• Title/Summary/Keyword: Storage-protein 2

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Protein Cross-linking in Freeze Dried Fish Meat (동결건조 어육의 단백질 Cross-linking에 관한 연구)

  • LEE Kang-Ho;JUNG Woo-Jin;SUH Jae-Soo;JEONG In-Hak;KIM Chung-Gon
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.19 no.2
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    • pp.100-108
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    • 1986
  • This study was carried out in order to investigate protein cross-linking in freeze-dried meat of flounder (Limanda herzensteini). Changes in solubility or extractability of proteins and electrophoretic patterns of the extracted proteins were determined to monitor the cross-linking during the storage of freeze-dried meat. Development of nonenzymatic browning and the loss of in vitro protein digestibilily were also measured to assess their influences on the changes of functional and nutritional properties of proteins. In addition, the effects of lysine added, and removal of fat and water extractives were also mentioned. The extractability of protein decreased upon storage time and temperature, and the loss of solubility of myosin was evident. In case of the samples stored at $5^{\circ}C$ for 150 days, the extractability of protein decreased $26.4\%$, while that of the samples stored at $20^{\circ}C$ for 60 days decreased about $39.7\%$. And it was noted that the loss of solubility of myosin was $68.3\%$ and $98.1%$ for the same storage conditions, respectively. It was noteworthy that the samples treated with $L-lysine{\cdot}HCl$ seemed to prevent more or less the loss of protein solubility, in that, even stored at $20^{\circ}C$ for 120 days, revealed only $57.03\%$ decrease. The nonenzymatic browning was proceeded with the increase of storage temperature, especially, in the samples treated with glucose. This suggests that the decrease in extractibility of myosin was accompanied by the extent of browning. But the browning was retarded in defatted samples. The in vitro apparent protein digestibility was also higher in the samples defatted or water extracted. It was suggested from these results that changes in properties of proteins in freeze dried fish meat were led by the protein cross-linking which was attributed to Maillard type of reactions and protein-lipid interactions.

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Storage Stability of the Synthetic Angiotensin Converting Enzyme (ACE) Inhibitory Peptides Separated from Beef Sarcoplasmic Protein Extracts at Different pH, Temperature, and Gastric Digestion

  • Jang, Ae-Ra;Jo, Cheo-Run;Lee, Moo-Ha
    • Food Science and Biotechnology
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    • v.16 no.4
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    • pp.572-575
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    • 2007
  • The angiontensin converting enzyme (ACE) inhibitory peptides were separated from beef sarcoplasmic protein extract and their amino acid sequences were identified as GFHI, DFHINQ, FHG, and GLSDGEWQ. The 4 peptides were synthesized in a laboratory and the ACE inhibitory activities of pep tides was measured after 2 months of storage at $4^{\circ}C$ under different pH conditions (6.0, 6.5, 7.0, 7.5, and 8.0) and the exposure of different temperatures (70, 80, 90, and $100^{\circ}C$) for 20 min to evaluate industrial use. No significant difference was detected by pH and temperature abuse for 20 min during storage. When the synthetic peptides were digested by pepsin, trypsin, and chymotrypsin, the ACE inhibitory activity was not changed. These results indicated that the 4 synthetic peptides with ACE inhibitory activity were pH-stable, heat-stable, and resistant to proteinases in gastro-intestinal tracts. Therefore, those 4 peptides can be used as a source for functional food product with various applications.

Studies on Lipids and Proteins of Rabbit Meat -II. Emphasis on quality of rabbit meat protein- (토끼고기의 지방질과 단백질에 관한 연구 -II. 단백질을 중심으로-)

  • Leekim, Yang-Cha;Cho, He-Cheong
    • Journal of Nutrition and Health
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    • v.10 no.2
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    • pp.27-34
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    • 1977
  • The present study was carried out to evaluate the nutritional quality of rabbit meat protein. The composition of amino acids contained in rabbit meat was compared with those of other animal meats such as beef, pork and chicken. Also included in this study was the question whether the cooking and storage conditions affect the amino acid composition and the pepsindigestibility of rabbit meat protein. The results are summarized as follows: 1. The large variation observed from sample to sample of EAA (essential amino acid) composition in rabbit meat was found to be an interesting but peculiar property of rabbit meat protein. The most limiting amino acid of rabbit meat protein was phenylalanine, whereas methionine was the first limiting amino acid of both beef and pork proteins. Chemical scores of various meat proteins were 68, 65, 66, and 74 for rabbit meat, beef, pork, and chicken respectively. 2. In pan roasting, the EAA damaged most by heat was methionine (15%). When cooked after two months of frozen storage, lysine decreased most. 3. Higher pepsin digestibility was obtained by cooking rabbit meat after seasoned in alcohol, ginger juice, and other spices compared with various other cooking conditions without seasoning. The pepsin digestibility value was even higher for the seasoned meat than for the raw meat. 4. Among various meats tested the rabbit meat showed the lowest pepsin digestibility. 5. A simple measurement of released methionine could be used to determine relative digestibility instead of measuring $NH_2-N$ content after pepsin digestion. From all the results obtained in this study it can be concluded that rabbit meat is a good Protein food item when used fresh and stored properly to prevent rancidity problems. It is suggested to study further the peroxidation effect of unsaturated fatty acids on protein quality. This study was supported by the Ministry of Science and Technology in Korea.

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Physicochemical Properties of Freeze Dried Ginseng from the Fresh Ginseng Stored at Low Temperature (저온저장 후 냉동건조한 인삼의 이화학적 특성)

  • 장진규;심기환
    • Journal of Ginseng Research
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    • v.18 no.1
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    • pp.60-65
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    • 1994
  • Fresh ginseng of same grade was stored under the 4$\pm$1$^{\circ}C$ and 87~92% RH for 10 weeks. During the storage, an aliquot amount of the ginseng was drawn, freeze dried and chemical constituents and physicochemical parameters were measured. After 10 weeks of storage drying rate and shrinkage of ginseng were 1520% and 9.04%, respectively, mold growth was seen at week 5 and observed for 51.2% of the ginseng week 10. Amylase activity level was elevated at the early stage of storage and decreased to 5% of initial value at week 5. At week 5, the elevated amylase activity was inconcomitant with the appearance of the mold growth. Crude protein contents were increased and decreased, respectively 5 week post storage. No significant changes in crude fat, crude fiber, ash, total sugar, n-butanol extract and ginsenoside were observed. The content of water-extractable substance showed maximum at week 7 to 8. The value of pH was slightly elevated and reducing sugar was increased during the storage. Key words Ginseng storage, physicochemical properties, drying rate, shrinkage, amylase activity.

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Effects of Storage Temperature on the Post-Mortem Changes of Wild and Cultured Olive Flounder Muscle

  • Cho Young Je;Kim Tae Jin;Yoon Ho Dong
    • Fisheries and Aquatic Sciences
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    • v.2 no.2
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    • pp.161-166
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    • 1999
  • The rigor-mortis progress of cultured olive flounder spiked at the brain started much faster than that of wild one. They attained full rigor state after 30 hrs at $0^{\circ}C$, 36 hrs at $5^{\circ}C$ and 50 hrs at $10^{\circ}C$ in the cultured flounder, while after 36 hrs at $0^{\circ}C$, 50 hrs at $5^{\circ}C$, and 60 hrs at $10^{\circ}C$ in the wild. ATP concentration in the muscle was around $5.9\mu mol/g$ for wild and $6.2\mu mol/g$ for cultured flounder. ATP breakdown progressed rapidly in $0^{\circ}C$ samples, followed by $5^{\circ}C$ and $10^{\circ}C$ samples. $Mg^{2+}$-ATPase activity of myofibrillar protein in the presence of 0.25mM CaCb was higher in cultured myofibri1lar protein than in wild one. $Mg^{2+}$-ATPase activities of myofibrillar protein increased during storage in samples stored at $0^{\circ}C$ and $5^{\circ}C$ while decreased in samples stored at $10^{\circ}C$. The level of breaking strength of muscle immediately after death was higher in the wild muscle than in the cultured muscle. The breaking strength reached maximum level at 10 hrs after death in both samples.

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Studies on the Thermal Stability of Free Drip Released from PSE Pork Muscle (PSE돈육 드립의 열안정성에 관한 연구)

  • 김천제
    • Food Science of Animal Resources
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    • v.20 no.2
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    • pp.146-151
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    • 2000
  • The objective of this study was to investigate the characteristics on the thermal denaturation of free drip released from pork loin during chilled storage using DSC(differential scanning calorimetry). DSC thermogram of drip released from normal pork(NORD) was characterized by a minor peak and two major peaks with temperature maxima at $61.5^{\circ}C$, $71.7^{\circ}C$ (associated with sarcoplasmic proteins) and $84.3^{\circ}C$ (associated with protein-protein interaction and aggregation). In the denaturation temperature of drip released from PSE pork (PSED), the peak(Tmax) at $59.0^{\circ}C$ was reduced by $2.5^{\circ}C$. When the thermograms were divided into segments correponding to the three peaks, $\Delta$H2 was shown to be reduced by 10% in PSED as compared to NORD. With the decrease in the solubility of sarcoplasmic proteins in PSE muscle, there was a corresponding increase the drip loss during the storage.

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Effect of Light on Developmental Changes and Activities of Microbody in the Cotyledons of Radish Seedlings (발아중 빛에 의한 무 유식물의 자엽 Microbody의 활성 변화)

  • 박민철
    • Journal of Plant Biology
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    • v.29 no.4
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    • pp.243-254
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    • 1986
  • The enzyme patterns and the food storage changes in radish (Raphanus sativus L. cv. Taewang) cotyledons during seedling development were studied. The radish seeds were germinated for 8 days at $25^{\circ}C$ under light (7, 000 lux) or dark condition. The lipid and protein contents per seed were 4.3 mg and 2.85 mg respectively. In 8-day-old light-grown seedling, the lipid and protein contents per cotyledon pair were 1.5 mg and 2.08 mg; in 8-day-old dark-grown seedling, they were 0.8 mg and 1.24 mg respectively. The heterotrophic phase of seedlings continued for 3 days after sowing and followed by autotrophic phase (3~6 day) and senescence phase (6~8 day). The food storage function decreased in response to time course. During heterotrophic phase, the activities of glyoxysomal enzymes (malate synthetase, isocitrate lyase, and catalase) were high at 2~3 day. Those patterns were somewhat more prominent in darkness. During the autotrophic phase, the activities of peroxysomal enzymes (glycolate oxidase and catalase) increased at 4~5 day.

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The study on the Storage Time of the Jangduck. The First Report, Making and Effects of Storage Time on Proximate Composition Components of Jangduck (장떡의 저장성에 관한 연구 제1보. 장떡의 제조와 저장기간에 따른 일반성분의 변화에 관한 연구)

  • 이숙미;염초애;조정순
    • Korean journal of food and cookery science
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    • v.11 no.2
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    • pp.108-112
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    • 1995
  • This study was attempted to analyze the proximate composition content of Jangduck in order to find out usefulness as a stored food. Sex different group of Jangduck were assigned according to the contents of three different glutinous rice(10, 20, or 30%) with or without 30fo beef supplematation. The contents of moisture, protein, fat, carbohydrate, fiber and crude ash of Jangduck were periodically analyzed four times during 60 days. The results wee summarized as follows: 1. The content of mois-ture in jangduck decreased as the level of glutinous rice flour increased in 15days. The moisture content slightly decreasedafter 30days of storage time. 2. The content of protein, fat, carbohydrate, crude fiber and ash of Jangduck were shown to be unchanged. 3. The crude protein of Jangduck was relatively high. 4. There was little change of proximate composition contents of Jangduck throu-ghout the total storage period.

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Nucleolar GTPase NOG-1 Regulates Development, Fat Storage, and Longevity through Insulin/IGF Signaling in C. elegans

  • Kim, Young-Il;Bandyopadhyay, Jaya;Cho, Injeong;Lee, Juyeon;Park, Dae Ho;Cho, Jeong Hoon
    • Molecules and Cells
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    • v.37 no.1
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    • pp.51-57
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    • 2014
  • NOG1 is a nucleolar GTPase that is critical for 60S ribosome biogenesis. Recently, NOG1 was identified as one of the downstream regulators of target of rapamycin (TOR) in yeast. It is reported that TOR is involved in regulating lifespan and fat storage in Caenorhabditis elegans. Here, we show that the nog1 ortholog (T07A9.9: nog-1) in C. elegans regulates growth, development, lifespan, and fat metabolism. A green fluorescence protein (GFP) promoter assay revealed ubiquitous expression of C. elegans nog-1 from the early embryonic to the adult stage. Furthermore, the GFP-tagged NOG-1 protein is localized to the nucleus, whereas the aberrant NOG-1 protein is concentrated in the nucleolus. Functional studies of NOG-1 in C. elegans further revealed that nog-1 knockdown resulted in smaller broodsize, slower growth, increased life span, and more fat storage. Moreover, nog-1 over-expression resulted in decreased life span. Taken together, our data suggest that nog-1 in C. elegans may be an important player in regulating life span and fat storage via the insulin/IGF pathway.

Effect of Allium hookeri Root on Physicochemical, Lipid, and Protein Oxidation of Longissimus Dorsi Muscle Meatball

  • Yoon, Dong-kyu;Kim, Ji-Han;Cho, Won-Young;Ji, Da-Som;Lee, Ha-Jung;Kim, Jung-Ho;Lee, Chi-Ho
    • 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.