• Journal of Food Hygiene and Safety
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• v.14 no.4
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• pp.415-421
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• 1999

The flavin-containing monooxygenases (FMOs) (EC 1.14. 13.8) are NADPH-dependent flavoenzymes that catalyze oxidation of soft nucleophilic heteroatom centers in a range of structurally diverse compounds including foods, drugs, pesticides, and other xenobiotics. In humans, FMOl appears to be the predominant form expressed in human fetal liver. cDNA-expressed human FMO and human liver microsomal FMO have been observed to N- and S-oxy-genate nucleophilic nitrogen- and sulfur-containing drugs and chemicals, respectively. In the present study, FMOl can be expressed in the baculovirus expression vector system at level of 2.68 nmol FMOl/mg of membrane protein. This isoform was examined for its capacity to metabolize methimazole to its S-oxide using thiocholine assay. Kinetic studies of its S-oxide by recombinant human FMO1 result in Km of 7.66 $\mu$M and Vmax of 17.79 nmol/min/mg protein.

• Bulletin of the Korean Chemical Society
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• v.25 no.5
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• pp.625-628
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• 2004

Ceruloplasmin (CP), the blue oxidase present in all vertebrates, is the major copper-containing protein of plasma. It has been proposed that oxidation of L-3,4-dihydroxyphenylalanine (DOPA) may contribute to the pathogenesis of neurodegenerative disorders. The effect of the oxidized products of DOPA on the modification of human CP was investigated. When CP was incubated with the oxidized L-DOPA, the protein was induced to be aggregated and ferroxidase activity was decreased in a time-dependent manner. Radical scavengers and catalase significantly inhibited the oxidized DOPA-mediated CP aggregation. Copper chelatrors, Diethylenetriaminepenta acetic acid (DTPA) and Diethyldithiocarbamic acid (DDC), also inhibited the oxidative modification of CP. The results suggested that DOPA oxidation led to the formation of free radical and induced the CP aggregation.

• Journal of the Korean Society of Food Science and Nutrition
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• v.19 no.5
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• pp.387-394
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• 1990

The effect of lysine or methionine addition on the lipid oxidation and protein properties in casein-fish oil model system during the storage of 21 days at 37$^{\circ}C$ was studied. The peroxide and TBA values were increased markedly and the amino acids addition to the system caused to reduce the extent of lipid oxidation in comparison with that of casein-fish oil system which was a control group. Significant changes in fatty acid composition of each group were observed. Polyenoic acid contents were drastically decreased during the storage in the groups with and without the amino acids additions, . And also significant losses of several amino acids were occurred with the reduction of solubility and digestibility of casein during the storage. However no different effects were observed in both additionsof lysine and methionine to the system.

• BMB Reports
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• v.29 no.6
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• pp.513-518
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• 1996

A soluble protein from Saccharomyces cerevisiae specifically provides protection against a thiolcontaining oxidation system but not against an oxidation system without thiol. This 25-kDa protein was thus named thiol-dependent protector protein (TPP). The role of TPP in the cellular defense against oxidative stress was investigated in Escherichia coli containing an expression vector with a yeast genomic DNA fragment that encodes TPP (strain YP) and a mutant in which the catalytically essential amino acid in the active site of TPP (Cys-47) has been replaced with alanine by site-directed mutagenesis (strain YPC47A). There was a distinct difference between these two strains in regard to viability, modulation of activities of superoxide dismutase and catalase, and the oxidative damage of DNA upon exposure to menadione. These results suggest that TPP may play a direct role in the cellular defense against oxidative stress by functioning as an antioxidant protein.

• Archives of Pharmacal Research
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• v.16 no.2
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• pp.89-93
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• 1993

Incubation of $S(-)-^3H$-nicotine with rabbit lung microsomes in the presence of dioxygen and NADPH results in the formation of metabolities that bind covalently to microsomal macro-molecules. The addition of cytochrome P-450 monooxygenase inhibitors, $\alpha$-methylbenzyl ami-nobenzotriazole and aroclor 1260, inhibited both (S)-nicotine metabolism and covalent binding. The relative rates of oxidation of nicotine $\Delta^{1',5'}$ iminium ion to continine indicates that lung $100,000\times{g}$ supematant catalyzed this oxidation approximately 18 times slower than that of liver system based on mg of protein, and increased covalent interactions. Since than that of liver system based on mg of protein, nd increased covalent interactions. Since the activity of lung iminium oxidase appears much lowr than the liver, it is tempting to speculate that localized concentrations of nicotine $\Delta^{1',5'}$ iminium ion in the lung will survive for a longer period of time. These results support that cytochrome P-450 catalyzed oxidation of nicotine leads to the formation of reactive nad electrophilic intemediates capable of chemical interactions with biomacromolecules.

• Food Science of Animal Resources
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• v.34 no.3
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• pp.273-279
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• 2014

The objective of this study was to investigate the effects of the packaging method on the lipid and protein oxidation, and color in aged top round from Hanwoo (Korean native cattle) for 14 d at $4^{\circ}C$. Catalase activity was the highest (p<0.05) in vacuum packaging (VP) treatment during storage, and was higher (p<0.05) in 50% Ox-MAP and 50% Ox-MAP+vacuum skin packaging (VSP) treatments than in other treatments at d 14. Superoxide dismutase activity was higher (p<0.05) in VP, 50% Ox-MAP, and 50% Ox-MAP+VSP treatments than in other treatments at d 14. During storage, total antioxidant activity was the highest (p<0.05) in VP treatment and was higher (p<0.05) in 50% Ox-MAP+VSP treatment than in 80% Ox-MAP treatment. TBARS value was the lowest (p<0.05) in VP treatment during storage and was lower (p<0.05) in 50% Ox-MAP and Ox-MAP+VSP treatments than in 80% Ox-MAP and Ox-MAP treatments, respectively. Carbonyl content was the lowest (p<0.05) in VP treatment from 10 d. From 7 d, the $a^*$ value was the highest (p<0.05) in VP treatment and was higher (p<0.05) in 50% Ox-MAP and 50% Ox-MAP+VSP treatments than in other treatments. The $b^*$ value was the highest (p<0.05) in VP treatment from 3 d, and was higher (p<0.05) in 80% Ox-MAP+VSP, 50% Ox-MAP, and 50% Ox-MAP+ VSP treatments than in 80% Ox-MAP treatment at d 14. Therefore, VP improved the oxidation and red color stabilities in stored-aged top round compared with Ox-MAP. In addition, 50% Ox-MAP improved the lipid oxidation and red color stabilities compared with 80% Ox-MAP, and its inhibitory effect on lipid oxidation was enhanced by combination with VSP.

• Journal of the Korean Society of Food Science and Nutrition
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• v.28 no.1
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• pp.153-160
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• 1999

Storage stability of boiled and freeze dried loach and antioxidative effect of Zanthoxylum schinifolium were studied to confirm the possibility in development of instant choo o tang(Korean traditional loach soup). Packaging and storage temperature did not cause a measurable change in in vitro protein digestibility and trypsin indigestible substrate within 45 days of storage but remarkable quality changes were occurred in all samples stored after 60 days. Vacuum packaging and low temperature storage(4 oC) had some effect in retarding protein quality deterioration due to delaying polyunsaturated fatty acid oxidation. Maximum peroxide value and TBA value were reached in 15 days, and there were a slow(TBA value) and rapid reduction(POV) after peaks were reached. In contrast, increasing brown pigment development and fluorescence intensity continued until 90 days of storage. Treatment of ethanolic extracts from Zanthoxylum schinifolium prior to freeze drying could protect against lipid oxidation of freeze dried loach products.

• Food Science of Animal Resources
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• v.32 no.2
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• pp.212-219
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• 2012

The objective of this study was to investigate the effect of high pressure (HP) processing on shelf life, as well as the addition of phosvitin on lipid and protein oxidation stability of minced chicken leg meat. Minced chicken leg meat was mixed with yolk phosvitin at 500 or 1000 mg/kg meat levels, and divided into raw and cooked groups. Then, the samples were subjected to HP at 0.1, 300, and 600 MPa. The total aerobic bacteria, lipid and protein oxidation, along with instrumental meat color ($L^*$, $a^*$, and $b^*$value) of the samples were measured during storage for 7 d at $4^{\circ}C$. In raw meat, the number of total aerobic bacteria was decreased by HP at 300 MPa (4 Log reductions) and 600 MPa (5 Log reductions) after 7 d of storage (p<0.05). HP at 600 MPa increased lipid oxidation of samples at all storage days and protein oxidation of samples during storage at 3 and 7 d. HP induced the changes of meat color by increase of $L^*$ value and decrease of $a^*$ value (p<0.05). The total aerobic bacteria was not detected in the cooked samples, regardless of HP pressure, and the lipid or protein oxidation of the cooked sample treated by 600 MPa was higher than that of the control (0.1 MPa) on day 7 or control on day 3, respectively (p<0.05). The results suggested that HP can improve the shelf life of minced chicken leg meat. However, phosvitin might be a limited antioxidative agent for the improvement of oxidation stability induced by HP.

• Toxicological Research
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• v.25 no.4
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• pp.243-251
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• 2009

Present study was conducted to evaluate the anti oxidative activity of the Agrimonia pilosa-Ledeb leaves on non-lipid oxidative damage. The antioxidative activity of methanolic (MeOH) extract of the Agrimonia pilosa-Ledeb leaves on non-lipid oxidation, including liposome oxidation, deoxyribose oxidation, protein oxidation, chelating activity against metal ions, scavenging activity against hydrogen peroxide, scavenging activity against hydroxyl radical and 2'-deoxyguanosine (2'-dG) oxidation were investigated. The MeOH extract of the Agrimonia pilosa-Ledeb leaves exhibited high anti oxidative activity in the liposome model system. Deoxyribose peroxidation was inhibited by the MeOH extract of the Agrimonia pilosa-Ledeb leaves and MeOH extract of the Agrimonia pilosa-Ledeb leaves provided remarkable protection against damage to deoxyribose. Protective effect of MeOH extracts of the Agrimonia pilosa-Ledeb leaves on protein damage was observed at $600{\mu}g$ level (82.05%). The MeOH extracts of the Agrimonia pilosa-Ledeb leaves at $300{\mu}g$ revealed metal binding ability (32.64%) for hydrogen peroxide. Furthermore, the oxidation of 2'-deoxyguanosine (2'-dG) to 8-hydroxy-2-deoxyguanosine (8-OH-2'dG) was inhibited by MeOH extracts of the Agrimonia pilosa-Ledeb leaves and scavenging activity for hydroxyl radical exhibited a remarkable effect. From the results in the present study on biological model systems, we concluded that MeOH extract of the Agrimonia pilosa-Ledeb leaves was effective in the protection of non-lipids against various oxidative model systems.

• Food Science of Animal Resources
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• v.38 no.6
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• pp.1203-1215
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• 2018

The antioxidant effects of Allium hookeri root (AHR) were investigated by evaluating lipid and protein oxidation in meatballs during refrigerated storage at $4{\pm}1^{\circ}C$. AHR was mixed at concentrations of 0.5% (w/w, T2) and 1% (w/w, T3) with minced longissimus dorsi muscle. Meatballs containing AHR (T2 and T3) were compared to those containing 0.05% (w/w) ascorbic acid (T1) as a reference and without antioxidant as a control. The 2-thiobarbituric acid reactive substances (TBARS) value, disulfide bond formation, carbonyl contents, and volatile basic nitrogen (VBN) value of T2 were lower than those of the control during storage (p<0.05). The pH values of T2 and T3 were higher than that of the control (p<0.05). Texture profile analysis of T2 revealed a lower value compared to the control (p<0.05). Therefore, the VBN value, TBARS value, disulfide bond formation, and carbonyl content in meatball containing AHR were lower than those of the control meatball. These results indicate that AHR improves the quality of meat products and functions as an antioxidant.