• Food Science of Animal Resources
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• v.39 no.2
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• pp.296-308
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• 2019

Although the yellow mealworm (Tenebrio molitor L.) is a promising alternative protein source, the effects of processing conditions on functional properties are unclear. In this study, a protein extract of yellow mealworm larvae (PEYM) was subjected to different heat temperature ($55^{\circ}C$, $75^{\circ}C$, and $95^{\circ}C$) with different time (20, 40, and 60 min) to evaluate the functional properties and protein oxidation. Different heat temperature treatment significantly affected the exposure of surface hydrophobicity of the proteins and protein molecule aggregation, which reached maximum levels at $95^{\circ}C$ for 60 min. Protein oxidation was inversely proportional to the temperature. Both the highest carbonyl value (1.49 nmol/mg protein) and lowest thiol value (22.94 nmol/mg protein) were observed at $95^{\circ}C$ for 60 min. The heating time-temperature interaction affected several functional properties, including solubility, emulsifying potential, and gel strength (GS). Solubility decreased near the isoelectric point (pH 5 to 6). As the temperature and heating time increased, emulsifying properties decreased and GS increased. The oil absorption capacity and foaming properties decreased and the water absorption capacity increased. These results confirmed that PEYM is a suitable source of proteins for processing and applications in the food industry.

• Tuberculosis and Respiratory Diseases
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• v.61 no.4
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• pp.330-338
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• 2006

Background: The main factors associated with weight loss in patients with COPD are not well known. Since chronic inflammation and oxidative stress play a major pathogenic role in COPD, these factors may be responsible for the patients' weight loss. Therefore, this study measured the body mass index (BMI) in COPD patients and evaluated the variables, such as systemic inflammatory marker, oxidative stress and lung function, that correlate with the BMI. Method: The stable COPD patients (M:F=49:4, mean age=$68.25{\pm}6.32$) were divided into the lower (<18.5), normal (18.5-25) and higher (>25) BMI group. The severity of the airway obstruction was evaluated by measuring the $FEV_1$. The serum IL-6 and TNF-$\alpha$ levels were measured to determine the degree of systemic inflammation, and the carbonyl protein and 8-iso-prostaglandin $F_2{\alpha}$ level was measured to determine the level of oxidative stress. Each value in the COPD patients and normal control was compared with the BMI. Results: 1) Serum 8-iso-prostaglandin $F_2{\alpha}$ in COPD patients was significantly higher ($456.08{\pm}574.12pg/ml$) than that in normal control ($264.74{\pm}143.15pg/ml$) (p<0.05). However, there were no significant differences in the serum IL-6, TNF-$\alpha$, carbonyl protein between the COPD patients and normal controls. 2). In the COPD patients, the $FEV_1$ of the lower BMI group was significantly lower ($0.93{\pm}0.25L$) than that of the normal BMI ($1.34{\pm}0.52L$) and higher BMI groups ($1.72{\pm}0.41L$) (p<0.05). The lower $FEV_1$ was significantly associated with a lower BMI in COPD patients (p=0.002, r=0.42). The BMI of very severe COPD patients was significantly lower ($19.8{\pm}2.57$) than that of the patients with moderate COPD ($22.6{\pm}3.14$) (p<0.05). 3). There were no significant differences in the serum IL-6, TNF-$\alpha$, carbonyl protein and 8-iso-prostaglandin $F_2{\alpha}$ according to the BMI in the COPD patients. Conclusion: The severity of the airway obstruction, not the systemic inflammatory markers and oxidative stress, might be associated with the BMI in stable COPD patients. Further study will be needed to determine the factors associated with the decrease in the BMI of COPD patients.

• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.3
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• pp.371-377
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• 1995

The effect of ${\alpha}$-tocopherol and ${\beta}$-carotene supplementation on reducing the oxidative damag in the liver of rats were studied. Forth-five male Sprague Dawley aged 4 weeks were randomly assigned to 9 groups of five for the 12 weeks of the study. Nine groups, sardine oil, sardine oil＋Vt E, sardine oil＋${\beta}$-carotene, soybean oil, soybean oil＋Vt E, soybean oil＋${\beta}$-carotene, lard, lard＋Vt E, lard＋${\beta}$-carotene group, were prepared. Sardine oil, soybean oil, or lard was used for dietary fat and 200% of ${\alpha}$ -tocopherol or 150% of ${\beta}$-carotene was supplemented to each diet. Each diet supplied 65% of total energy as carbohydrate, 15% as protein, and 20% as lipid. The MDA value and protein carbonyl contents of sardine oil group were significantly different(p<0.05) to those of other fat groups indicating that the most severe lipid oxidation occurred in the group fed diet containing highly polyunsaturated fatty acid. When ${\alpha}$-tocopherol or ${\beta}$ -carotene was supplemented to the sardine oil diet, MDA value(-35%, -15%, respectively) and protein carbonyl content(-44%, -32%, respectively) decreased significantly(p<0.05). Cu, Zn-superoxide dismutase(SOD) and catalase activities of three different sardine oil groups with or without antioxidants were lower than those of soybean oil or lard group. The reducing effect of ${\alpha}$-tocopherol on oxidative damage in sardine oil group supplemented with ${\alpha}$-tocopherol was noticeable(p<0.05). However the adverse effect of ${\beta}$-carotene was observed. SOD and catalase activities of ${\beta}$-carotene supplemented groups were that the lowest among the same fat groups, but the differences were not statistically significant. The possible cause of decreased enzyme activity seemed to be related to the vitamin A(Vt A) toxicity in the liver where retinol converted from dietary ${\beta}$-carotene in the intestinal mucosa was stored.

• 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.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1996.04a
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• pp.182-182
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• 1996

Annexin I is a member of the annexin family of calcium dependent phospholipid binding proteins and has anti-inflammatory activity by inhibiting phospholipase A$_2$ (PLA$_2$). Recent X-ray crystallographic study of annexin I identified six Ca$\^$2+/ binding bites, which was different types (type II, III) from the well-known EF-hand motif (type I). In this work, the structure of annexin I was studied at atomic level by using $^1$H, $\^$15/N and $\^$l3/C NMR(nuclear magnetic resonance) spectroscopy, and the effect of Ca$\^$2+/ binding on the structure of annexin I was studied, and compared with that of Mg$\^$2+/ binding, When Ca$\^$2+/ was added to annexin I, NMR peak change was occured in high- and low-field regions of $^1$H-NMR spectra. NMR peak change by Ca$\^$2+/ binding was different from that by Mg$\^$2+/ binding. Because annexin I is a larger protein with 35 kDa molecular weight, site-specific (amide-$\^$15/N, carbonyl-$\^$l3/C) labeling technique was also used. We were able to detect methionine, tyrosine and phenylalanine peaks respectively in $\^$13/C-NMR spectra, and each residue was able to be assigned by the method of doubly labeling annexin I with [$\^$13/C] carbonyl-amino acid and [$\^$15/N] amide-amino acid. In $\^$l3/C-NMR spectra of [$\^$13/C] carbonyl-Met labeled annexin I, we observed that methionine residues spatially located near Ca$\^$2+/ binding Sites Were Significantly effected by Ca$\^$2+/ binding. From UV spectroscopic data on the effect of Ca$\^$2+/ binding, we knew that Ca$\^$2+/ binding sites of annexin I have cooperativity in Ca$\^$2+/ binding. The interaction of annexin I with PLA$_2$ also could be detected by using heteronuclear NMR spctroscopy. Consequently, we expect that the anti-inflammatory action mechanism of annexin I may be a specific protein-protein interaction. The residues involved in the interaction with PLA$_2$ can be identified as active site by assigning NMR peaks effected by PLA$_2$ binding.

• Korean Journal of Food Science and Technology
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• v.33 no.1
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• pp.1-6
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• 2001

Emulsion products with water soluble protein were exposed under light at $5^{\circ}C$ for 8 days. Peroxide value (POV) was increased significantly at the bigining of storage and 2-thiobarbituric acid (TBA) value also increased until 4 days of storage with increase of the production of carbonyl compounds, suggesting that the condition was reacted different from that of the lipid autoxidation. The reaction was similar to the flavor reversion that usually produced from the bigining of soybean oil oxidation. The reason might be the meat pigment, myoglobin, oxidation and it would be due to the singlet oxygen rather than superoxide anion. When the light was excluded general pattern was similar but the production of oxidation products were smaller than that when the sample was exposed under light. The effect of the singlet oxygen was also smaller which meant that the singlet oxygen produced during emulsion process may affect on the flavor reversion at the bigining of storage. The POV of the emulsion without water soluble protein increase gradually by storage and the results indicated that the degradation rate of the peroxides were lower than the sample with water soluble protein. Especially after 4 days of storage, production of carbonyl compounds were decreased. During storage it would be possible to produce the singlet oxygen and the sensitizer from the plants that can be produced during decoloration of soybean oil may be responsible for it. When the light was excluded the production of oxidation products were reduced at the begining of storage and the effect of quencher also was not detected. Therefore the results indicated that the light can accelerate the lipid oxidation.

• Food Science and Biotechnology
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• v.18 no.1
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• pp.130-136
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• 2009

The present study was conducted to determine the protective ability of the ethanol extracts of Hypericum scabroides Robson & Poulter (HS) and Hypericum triquetrifolium Turra (HT) against the protein oxidation and DNA damage induced by Fenton system. The ability of HS and HT to prevent oxidative damage to bovine serum albumin (BSA) induced by $Fe^{3+}/H_2O_2$ and ascorbic acid was investigated. The ethanol extracts of HS and HT at different concentrations ($50-1,000{\mu}g/mL$) efficiently prevented protein oxidation induced by hydroxy radical as assayed by protein oxidation markers including protein carbonyl formation (PCO) and polyacrylamide gel electrophoresis. The effect of ethanol extracts of HS and HT on DNA cleavage induced by UV-photholysis of $H_2O_2$ using pBluescript M13+ plasmid DNA were investigated. These extracts significantly inhibited DNA damage induced by reactive oxygen species (ROS). Therefore, HS and HT extracts may be useful in the food industry as effective synthetic antioxidants.

• Korean Journal of Food Science and Technology
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• v.10 no.4
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• pp.387-393
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• 1978

Lipid oxidation is one of the major factors affecting on deterioration of nutritional quality in dried fish products. In this paper, the relationship between oxidized products of lipid and brown pigments, free amino acids and available lysine during the storage of dried sea eel, Muraesox cinereus, was investigated. And the inhibiting effect of antioxidant to lipid oxidation and its role to the protein quality were also discussed. From the results, TBA and carbonyl value rapidly increased while amino-N and available lysine diminished during hot air drying. This suggests that drying conditions greatly affected to the oxidation of lipid and making amino acids 'unavailable'. TBA value increased up to 20 days, and hereafter gradually diminished. Increase in TBA and carbonyl value and formation of fat oxidative brown pigment were closely related to the loss of free amino-N and available lysine. The loss of available lysine seemed to be affected by the formation of unsaturated carbonyl compounds rather than saturated carbonyl compounds. By the treatment of antioxidant, the loss of amino acids and available lysine was somewhat retarded. This may suggests that the oxidation of lipid or oxidative browning reactions are functioning to the loss of available lysine. In antioxidant treated sample, 23% of amino-N to the total amino-N in the fresh sample was lost after 20 days storage at $30^{\circ}C$ while the loss of amino-N to 39% in case of the control, and afterward the value treated to be slightly reduced or remained steady.

• Journal of the Korean Magnetic Resonance Society
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• v.2 no.2
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• pp.141-151
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• 1998

Human annexin I is a member of annexin family of calcium dependent phospholipid binding proteins, which have been implicated in various physiological roles including phospholipase A2(PLA2) inhibition, membrane fusion and calcium channel activity. In this work, the structure of N-terminally truncated human annexin I ({{{{ DELTA }}-annexin I) and its interactions with Ca2+, ATP and cAMP were studied at atomic level by using nuclear magnetic resonance (NMR) spectroscopy. The effect of Ca2+ binding on the structure of {{{{ DELTA }}-annexin I was investigated. The addition of Ca2+ to {{{{ DELTA }}-annexin I caused some changes in 13C NMR spectra. Carbonyl carbon resonances of some histidines were significantly broadened by Ca2+ binding. However, in the case of methionine, phenylalanine, and tyrosin, small changes could be observed. We found that ATP and cAMP bind {{{{ DELTA }}-annexin I, and the binding ratio of ATP to {{{{ DELTA }}-annexin I is 1. These results are well consistent with the report that cAMP and ATP interact with annexin I, and affect the calcium channels formed by annexin I. Because {{{{ DELTA }}-annexin I is a large protein with 35 kDa molecular weight, site-specific (carbonyl-13C) labeling technique was used to study the interaction sites of {{{{ DELTA }}-annexin I with Ca2+. NMR study was focused on the carbonyl carbon resonances of tyrosine, phenylalanine, methionine and histidine residues of {{{{ DELTA }}-annexin I because the number of these amino acids is small in the amino acid sequence of {{{{ DELTA }}-annexin I.

• Elastomers and Composites
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• v.54 no.2
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• pp.110-117
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• 2019

The characterization of the ozone oxidation for raw natural rubber (NR) was investigated under controlled conditions through image and fourier transform infrared (FT-IR) analysis. The ozone oxidation was performed on a transparent thin film of raw NR coated on a KBr window in a dark chamber at $40^{\circ}C$ under low humidity conditions to completely exclude thermal, moisture, or light oxidation. The ozone concentration was set at 40 parts per hundred million (pphm). Before or after exposure to ozone, the image of the thin film for raw NR was observed at a right or tilted angle. FT-IR absorption spectra were measured in the transmission mode according to ozone exposure time. The ozone oxidation of NR was determined by the changes in the absorption peaks at 1736, 1715, 1697, and $833cm^{-1}$, which were assigned to an aldehyde group (-CHO), a ketone group (-COR), an inter-hydrogen bond between carbonyl group (-C=O) from an aldehyde or a ketone and an amide group (-CONH-) of protein, and a cis-methine group ($is-CCH_3=CH-$, respectively. During ozone exposure period, the results indicated that the formation of the carbonyl group of aldehyde or ketone was directly related to the decrement of the double bond of cis-1,4-polyisoprene. Only carbonyl compounds such as aldehydes or ketones seemed to be formed through chain scission by ozone. Long thin cracks with one orientation at regular intervals, which resulted in consecutive chain scission, were observed by image analysis. Therefore, one possible two-step mechanism for the formation of aldehyde and ketone was suggested.