• Title/Summary/Keyword: storage protein

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Regulation Mechanism of Soybean Storage Protein Gene Expression (대두 저장단백질 유전자의 발현 조절 메카니즘)

  • 최양도;김정호
    • Proceedings of the Botanical Society of Korea Conference
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    • 1987.07a
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    • pp.283-307
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    • 1987
  • Glycinin and $\beta$-conglycinin are the most abundant storage protein in soybean. These proteins are known to be synthesized predominantly during germination and cell expansion phase of seed development for short period, and synthesized not in other tissues. Genes encoding these storage proteins are useful system to study the mechanism of development stage and tissue specific gene expression in eukaryotes, especially plants, at the molecular level. The cDNA and genomic clones coding for glycinin have been isolated and regulation mechanism of the gene expression has been studied. Initially, development and tissue-specific expression of the glycinin gene is regulated at the level of transcription. Post-transcriptional processing is also responsible for delayed accumulation of the mRNA. Translational control of the storage protein gene has not been reported. Post-translational modification is another strategic point to regulate the expression of the gene. It is possible to identify positive and/or negative reguratory clements in vivo by producing transgenic plants agter gene manipulation. Elucidation of activation and repression mechanism of soybean storage protein genes will contribute to the understanding of the other plant and eukaryotic genes at molecular level.

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Storage Stability of Freeze Dried Loach for Instant Choo-o-tang (즉석 추어탕을 냉동 건조미꾸라지의 저장성)

  • 류홍수;문숙임;이수정;문갑순
    • 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.

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Effect of Storage Period and Rechilling Process on Tenderness of Myofibrillar Protein of Chilled or Frozen Beef (냉장 또는 동결우유의 저장기간과 재냉장이 근원섬유단백질의 연도에 미치는 영향)

  • 김미숙;문윤희
    • The Korean Journal of Food And Nutrition
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    • v.11 no.5
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    • pp.536-541
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    • 1998
  • This study was carried out to investigate the changes of characteristics of myofibrillar protein for the vacuum chilled, the air frozen or the rechilled Holstein beef loin. The vacuum chilled beef was stored at 1$^{\circ}C$ and the air frozen beef was stored at -20$^{\circ}C$ for 60 days. The rechilled beef was restored for 3 days at 1$^{\circ}C$ by using the vacuum chilled or the air frozen beef. Myofibrillar protein extractability, 30,000 dalton component content and Mg-ATP ase activity for the vacuum chilled beef were higher than those of the air frozen beef. Each parameters increased significantly for the vacuum chilled beef after the 20 days storage, but there was no significant difference for the vacuum chilled beef after the 20 days storage, but there was no significant difference for the air frozen beef during the 60 days storage. By the rechilling process, myofibrillar protein extractability of the vacuum chilled and the frozen beef were not significant difference. The 30,000 dalton component of the vacuum chilled beef was showed not significant increment by rechilling, but the frozen beef was showed significant increment by rechilling. The Mg-ATPase activity of myofibrillar protein of the vacuum chilled beef was not changes by rechilling, but the frozen beef after the 20 days storage was significant increment by rechilling.

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A Study of Storage Protein in Lymantria dispar L. (매미나방(Lymantria dispar L.)의 저장단백질에 관한 연구)

  • 원종엽;김학열
    • The Korean Journal of Zoology
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    • v.33 no.3
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    • pp.346-353
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    • 1990
  • Two storage proteins, storage protein-1 (SPl) and storage protein -2 (SP2) were found in hemolymph and fat body during the development of Lymantria dispar L. SP1 has a molecular weight of 440, 000 and consists of six identical subunits (MW = 72, 000). The pI value of SP1 was 6.2. SP1 shows a similar high concentration during the late larval stage in both male and female. However, SP1 represents a quite different pattern during pupal stage between male and female. SP1 gradually decreases in male but increases in female. SP1 is immunologically identical to yolk protein. Also, SP1 of L. dispar shows immunologically partial reactions with storage proteins of Hyphantria cunea and Galleria mellonella.

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Effect of Packing Method on Physico-chemical Properties of Frozen Chicken (포장방법이 동결계육의 이화학적 특성에 미치는 영향)

  • 박구부;하정기;박범영;이상진;박용윤;박태선;신택순;이정일
    • Korean Journal of Poultry Science
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    • v.23 no.4
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    • pp.193-201
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    • 1996
  • This experiment was carried out to find out the effect of packing methods on physico-chemical properties of breast and thigh meats in chicken, which was dried by air spray chilling method. The chicken carcass was cut into breast and thigh muscles, which were either vacuum packed or atmosphere packed, and stored at -2O˚C for 1, 4, 8, 12 and 16 wk after quick freezing at -45˚C for 35 min. The pH values of atmosphere-packed breast meat and vacuum-packed breast meat after one wk of storage were higher than those of atmosphere-packed thigh meat and vacuum-packed thigh meat(P< .05). The pH values increased as storage period extended, but no significant difference was detected between two packing method(vacuum vs. atmosphere). Total moisture contents of breast meats after one wk of storage were higher than those of thigh meats. The total moisture contents decreased slowly as storage period extended, but no significant difference was detected between two packing method(vacuum vs. atmosphere). The shear force value of thigh meat was higher than that of breast meat. The shear force values of both meats decreased as storage period extended, regardless of packing method. The water soluble protein extractability of thigh meats was higher than that of breast meat, and the water soluble protein extractability of all treatments decreased until 8 wk after storage, but increased gradually after 8 wk of storage period. The salt soluble protein extractability of breast meat was higher than that of thigh meat, and the salt soluble protein extractability of all treatments decreased as storage period extended. With regard to the packing method, the vacuum packing showed higher value than that of atmosphere packing method until 8 wk of storage. Total lipid contents of atmosphere- and vacuum-packed thigh meats at 1 wk of storage were higher than those of breast meats, and the total lipid contents of all of treatments decreased as storage period extended. However, no significant difference was detected between two packing methods. The fatty acid contents of breast and thigh meats were in order of o1eic(33,5~42.4), palmitic(19.7~30.8) and linoleic acid(10.8~17.4).

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Purification and Characterization of Storage Protein-1 from Galleria mellonella (꿀벌부채명나방(Galleria mellonella L.)의 저장단백질-1(storage protein-1)의 정제 및 물리화학적 연구)

  • 이용호;여성문김학열
    • The Korean Journal of Zoology
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    • v.35 no.4
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    • pp.466-473
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    • 1992
  • Storage protein-1 (SP-1) of Gallerio mellonella was identified in hemolvmph and fat body by electrophoresis. SP-1 was purified from hemolvmph by KBr density gradient ultracentrifugation , DEAE-cellulose (DE52) ion-exchange chromatography, and gel permeation chromatography (Sephadex G-200). Purity of SP-1 was confirmed by Non-SDS PAGE and electron microscope. SP-1 is 9.4 nm in diameter and regular octahedron in shape. SP-1 has isoelectric point of 5.7 and native molecular weight of 365 K dalton and is composed of one type of subunit with molecular weight of 82 K dalton. Ttiacylslvcerol and phospholipid were found to be maior lipid components in SP-1.

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Utilization of Slaughter Porcine Blood as an Animal Feed (도축부산물인 돈혈의 재활용에 관한 연구)

  • 김정학;박강희;류경선;이제훈
    • Journal of Animal Environmental Science
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    • v.3 no.2
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    • pp.133-143
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    • 1997
  • Optimal conditions for collecting, storing and drying temperature to utilize slaughter porcine blood for blood meals and the effects of blood meal on growth in broiler chicks were investigated. Dry matter and protein contents of slaughter procine blood were 19.5% and 77%(dry basis), respectively. As for the composites of amino acids in the blood, aspartic acid, arginine, glycine, histidine, leucine, lysine, phenylalanin threonine were shown high. There was no significant difference between the collections by bloodletting and vacuumming in terms of microbial contamination. Storage of slaughter porcine blood showed no differences in protein, DNA and triglyceride contents and pH between the storage methods of freezing (-20$^{\circ}C$) and refrigerating (-4$^{\circ}C$). In case of room temperature storage, however, the decrease in pH and the appearance of new protein due to microbial contaminations increased as the storage periods were prolonged. When drying was done by flash methods, the drying period got shortened as the temperature became higher, yet protein and triglyceride were destoryed more. When drying was done over 120$^{\circ}C$, even at the same degree, the breakdowns of protein and triglyceride increased more as drying period got longer. In feeding trials of broiler chicks, dietary supplementation of the flash dried blood meal at 2% level showed significant difference in growth rate(P<.05%). These results indicated that the appropriate handling and manufacturing of slaughter porcine blood enabled the blood to be used as a protein source for broiler chicks.

On the Occurrence and Distribution of Storage Proteins During the Metamorphosis of Bombyx mori L (누에의 變態에 따른 貯藏蛋白質의 出現과 分布에 관하여)

  • Eul Won Seo;Hak Ryul Kim
    • The Korean Journal of Zoology
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    • v.29 no.1
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    • pp.1-12
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    • 1986
  • Electrophoretic, immunological, and column chromatography methods were used to determine the appearance and distribution of storage proteins in various organs during the metamorphosis of Bombyx mori L. Two storage proteins start to appear in haemolymph in early 5th instar stage and show the identical mobility with fat body proteins. These proteins show the high concentration in haemolymph in last instar stage but accumulate in fat body after pupation. Storage protein-2 shows the distinct pattern for general storage proteins in both male and females. This protein is involved with the formation of cuticle protein in late last instar stage and appears to be temperally deposited in midgut during the pupal stage. Also SP-2 shows the identity with vitellogenin electrophoretically and immunologically and especially the positive reaction with antibody against yolk protein during the pupal stage, demonstrating that the storage protein is closely related to the formation of yolk protein.

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Inhibition of lipid and protein oxidation in raw ground pork by Terminalia arjuna fruit extract during refrigerated storage

  • Chauhan, Pranav;Pradhan, Soubhagya Ranjan;Das, Annada;Nanda, Pramod Kumar;Bandyopadhyay, Samiran;Das, Arun K.
    • Asian-Australasian Journal of Animal Sciences
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    • v.32 no.2
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    • pp.265-273
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    • 2019
  • Objective: Terminalia arjuna plant, specially its leaves, bark, and roots, are widely used in traditional herbal medicine due to presence of bioactive components and being a rich source of natural antioxidants. But its fruit has not been used for any such purposes despite its potential to retard oxidation. Hence, the antioxidant potential of Arjuna fruit extract (AFE) in retarding lipid and protein oxidation of raw ground pork was evaluated during refrigerated storage for 9 days. Methods: The AFEs were prepared using different solvents viz. ethanol (EH), water, ethanol: water (60:40) and methanol:hot water (60:40). The AFEs were analysed for total phenolic content (TPC), 2, 2-diphenyl-1-picrylhydrazyl radical scavenging activity and reducing power. Water extract (WE) and ethanol-water extract (EH-WE) were selected and incorporated at 1.0% into freshly minced pork meat and compared with a synthetic antioxidant, in retarding lipid and protein oxidation during storage. Results: The TPC in AFEs using different solvents ranged from 11.04 to 16.53 mg gallic acid equivalents/g and extracts exhibited appreciable scavenging activity ranging from 50.02% to 58.62%. Arjuna extracts significantly (p<0.05) improved the colour score of meat samples by reducing the formation of metmyoglobin during storage. Both the AFEs (WE and EH-WE) significantly (p<0.05) lowered the thiobarbituric acid reactive substances value, peroxide formation and formation of protein carbonyls in raw pork than control sample during storage. Upon sensory evaluation of all samples, it was found that AFE treatment could prolong the storage period of meat samples, without influencing the colour and odour score, up to 6 days. Conclusion: AFEs used at 1% improved the oxidative stability, colour and odour score and prolonged the refrigerated shelf life of ground pork up 6 days. Therefore, AFE could be explored as an alternative natural antioxidant in retarding lipid and protein oxidation in meat products.

Proteomic Approach of the Protein Profiles during Seed Maturation in Common Buckwheat (Fagopyrum esculentum Moench.)

  • Park, Min-Hwa;Shin, Dong-Hoon;Han, Myoung-Hae;Yun, Young-Ho;Bae, Jeong-Sook;Lee, Yun-Sang;Chung, Keun-Yook;Lee, Moon-Soon;Woo, Sun-Hee
    • Korean Journal of Plant Resources
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    • v.22 no.3
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    • pp.227-235
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    • 2009
  • Single seeds of common buckwheat cultivar Suwon No. 1 when subjected to SDS-PAGE revealed very high polymorphism. High variation existed for protein or protein subunits with molecular weight 54-47kDa, 45-25kDa and 16-11kDa. The electrophoregram showed variation for globulin as well as other protein fractions. About 300 proteins were separated by two-dimensional electrophoresis in common buckwheat (Fagopyrum esculentum Moench.) seed. Seed maturation is a dynamic and temporally regulated phase of seed development that determines the composition of storage proteins reserves in mature seeds. Buckwheat seeds from 5, 10, 15, 20, and 25 days after pollination and matured stage were used for the analysis. This led to the establishment of high-resolution proteome reference maps, expression profiles of 48 spots. It was identified 48 proteins from MALDI-TOF/MS analysis of wild buckwheat seed storage proteins. The 48 proteins were found identical or similar to those of proteins reported in buckwheat and other plants; it is belonging to 9 major functional categories including seed storage proteins, stress/defense response, protein synthesis, photosynthesis, allergy proteins, amino acid, enzyme, metabolism, and miscellaneous. It appears that the major allergenic storage protein separated played the important role in buckwheat breeding and biochemical characterization.