• Journal of the Korean Society of Food Science and Nutrition
• /
• v.32 no.7
• /
• pp.1046-1052
• /
• 2003

Viscoelastic behavior of oxidized starch gel, modified with sodium hypochlorite (NaOCl) and the adding effects of protein in oxidized starch gel was studied by dynamic viscoelastic measurement. The storage modulus(G′) of starch gel increased with the increase of starch concentration. They showed higher value when starch suspension was treated to 95$^{\circ}C$ rather than 85$^{\circ}C$. Consistency of starch gel was decreased over 1.0% active Cl/g starch when heated to 95$^{\circ}C$, which means that the swelling of starch granules increased with concentration of NaOCl and showed more sensitive against shear. As the extent of oxidation increased, starch granules were easily destroyed. Therefore, it is hard to separate between compartment of leached-out amylose and that of amylopectin, which means that the ability of gel formation was reduced. When oxidized starches were gelatinized in presence of soy protein and sodium caseinate, it was found that G′ decreased, and frequency dependence of G′ and G" increased with the increased degree of oxidation in starch. The reduce of starch-protein interaction was thought to be through the dissociation of the branched amylopectin, which playa leading role in protein interaction, with the oxidation of starch.

• Korean Journal of Food Science and Technology
• /
• v.31 no.1
• /
• pp.62-67
• /
• 1999

Periodate-oxidized soluble starch and maltohexaose, maltotetraose, maltose, and glyceraldehyde reacted with sweet potato ${\beta}-amylase$, wheat ${\beta}-amylase$, aldolase, bovine serum albumin, catalase, carboxypeptidase, ferritin and pronase. Electrophoretical mobility of modified proteins was different from that of native proteins, and modified proteins were stained with periodic acid-Schiff while native proteins did not stain. This results means that oxidized sugars attached on proteins. This bond is based on the Schiffs base between CHO group of oxidized sugar and ${\varepsilon}-NH_2$ group of lysine of protein. There is no changed UV absorption spectrum of sweet potato ${\beta}-amylase$ modified with oxidized soluble starch, in comparison with native enzyme.

• Korean Journal of Food Science and Technology
• /
• v.31 no.2
• /
• pp.482-487
• /
• 1999

Periodate-oxidized soluble starch and maltohexaose reacted with ${\alpha}-NH_2$ group of free amino acids and ${\varepsilon}-NH_2$ group of peptidyl lysine. The result shows that periodate-oxidized soluble starch and maltooligosaccharides reacted with protein and formed Schiff base between CHO group of oxidized sugar and ${\varepsilon}-NH_2$ group of surface lysine of protein molecule. Carbon and hydrogen composition of sweet potato ${\beta}-amylase$ modified with oxidized soluble starch increased and it's nitrogen composition decreased. Carbohydrate contents of sweet potato ${\beta}-amylase$ modified with oxidized soluble starch were 13.2% (pentamer), 13.4% (monomer), and with oxidized maltohexaose were 9.7% (pentamer), 9.3% (monomer) by $phenol-H_2SO_4$ method. Alpha-amino group of N-terminal, and ${\varepsilon}-NH_2$ group of lysine, of sweet potato ${\beta}-amylase$ were reacted with oxidized soluble starch by dinitrophenylation were 70% (pentamer), 73% (monomer) and 33% (pentamer), 26% (monomer), respectively, in comparison with native enzyme.

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

• Bulletin of the Korean Chemical Society
• /
• v.26 no.8
• /
• pp.1255-1259
• /
• 2005

Lewy bodies (LBs) are neuronal inclusions that are closely related to Parkinson's disease (PD). The filamentous component of LB from patients with PD contains biochemically altered $\alpha$-synuclein. We have investigated the effect of the oxidized products of catecholamines on the modification of $\alpha$-synuclein. When $\alpha$-synuclein was incubated with the oxidized 3,4-dihydroxyphenylalanine (L-DOPA) or dopamine, the protein was induced to be aggregated. The oxidized catecholamine-mediated $\alpha$-synuclein aggregation was enhanced by copper ion. Radical scavengers, azide and N-acetyl cysteine significantly prevented the oxidized catecholamine-mediated $\alpha$-synuclein aggregation. The results suggest that free radical may play a role in $\alpha$-synuclein aggregation. Exposure of $\alpha$-synuclein to the oxidized products of catecholamines led to the formation of dityrosine. Antioxidant dipeptides carnosine, homocarnosine and anserine significantly protected $\alpha$-synuclein from the aggregation induced by the oxidized products of catecholamines.

• Animal Bioscience
• /
• v.34 no.4
• /
• pp.724-733
• /
• 2021

Objective: The objectives of this study were to investigate the direct antioxidative effect of 90 Kda heat shock protein (Hsp90) obtained from duck muscle. Methods: The interaction of Hsp90 with phospholipids and oxidized phospholipids was studied with surface plasmon resonance (SPR), and their further oxidation in the presence of Hsp90 was evaluated with thiobarbituric acid reactive substances (TBARS) assay. The scavenging effect on the 1,1-diphenyl-2-picrylhydrazyl (DPPH) and 2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonic acid (ABTS) was measured, and the electron paramagnetic resonance (EPR) spectroscopy in combination with 5-tert-Butoxycarbonyl-5-methyl-1-pyrroline-N-oxide and 2-phenyl-4,4,5,5,-tetramethylimidazoline-1-oxyl-3-oxide (PTIO) was utilized to determine the abilities of Hsp90 in scavenging hydroxyl and PTIO radicals. Results: SPR showed Hsp90 could bind with both phospholipids and oxidized phospholipids, and prevent their further oxidation by the TBARS assay. The DPPH and ABTS scavenging activity increased with Hsp90 concentration, and could reach 27% and 20% respectively at the protein concentration of 50 μM. The EPR spectra demonstrated Hsp90 could directly scavenge ·OH and PTIO· radicals. Conclusion: This suggests that Hsp90, a natural antioxidant in meat, may play an important role in cellular defense against oxidative stress, and may have potential use in meat products.

• Mass Spectrometry Letters
• /
• v.3 no.1
• /
• pp.10-14
• /
• 2012

Artificially oxidized cysteine residues in peroxiredoxin 6 (Prx6) were detected by electrospray interface capillary liquid chromatography-linear ion trap mass spectrometry after the preparation of two-dimensional gel electrophoresis (2D-GE). We used Prx6 as a model protein because it possesses only two cysteine residues at the 47th and 91st positions. The spot of Prx6 on 2D-GE undergoes a basic (isoelectric point, pI 6.6) to acidic (pI 6.2) shift by exposure to peroxide due to selective overoxidation of the active-site cysteine Cys-47 but not of Cys-91. However, we detected a tryptic peptide containing cysteine sulfonic acid at the 47th position from the basic spot and a peptide containing both oxidized Cys-47 and oxidized Cys-91 from the acidic spot of Prx6 after the separation by 2D-GE. We prepared two types of oxidized Prx6s: carrying oxidized Cys-47 (single oxidized Prx6), and other carrying both oxidized Cys-47 and Cys-91 (double oxidized Prx6). Using these oxidized Prx6s, the single oxidized Prx6 and double oxidized Prx6 migrated to pIs at 6.2 and 5.9, respectively. These results suggest that oxidized Cys-47 from the basic spot and oxidized Cys-91 from the acidic spot are generated by artificial oxidation during sample handling processes after isoelectric focusing of 2D-GE. Therefore, it is important to make sure of the origin of cysteine oxidation, if it is physiological or artificial, when an oxidized cysteine residue(s) is identified.

• Korean Journal of Food Science and Technology
• /
• v.30 no.1
• /
• pp.42-48
• /
• 1998

Physicochemical properties of waxy maize starch and oxidized waxy maize starch with sodium hypochlorite $(0{\sim}60\;mg\;CL_2/g\;starch,40^{\circ}C,\;pH\;10,\;3.0\;hr)$ were studied. As sodium hypochlorite concentration was increased, the content of crude lipid and crude protein of the oxidized starch were decreased. And crude protein content and whiteness was considered to show negative regression. However, the crude ash content of the oxidized starch increased significantly with oxidation and bore a positive regression to the chlorine content. There was a progressive increase in the carboxyl content with increasing oxidant level. After pasting in hot water and cooling, viscosity of the oxidized starches were drastically lower than that of native starch . As carboxyl contents of the oxidized starch increased, the solubility and swelling power was increased. When waxy maize starch treated with 0, 1.5, 3.0 and 6.0% sodium hypochlorite, temperature of initial gelatinization of oxidized starch was shown to 65, 65, 60 and $50^{\circ}C$, respectively. The oxidized waxy maize starches also form clearer pastes. Water binding capacity of the oxidized starch decreased as the degree of carboxyl group substitution increased. Waxy maize starch has polygonal and some round granules which range from about 3.7 to $20\;{\mu}m$ in diameter. Surface appearance of the waxy maize starch became rough when oxidized with sodium hypochlorite. When homogenate of the oxidized waxy maize starch solution and corn germ oil was stored under room temperature for 24 hours, the emulsion stability was considered to depend on starch concentration and degree of substitution.

• BMB Reports
• /
• v.37 no.3
• /
• pp.325-329
• /
• 2004

Oxidation of catecholamines may contribute to the pathogenesis of Parkinson's disease (PD). The effect of the oxidized products of catecholamines on the modification of Cu,Zn-superoxide dismutase (SOD) was investigated. When Cu,Zn-SOD was incubated with the oxidized 3,4-dihydroxyphenylalanine (DOPA) or dopamine, the protein was induced to be aggregated. The deoxyribose assay showed that hydroxyl radicals were generated during the oxidation of catecholamines in the presence of copper ion. Radical scavengers, azide, N-acetylcysteine, and catalase inhibited the oxidized catecholamine-mediated Cu,Zn-SOD aggregation. Therefore, the results indicate that free radicals may play a role in the aggregation of Cu,Zn-SOD. When Cu,Zn-SOD that had been exposed to catecholamines was subsequently analyzed by an amino acid analysis, the glycine and histidine residues were particularly sensitive. These results suggest that the modification of Cu,Zn-SOD by oxidized catecholamines might induce the perturbation of cellular antioxidant systems and led to a deleterious cell condition.

• Molecules and Cells
• /
• v.25 no.3
• /
• pp.452-456
• /
• 2008

The interactions between monocytes and extracellular matrix proteins have been implicated in atherosclerosis pathophysiology. In the present study we evaluated monocyte attachment and migration through oxidized and non-oxidized collagen IV. Monocyte attachment was tested on microwells coated with either native or oxidized collagen IV. Monocyte migration through collagen IV was examined on transwells. Monocytes derived from patients with diabetes mellitus showed an increased ability to attach and migrate through collagen IV as compared to those derived from healthy volunteers. Moreover, control monocytes attached to oxidized collagen at a higher degree, while they migrated through oxidized collagen at a lower degree, as compared to the native protein. Our results also showed the involvement of the alpha2 integrin subunit in the above phenomena suggesting a modified interaction between monocytes and collagen IV in diabetes mellitus.