from its wild type, TW. D-AAO genes from both TW and T26 strains were cloned and sequenced. There was one nucleotide changed from T to C at 811 position, resulting in an amino acid codon changed from Phe-258 to Ser-258.

• BMB Reports
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• v.28 no.3
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• pp.275-280
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• 1995

The respiratory burst oxidase of neutrophils is a multicomponent enzyme, domant in resting cells, that catalyzes the reduction of oxygen to $O_{2}^{-}$ at the expense of NADPH. In the resting neutrophil, some of the components of the oxidase, including proteins p47 and p67, are in the cytosol, while the rest are in the plasma membrane. Recent evidence has suggested that at least some of the cytosolic oxidase components exist as a complex. The cytosolic complex with a molecular weight of ~240 kDa was found to bind to blue-agarose and 2',5'-ADP-agarose, which recognize nucleotide requiring enzymes. In order to identify the nucleotide binding component of the cytosolic complex we purified recombinant p47 and p67 fusion proteins using the pGEX system. Pure recombinant p47 was retained completely on 2',5'-ADP-agarose, whereas pure recombinant p67 did not bind to these affinity beads. On the basis of these results, we infer that p47 may contain the nucleotide binding site.

• BMB Reports
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• v.30 no.2
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• pp.138-143
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• 1997

In order to assess controversial' proposals concerning the fatty acid-induced uncoupling of mitochondrial oxidative phosphorylation, we investigated the interaction of stearic acid with key mitochondrial proteins and measured the effect of stearic acid on the respiration of cytochrome c oxidase vesicles. Electron paramagnetic resonance spectra of spin-labeled stearic acid clearly demonstrated that cytochrome c oxidase interacts strongly with stearic acid. However, the respiration of detergent-solubilized cytochrome c oxidase was not altered significantly by stearic acid. Surprisingly, adenine nucleotide carrier, which was assumed to bind and translocate fatty acid anions in the Skulachev model of uncoupling, did not bind stearic acid at all. The respiration rate of cytochrome c oxidase vesicles was increased by ~70% in the presence of $20{\mu}m$ stearic acid and this uncoupling was attributed to a simple protonophoric effect of stearic acid.

• BMB Reports
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• v.33 no.4
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• pp.353-357
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• 2000

A new assay method of ${\alpha}-Oxidase$ (fatty acid : oxygen dioxygenase, 1-decarboxylating) was developed using a bioluminescence reaction system of marine luminous bacterium, Photobacterium phosphoreum. ${\alpha}$-Oxidase was isolated from a cucumber (Cucumis sativus). Pentadecanoic acid was used as a substrate, and the product, tetradecanal, was analyzed with a bacterial luciferase-coupled reaction. Initial light intensity was directly related to the concentration of tetradecanal in the range of 1 nM to 10 ${\mu}M$. Optimal pH and temperature were 7.5 and $25^{\circ}C$, respectively. Optimal pentadecanoic acid concentration in a standard assay of ${\alpha}$-oxidase was 0.1 mM. The Km value of pentedecanoic acid was $85{\mu}M$. This method is straightforward, rapid, convenient, and easy. Its needs no treatment or extraction of reaction mixture.

• The Korean Journal of Pharmacology
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• v.8 no.2
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• pp.41-47
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• 1972

Fluorides were supposed to exert a stimulatory action on the catecholamine release. In this study, the authors attempted to investigate the action of sodium fluoride on the catecholamine release from the isolated perfused cow adrenal gland and rat heart. And also the inhibitory effect of sodium fluoride on the monoamine oxidase activity in rat heart and liver mitochondria was investigated. The monoamine oxidase activity was measured by the conversion of benzylamine to benzaldehyde. The results obtained were follows; 1. Sodium fluoride stimulated the release of catecholamine from the isolated perfused cow adrenal gland and rat heart. 2. Sodium fluoride inhibited the rat heart and liver mitochondrial monoamine oxidase activity.