• Title/Summary/Keyword: water-soluble proteins

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Processing of Ready-to-Cook Food Materials with Dark Fleshed Fish 1, Processing of Ready-to-Cook Sardine Meat "Surimi" (일시다획성 적색육어류를 이용한 중간식품소재 개발에 관한 연구 1. 정어리 연육의 가공)

  • LEE Byeong-Ho;LEE Kang-Ho;YOU Byeong-Jin;SUH Jae-Soo;JEONG In-Hak;JUNG Woo-Jin;KANG Jeong-Oak
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.18 no.5
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    • pp.401-408
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    • 1985
  • In order to develop new types of product which can offer a sanitary and preservative duality, and convenience to consumers in marketing and cooking particularly in urban area, two processing methods of ready-to-cook food materials with dark fleshed fishes like sardine and mackerel were investigated. A method applied, in this work, is processing of ready-to-cook sardine meat "surimi" in which sardine meat is treated with alkaline solution to stabilize myofibrillar proteins, washed thoroughly with water to remove soluble components, and added with a proper amount of polyphosphate and sorbitol to enforce the functional property of meat such as water holding capasity, elasticity, and gel strength. The textural properties of fish meat paste made from the "surimi" meat were greatly dependent upon the stability of myofibrillar proteins and the elimination of water soluble components. The salt soluble proteins of sardine meat were so unstable in post-mortem stage that the gel forming ability was lost within 3 days at $5^{\circ}C$ storage and 2 to 3 weeks even at $-20^{\circ}C$ although the freshness was well kept for a week at $5^{\circ}C$ and several months of storage at $-20^{\circ}C$. A proper way of treatment to keep the proteins stable was that fish meat must be washed with $0.4\%$ sodium bicarbonate solution followed by 3 to 4 times washing with water. This resulted in removal of $80\%$ water soluble proteins and 50 to $60\%$ lipids. The addition of polyphosphate and sorbitol affected the stability of proteins during the storage of "surimi" meat. When phosphate and sorbitol were added in the ratio of $0.3\%:\;0.3\%,\;0.6\%:\;3\%,\;0.6\%:\;6\%,\;0:\,0.3\%\;and\;0.3\%:\;0$, the gel forming ability terminated in 35 days, 21 days, 14 days, 14 days, and 14 days of storage at $-30^{\circ}C$, respectively, while that of the control was 7 days. And it was also noteworthy that at least 8.0 mg/g of salt soluble protein nitrogen content was required for gel formation.

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The Cutaneous Protection for Detergent Formulation of Nature Wheat Protein Surfactant Complexes (천연 밀단백질/계면활성제 복합체의 세정에 있어 피부보호)

  • Jeong, Hwan-Kyeong;Park, Heung-Cho;Kim, Myung-Soo;Nam, Ki-Dae
    • Journal of the Korean Applied Science and Technology
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    • v.19 no.2
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    • pp.79-85
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    • 2002
  • The cutaneous tolerability of detergent formulations can be improved by means of suitable additives. They complex the surfactant molecules lowering the concentration of their free monomeric species. Proteins derivatives used as additives for detergency are usually prepared by partial hydrolysis of plant reserve proteins. The main purpose of the hydrolytic cleavage is to make them water soluble and suitable for liquid products. Water solubility and stability are obtained by means of complexation with surfactants which also increase their actual hydrophobicity, an important parameter affecting cosmetic properties of proteins. Transepidermal water loss (TEWL) and electric capacitance (EC) have been adopted as investigation technigues to evaluate the skin integrity/damage in vitro tests, The performance of native wheat protein / surfactant complexes has been compared with traditional protein hydrolysates as detergent additives. The results show a noticeable reduction of skin irritation in surfactant formulations with addition of native wheat protein.

Water-insoluble, Whey Protein-based Microcapsules for Controlled Core Release Application

  • Lee, Sung-Je
    • Journal of Dairy Science and Biotechnology
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    • v.23 no.2
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    • pp.115-123
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    • 2005
  • Microcapsules consisting of natural, biodegradable polymers for controlled and/or sustained core release applications are needed. Physicochemical properties of whey proteins suggest that they may be suitable wall materials in developing such microcapsules. The objectives of the research were to develop water-insoluble, whey protein-based microcapsules containing a model water-soluble drug using a chemical cross-linking agent, glutaraldehyde, and to investigate core release from these capsules at simulated physiological conditions. A model water soluble drug, theophylline, was suspended in whey protein isolate (WPI) solution. The suspension was dispersed in a mixture of dichloromethane and hexane containing 1% biomedical polyurethane. Protein matrices were cross-linked with 7.5-30 ml of glutaraldehyde-saturated toluene (GAST) for 1-3 hr. Microcapsules were harvested, washed, dried and analyzed for core retention, microstructure, and core release in enzyme-free simulated gastric fluid (SGF) and simulated intestinal fluid(SIF) at $37^{\circ}C$. A method consisting of double emulsification and heat gelation was also developed to prepare water-insoluble, whey protein-based microcapsules containing anhydrous milkfat (AMF) as a model apolar core. AMF was emulsified into WPI solution (15${\sim}$30%, pH 4.5-7.2) at a proportion of 25${\sim}$50%(w/w, on dry basis). The oil-in-water emulsion was then added and dispersed into corn oil ($50^{\circ}C$) to form an O/W/O double emulsion and then heated at $85^{\circ}C$ for 20 min for gelation of whey protein wall matrix. Effects of emulsion composition and pH on core retention, microstructure, and water-solubility of microcapsules were determined. Overall results suggest that whey proteins can be used in developing microcapsules for controlled and sustained core release applications.

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Adsorption Property of Shrimp Shell Chitosan to Water Soluble Proteins (수용성 단백질에 대한 새우껍질 Chitosan의 흡착 특성)

  • 손병일;김경삼
    • The Korean Journal of Food And Nutrition
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    • v.13 no.3
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    • pp.242-248
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    • 2000
  • 수산물 가공시 흘러나오는 폐수 중에 함유되어 있는 수용성 단백질을 chitosan에 흡착시키기 위하여 albumin과 hemoglobin, albumin-myoglobin 혼합단백질을 이용하여 chitosan과의 흡착 및 chitosan 제조조건에 따른 흡착효과와 chitosan의 수용성 단백질 흡착에 미치는 인자를 살펴본 결과는 다음과 같다. Chitosan위 탈아세틸화 조건을 60, 70, 80%로 달리하여, albumin, hemoglobin, albumin-myoglobin 혼합용액에 적용했을때 chitosan의 탈아세틸화도가 높을수록 chitosan과 단백질 사이의 흡착률은 높게 나타났다. 초음파 처리에 의하여 chitosan의 분자량이 작을수록 chitosan과 단백질 사이의 흡착률은 높게 나타났다. pH변화에 따른 chitosan과 수용성 단백질의 흡착률은 albumin 및 albumin-myoglobin 혼합용액에서는 pH 4.0에서, hemoglobin용액에서는 pH 7.0에서 흡착률이 높게 나타났다 chitosan과 수용성단백질과의 흡착에서 반응시간은 albumin및 albumin-myoglobin 혼합용액에서는 4시간, hemoglobin용액에서는 3시간까지 흡착률이 증가하였고, 그 이후의 시간이 경화하여도 흡착률의 증가는 거의 보이지 않았다. 수용성 단백질 용액에 NaCl 농도를 0.1M에서 1.0M로 증가시켜 첨가했을때 염의 농도가 높을수록 chitosan과 단백질 사이의 흡착이 잘 일어나지 않았다.

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Separation and Composition of Sesame Meal Protein (참깨박(粕) 단백질(蛋白質)의 분리(分離)와 조성(組成))

  • Kim, Jun-Pyong;Shim, Woo-Man;Kim, Chong-Ik
    • Applied Biological Chemistry
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    • v.23 no.1
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    • pp.14-22
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    • 1980
  • White and black sesame produced in Korea were defatted with ethyl ether or n-hexane. Defatted sesame meal was extracted with water and salt solution, and protein extraction was precipitated at various pH 1 through 12, with trichloro acetic acid (TCA), tannic acid and ammonium sulfate, respectively. Protein was purified by Sephadex A-25, G-75, G-100 and G-200, and identified its protein fraction by polyacrylamide gel electrophoresis. Amino acids composition of protein in white sesame was analyzed by automatic amino acid analyzer. Protein contents of white sesame, black sesame and sesame meal are 20.5%, 19.2%, and 44.7%, respectively. n-Hexane was the most suitable solvent for extraction of oil from sesame. Crude protein precipitation was better in higher pH. The protein extraction was more effective with the solution containing sodium chloride tinder the pH 8. Globulin in total protein was high and prolamin was less than in other cereal proteins. Glutamic acid contents of white sesame and sesame globulin were 17.1%, and 20%, respectively. Both proteins contained relatively high levels of essential amino acids. 12-13 bands were found in water soluble protein and 2 bands in salt soluble protein were detected by the disc gel electrophoresis, and were identified in both of white and black sesame. The salt soluble protein of white sesame could be purified by Sephadee G-100 and G-200.

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Protein Profiles of Major Korean Rice Cultivars

  • Wei, Chuanha;Kwon, Oh-Yun;Liu, Xi-Wen;Kim, Hyoung-Chin;Yoon, Won-Kee;Kim, Hwan-Mook;Kim, Mee-Ree
    • Preventive Nutrition and Food Science
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    • v.12 no.2
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    • pp.103-110
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    • 2007
  • The protein profiles among Korean rice cultivars were assessed by total protein determination, solubility fractionation, SDS-PAGE analysis and scanning densitometry. In the extraction of protein, the SDS/urea system at a neutral pH was more efficient than that at alkaline pH. The determination of total protein showed that the protein content was similar among cultivars, ranging from 87.9 to 92.7 mg/g dry weight. Additionally, the water/NaCl-soluble protein fraction, containing 14${\sim}$16 kDa albumin and 22 kDa globulin ${\alpha}$-globulin, was also similar among cultivars, with a range of 9.94 to 11.98 mg/g dry weight. The SDS-PAGE/densitometry of total protein showed that there was no discernable difference in proteins of higher molecular weights among various cultivars, whereas the amount of lower molecular weight proteins (14${\sim}$16 kDa) is somewhat variable among cultivars. Furthermore, SDS-PAGE analysis of water/NaCl-soluble and propanol-soluble fractions indicates that there is a discernible change in the content of albumin, globulin or prolamin among cultivars. Thus, the PAGE/densitometry method, preceded by solubility fractionation, is useful for examining differences in protein profiles of rice cultivars.

STUDIES ON THE EXTRACTION OF SEAWEED PROTEINS 4. Precipitation Conditions and Nutritional Evaluation of Isolated Seaweed proteins (해조단백질 추출에 관한 연구 4. 추출단백질의 심전조건 및 영양적 평가)

  • WOO Soon-Im;RYU Hong-Soo;LEE Kang-Ho
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.12 no.4
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    • pp.225-234
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    • 1979
  • For the effective utilization of diverse and abundant resource of seaweeds in Korea as a food protein supplment, extraction conditions of water, salt, and alkali soluble proteins were investigated in previous work(Ryu and Lee, 1977: Lee et al., 1977: Lee et al., 1978). The present study as a part of the serial work was thus aimed to find the conditions of isolation and purification of extracted proteins, and to evaluate the nutritional quality of the isolated seaweed proteins in terms of amino acid composition, chemical score, protein score, modified essential amino acid index(MEAAI), and in vitro digestibility presented as pepsin-pancreatin digest residue index (PPDRI). As for the isolation of extracted proteins, TCA treatment was more effective for the proteins from rhodophyceae and Chlorophyceae while the precipitation at isoelectric point was more desirable for Phaeophyceae proteins. In amino acid composition, water soluble protein fraction was superior to the other fractions in Porphyra suborbiculata whereas both water and alkali soluble fractions seemed to bo more benefitial for Enteromorpha linza and Ulva pertusa; the extraction with alcohol-alkali mixed solvent for Undaria pinnatifida and Sargassum fulvellum. Glutamic acid and aspartic acid content was particularly high in all protein fractions examined. The total amino acid content of Porphyra suborbiculata and Enteromorpha linza was almost equivalent to that of dried whole egg although the essential amino acid content was lower. A comparative analysis was made on the inedexes between raw seaweed powder and isolated protein. Chemical score of Porphyra suborbiculata and Ulva pertusa was approximately 35 and 56 in cafes of raw powder and isolated protein respectively while only 10 to 16 for raw powder of Undaria pinnatifida and Sargassum fulvellum and 30 to 35 for their isolated proteins. Protein score of all isolated proteins was in the range of 63 to 73 which indicates that isolated protein would be mere valuable than the fern of raw seaweed powder. Digestibility by means of PPDRI was found to be extremely low in case of raw powder but it could be doubled in case of isolated protein yielding 67 to 70 for Porphyra suborbiculata and Ulva pertusa.

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Postmortem Changes in the Physico-Chemical Characteristics of Korean Native Chicken (저장기간에 따른 한국산 토종닭고기의 품질 특성)

  • 성삼경;권연주;김대곤
    • Korean Journal of Poultry Science
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    • v.25 no.2
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    • pp.55-64
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    • 1998
  • This study was carried out to investigate the postmortem changes in physico-chemical characteristics of chicken meat with different breeds. Thigh and breast meats from Korean Native Chicken(KNC, 15-wk old), Wangchoo(15-wk old), and broiler(7-wk old) were stored at 5 ˚C. Differences in postmortem pH changes were not recognized among breeds, and pH showed by the lowest value at the 1st day of postmortem in all breeds. Breast meat had tendency to drop pH faster than thigh meat. Heme pigment contents showed no differences among breeds. KNC showed the lowest cholesterol contents in all breeds, total collagen contents showed the lowest value at the 1st day of postmortem, and thereafter it was gradually increased. Heat soluble collagen contents was lowest in Wangchoo. Water soluble and salt soluble protein showed the lowest extractability at the 1st day of storage. Broiler showed the highest extractability of these proteins and Wangchoo showed the lowest. Water holding capacity(WHC) had increasing tendency whilst cooking loss had decreasing tendency by the ageing. WHC of breast and thigh meat showed the highest values in KNC and broiler, respectively. Myofibrillar fragmentation index (MFI) was significantly increased in all breeds by the ageing. Breast and thigh meat showed almost same MFI in KNC and broiler, and in KNC and Wangchoo, respectively. Hardness of breast meat showed decreasing tendency by the ageing.

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Localization of Germin Genes and Their Products in Developing Wheat Coleoptiles

  • Caliskan, Mahmut;Ozcan, Birgul;Turan, Cemal;Cuming, Andrew C.
    • BMB Reports
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    • v.37 no.3
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    • pp.339-342
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    • 2004
  • Germination is a process which characterized with nescient synthesis of genes. Among the genes synthesized during the germination of wheat embryos, germin genes, proteins and their enzymatic activity were defined. Germin is a water soluble homopentameric glycoprotein which is remarkable resistant to degradation by a broad range of proteases including pepsin. Germin proteins found to have strong oxalate oxidase activity which produces hydrogen peroxide by degrading oxalic acid. The current study, aimed to localize the germin genes, proteins and enzymatic activities in developing coleoptiles which is a rapidly growing protective tissue of leaf primordium and shoot apex. Non-radioactively abeled germin riboprobes were employed to localize germin mRNAs in situ. FITC (Fluorescein isothiocyanate) and alkaline phosphatase linked anti-germin antibodies were used to localize germin proteins under the fluorescence and light microscopy and finally germin enzymatic activity was localized by using appropriate enzyme assay. The results revealed that in coleoptiles germin genes, proteins and their enzymatic activity were predominantly associated with the cells of epidermis and vascular bundle sheath cells.