• Title/Summary/Keyword: water-soluble proteins

Search Result 121, Processing Time 0.029 seconds

Effects of Chilling and Packing Methods on Physico-chemical Properties of Cold-stored Chicken Breast and Thigh Meats (냉각방법과 포장방법에 따른 냉장계육의 이화학적 특성 변화)

  • 박구부;하정기;진상근;박태선;신택순;이정일
    • Korean Journal of Poultry Science
    • /
    • v.24 no.1
    • /
    • pp.17-28
    • /
    • 1997
  • This experiment was carried out to investigate the effects of different chilling and packing methods on physico-chernical properties of cold-stored chicken breast and thigh meats. Dehoned chicken breast and thigh meats were chilled either air spray or ice-water immersion method. The chilled meats were either vacuum packed or atmosphere packed, and stored at -2˚C for 1, 3, 7, 11, 15, and 20 days. The pH of both immersion chilled meats and vacuum packed meats were higher than those of their counterparts(P<0.05). The pH of atmosphere packed meats increased as the storage period extended. The moisture contents of vacuum packed meats were remarkably higher than those of atmosphere packed meats. The pH of all treatments decreased as the storage period extended. The shear values of air spray chilled and vacuum packed breast meats were significantly higher than immersion chilled and vacuum packed ones. However, immersion chilled and atmosphere packed breast meats were significantly higher than those of air spray chilled and atmosphere packed breast meats. The shear values of immersion chilled and vacuum packed thigh meats were significantly higher than those of immersion chilled and vacuum packed thigh meats. In atmosphere packed thigh meats, air spray chilling method showed higher shear values than those of immersion chilled thigh meats. In thigh muscle, tenderness values tended to decrease as the storage period extended(P<0.05). Contents of water soluble proteins of vacuum packed and air spray chilled breast and thigh meats were higher than those of their counterparts as the storage period extended(P<0.05). The contents of water soluble proteins significantly decreased as the storage period extended. Salt soluble proteins of atmosphere packed breast and thigh meats were remarkably higher than those of vacuum packed ones(P<0.05). Total lipid contents of atmosphere packed and air spray chilled breast and thigh meats were higher than those of atmosphere packed and immersion chilled meats as the storage period extended. The vacuum packed meats were significantly higher in total lipid contents than those of atmosphere packed meats. The storage period decreased the total lipid contents of cold chicken, Major fatty acids in cold-stored chicken were oleic, palmitic, linoleic and stearic acids, regardless of chilling method. Unsaturated fatty acids of all treatments decreased, but saturated fatty acids increased as the storage period extended.

  • PDF

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

  • LEE Keun-Tai;PARK Seong-Min;CHOI Hyeon-Mee;CHOI Sang-Hyun;MOON Bo-In;KIM Kyung-Tae;SONG Ho-Su
    • Korean Journal of Fisheries and Aquatic Sciences
    • /
    • v.34 no.5
    • /
    • pp.473-477
    • /
    • 2001
  • Chitosan has been used as an effective adsorbant for the treatment of wastewater from seafood processing. We investigated the effects of deacetylation degree (DD) and molecular weight (MW) of chitosan on protein adsorption ability and also the optimum conditions of chitosan treatment for protein adsorption in 3 kinds of protein (albumin, hemoglobin and albumin-myoglobin mixture) solutions. The higher deacetylation degree and the lower molecular weight chitosan, the higher adsorption for water soluble proteins was accomplished. The optimum pHs for adsorption of albumin, hemoglobin and albumin-myoglobin mixture (4: 1, w/w) were 4.0, 7.0 and 4.0 respectively and the optimum time was $3\~4$ hrs for all proteins. Sodium chloride in the model system of protein solution was a preventing factor for protein adsorption ability of chitosan (DD=$80\%$, MW=350 kDa).

  • PDF

Protease Inhibitors in Porcine Colostrum: Potency Assessment and Initial Characterization

  • Zhou, Q.;He, R.G.;Li, X.;Liao, S.R.
    • Asian-Australasian Journal of Animal Sciences
    • /
    • v.16 no.12
    • /
    • pp.1822-1829
    • /
    • 2003
  • Porcine colostrum and milk were separated into the acid-soluble and casein fractions by acidification followed by centrifuge. The acid-soluble fraction of porcine colostrum was further separated by liquid chromatography and anisotropic membrane filtration. Trypsin and chymotrypsin inhibitory capacity in porcine colostrum, milk and their components was determined by incubating bovine trypsin or chymotrypsin in a medium containing their corresponding substrates with or without addition of various amounts of porcine colostrum, porcine milk or their components. The inhibition of insulin-like growth factor I (IGF-I) and epidermal growth factor (EGF) degradation in pig small intestinal contents by porcine colostrum was measured by incubating iodinated IGF-I or EGF with the intestinal contents with or without addition of porcine colostrum. Degradation of labeled IGF-I or EGF was determined by monitoring the generation of radioactivity soluble in 30% trichloroacetic acid (TCA). The results showed that porcine colostrum had high levels of trypsin and chymotrypsin inhibitory activity and increased the stability of IGF-I and EGF in pig intestinal contents. The inhibitory activity declined rapidly during lactation. It was also found that trypsin and chymotrypsin inhibitory activity and the inhibition on IGF-I and EGF degradation in the acid-soluble fraction were higher than that in the casein fraction. Heat-resistance study indicated that trypsin inhibitors in porcine colostrum survived heat treatments of $100^{\circ}C$ water bath for up to 10 min, but exposure to boiling water bath for 30 min significantly decreased the inhibitory activity. Compared with the trypsin inhibitors, the chymotrypsin inhibitors were more heatsensitive. Separation of the acid-soluble fraction of porcine colostrum by liquid chromatography and anisotropic membrane filtration revealed that the trypsin and chymotrypsin inhibitory capacity was mainly due to a group of small proteins with molecular weight of 10,000-50,000. In conclusion, the present study confirmed the existence of high levels of protease inhibitors in porcine colostrum, and the inhibition of porcine colostrum on degradation of milk-borne growth factors in the pig small intestinal tract was demonstrated for the first time.

Comparison of the Nutritional Composition of Bullfrog Meat from Different Parts of the Animal

  • Zhu, Yanli;Bao, Min;Chen, Chong;Yang, Xiaoli;Yan, Wenliang;Ren, Fazheng;Wang, Pengjie;Wen, Pengcheng
    • Food Science of Animal Resources
    • /
    • v.41 no.6
    • /
    • pp.1049-1059
    • /
    • 2021
  • The objective of this study was to evaluate the nutritional content of bullfrog meat from different parts of the animal, including fore-chest, thigh and calf. Bullfrog meat was found to be a rich source of proteins, essential amino acids and minerals, but with a low fat content, compared with other aquatic meat products. There was no significant difference (p>0.05) between thigh and calf in mineral content (K, P, Na, Mg, Ca, Zn, Fe, Cu, and Mn), but the contents of K, P, and Mg were higher in thigh and calf than in the fore-chest (p<0.05). The salt-soluble, water-soluble and insoluble protein bands in sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) electrophoresis, from fore-chest, thigh and calf were similar, with the most abundant bands being 35 kDa (salt-soluble protein), 35-48 kDa (water-soluble protein) and 48 kDa (insoluble protein). The results showed that the insoluble protein content in the fore-chest meat was higher than that in the thigh meat and calf meat, but the salt-soluble protein fraction was the most abundant in thigh meat. These results showed that the nutrients in different parts of bullfrog meat were different.

Effect of Washing and Additives on Gel Formation of Squid Surimi

  • LEE Nahm-Gull;CHO Young-Je
    • Korean Journal of Fisheries and Aquatic Sciences
    • /
    • v.29 no.6
    • /
    • pp.754-760
    • /
    • 1996
  • Effects of washing and additives on the texture of squid surimi gel which has been known to hard to gelation due to high protease activities and many water solubles were studied by SDS-PAGE, compression test, jelly strength and transmission electron microscopy analysis (TEM). Myosin (205 kDa) heavy chain was the major protein in water soluble fractions. It was impossible to make a gel after washing of the minced squid meat. These results suggested that squid (Todarodes pacificus) minced meat does not need a washing for good jelly products. $3.0\%$ of bovine plasma protein (BPP) produced the hardest gel ($16\%$ harder than the control) among the additives including egg white (EW), potato extracts (PE) and transglutaminase-K (TG-K) by compression test (P>0.05). Microstructure of control, $2\%$ EW and $4\%$ TG-K treated gels showed a sponge-like structure with more vacant space. Gels containing $3\%$ BPP formed the most rigid and arranged networks. Those results indicates that poor gel-network formation Was due to the degradation of myofibrillar proteins by proteases contained in the minced meat, which result in non-interlinkage.

  • PDF

Angiotensin I-converting Enzyme Inhibitory Activities of Porcine Skeletal Muscle Proteins Following Enzyme Digestion

  • Katayama, K.;Fuchu, H.;Sakata, A.;Kawahara, S.;Yamauchi, K.;Kawamura, Y.;Muguruma, M.
    • Asian-Australasian Journal of Animal Sciences
    • /
    • v.16 no.3
    • /
    • pp.417-424
    • /
    • 2003
  • Inhibitory activities against angiotensin I-converting enzyme (ACE) of enzymatic hydrolysates of porcine skeletal muscle proteins were investigated. Myosin B, myosin, actin, tropomyosin, troponin and water-soluble proteins extracted from pork loin were digested by eight kinds of proteases, including pepsin, $\alpha$-chymotrypsin, and trypsin. After digestion, hydrolysates produced from all proteins showed ACE inhibitory activities, and the peptic hydrolysate showed the strongest activity. In the case of myosin B, the molar concentration of peptic hydrolysate required to inhibit 50% of the activity increased gradually as digestion proceeded. The hydrolysates produced by sequential digestion with pepsin and $\alpha$-chymotrypsin, pepsin and trypsin or pepsin and pancreatin showed weaker activities than those by pepsin alone, suggesting that ACE inhibitory peptides from peptic digestion might lose their active sequences after digestion by the second protease. However, the hydrolysates produced by sequential digestion showed stronger activities than those by $\alpha$-chymotrypsin, trypsin or pancreatin alone. These results suggested that the hydrolysates of porcine meat were able to show ACE inhibitory activity, even if they were digested in vivo, and that pork might be a useful source of physiologically functional factors.

Effects of Light and Water Soluble Proteins on the Lipid Oxidation of Meat Emulsion Model System during Refrigerated Storage (광 조사 및 차단 조건에서의 고기모형 유화물의 지방산화에 미치는 수용성 단백질의 효과)

  • Park, Hyung-Il;Chung, Myung-Sub;Lee, M.
    • Korean Journal of Food Science and Technology
    • /
    • v.29 no.3
    • /
    • pp.395-399
    • /
    • 1997
  • Meat model emulsions ware prepared with salt-soluble protein and soybean oil. Effects of water-soluble protein (WSP) on the meat model emulsion treated with/without BHT during 8 day storage $5^{\circ}C$ under both dark and light illumination were studied by measuring POV and TBA. An emulsion without BHA and WSP was used as a control. Under light storage, there was no significant difference in peroxide values between the control and the sample treated with BHA except the 2nd day of storage. However, TBA values of the sample treated with BHA were significantly (p<0.05) lower than those of control except the 4th day of storage. TBA and POV of the samples treated with WSP and WSP + BHA were higher than control after 4th day of storage under light. That is, water soluble protein, which was composed mainly of myoglobin, increased lipid oxidation under light storage. The similar trends were also shown in the samples stored under dark. These results suggested that acceleration of lipid oxidation of the meat model emulsions by water soluble protein (WSP) under both light and dark might not be due to the singlet oxygen formation, but due to superoxide anion formed.

  • PDF

STUDIES ON THE EXTRACTION OF SEAWEED PROTEINS 1. Extraction of Water Soluble Proteins (해조단백질의 추출에 관한 연구 1. 수용성 단백질의 추출)

  • RYU Hong-Soo;LEE Kang-Ho
    • Korean Journal of Fisheries and Aquatic Sciences
    • /
    • v.10 no.3
    • /
    • pp.151-162
    • /
    • 1977
  • Distribution of marine algae is diverse in Korea and the resource of edible algae is abundant marking 239,037 tons of yearly production in 1976. They have been known as a protein source and used as a supplement in Korean diet. It is necessary to estimate the potentiality and properties of usable algal proteins especially as food resources and studies of extraction and separation of the proteins, therefore, are basically required for this purpose. In this study, the influence of various factors including the sample treatment, extraction time and temperature, sample us extraction solvent ratio and pH upon the extractability of the water soluble protein was determined. And the effect of precipitation treatment for isolation of the algal protein from the extracts was also tested. Nine species of algae, the major ones in consumption as food namely Porphyra suborbiculata, Undaria pinnatifida, Hizikia fusiforme, Sargassum fulvellu, Enteromorpha linza, Codium fragile, Sargassum kjellmanianum and Ulva pertusa were collected as fresh from Kijang, Yangsan Gun, in the vicinity of Busan city. The content of crude protein $(N\times6.25)$ of the algae ranged from $9.46\%\;to\;24.14\% showing the highest value in Porphyra suborbiculata and the minimum in Hizikia fusiforme. In the effort of maceration of blending methods on the extractability, immersion freezing in dry ice-methanol solution appeared most effective yielding 1.5 to 2.5 times extractability than that of the mortar grinding method. The effect of the ratio of sample vs solvent on extractability differed from species. It was enhanced at the ratio of 1:20 (w/v) in Ulva pertusa and Enteromorpha linza while the ratio was 1:30 (w/v) for Cedium fragile, Undaria pinnatifida, Hizikia fusiferme, Sargassum fulvellum and Porphyra suborbiculata and 1:40 for Sargassum kjellmanianum respectively. The effect of extraction time and temperature was revealed differently from species which might be caused by differences in the constitution of algal tissues resulting in that the extraction for 1 hour at $50^{\circ}C$ gave the maximum extractabilily in Ulva pertusa and Enteromorpha linza, 2 hours in Porphyra suborbiculata, Hikikia fusiforme, Undaria pinnatifida, Sargassum kjellmanianum and 3 hours in Codium fragile. And the extractability was higher at $50^{\circ}C$ to $60^{\circ}C$ for the most of the tested samples except Hizikia fusiforme. The optimum pH for the extraction was 9 to 12. The recovery of extractable nitrogen to the total nitrogen was $63\%$ in average with the first extracts and $8.6\%$ with the second extracts respectively. Both extracts were prepared by 2 hour extraction at $50{\pm}1^{\circ}C$ with dry ice-methanol frozen and seasand macerated materials. And these conditions assumed to be an optimum for the extraction of water soluble algal proteins since the nitrogen content after the first extraction covered $90\%$ of the total water extractable nitrogen. In the precipitation of the extracted proteins, Barnstein method and methanol treatment seemed to be more efficient than other precipitation methods.

  • PDF

Trypsin Inhibitors from Various Soybean Varieties (대두 품종별 트립신 인히비터에 관하여)

  • Kim, Hyung-Gap;Kim, Myung-Chan;Chang, Kwon-Yawl;Kim, Jong-Kyu
    • Korean Journal of Food Science and Technology
    • /
    • v.14 no.2
    • /
    • pp.106-111
    • /
    • 1982
  • To investigate the soybean trypsin inhibitors from seven varieties of soybeans and their twenty one $F_1-hybrids$, water soluble proteins were extracted. Trypsin inhibitors were isolated from those proteins and purified by sephadex G-75 column chromatography and polyacrylamide gel electrophresis. Total 16 kinds of trypsin inhibitors were isolated. From each variety of soybeans, $5{\sim}12$ kinds of trysin inhibitors could be detected and among them, 5 kinds of trypsin inhibitors were mainly distributed.

  • PDF