• Title/Summary/Keyword: Protein isolate

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Effects of Soy Protein and Isoflavones on Bone Markers and Hormones in Growing Male Rats (콩 단백질과 Isoflavones가 성장기 수컷 흰쥐에서 골 지표와 호르몬에 미치는 영향)

  • 최미자
    • Journal of Nutrition and Health
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    • v.36 no.5
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    • pp.452-458
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    • 2003
  • Soybean is a rich source of isoflavones such as genistein and daidzein. Soy isoflavones have both weak estrogenic and anti-estrogenic effects and are structurally similar to tamoxifen, an agent that has an effect similar to that of estrogen in terms of reducing postmenopausal bone loss. The purpose of this study was to determine the effects of differences in protein source (casein vs soy) and isoflavone levels (reduced vs higher levels) on selected bone markers and hormones in growing male rats. Thirty weanling Sprague-Dawley young rats were divided into 3 groups: The control group was fed a casein-based diet, the soy concentrate group was fed soy protein with totally reduced isoflavones content (isoflavones 0.07 mg/g protein), and the soy isolate group was fed soy protein with a higher than normal isoflavones content (isoflavones 3.4 mg/g protein). The degree of bone formation was estimated by measuring serum osteocalcin and alkaline phosphoatase (ALP). By determining collagen cross-linkage by immunoassay and correcting with creatinine values, the bone resorption rate was compared. Serum osteocalcin, growth hormone, estrogen and calcitonin were analyzed using radio immunoassay kits. The bone formation marker and ALP activity were differentiated by protein source, showing higher values than casein in feeding either soy isolate or soy concentrate. In this study using growing rats, the differences in isoflavone contents were not a significant factor in either bone formation or bone reaborption markers. Moreover, the soy isolate group had significantly higher levels of growth hormone than the casein group. The findings of this study suggest that growth hormone is partially responsible for its bone-formation effects in young growing rats. Soy protein and the isoflavones in soy protein are beneficial for bone-formation in growing male rats. Therefore, exposure to soy protein and isoflavones early in life may have long-term health benefits in preventing bone diseases such as osteoporosis. Further study to evaluate the mechanism of action of isoflavones on bones is warranted. (Korean J Nutrition 36(5): 452∼458, 2003)

Expression of major piroplasm protein(p33)of Theileria sergenti (Korean isolate) and its immunogenicity in guinea pigs

  • Kang, Seung-Won;Kweon, Chang-Hee;Choi, Eun-Jin;Yoon, Yong-Dhuk
    • Parasites, Hosts and Diseases
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    • v.37 no.4
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    • pp.277-283
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    • 1999
  • To investigate the development of a subunit vaccine against theileriosis in cattle, the DNA fragments encoding piroplasm surface protein (p33) of Theileria sergenti of a Korean isolate were expressed in baculoviruses. The expressed p33 was characterized by indirect fluorescent antibody (IFA) and western blotting analysis. The expression of p33 was mainly detected on the surface of infected Sf21 cells by IFA. The immunoblotting analysis revealed the presence of a same molecular weight protein band of p33. The antigenicity of expressed polypeptide was further examined through the inoculation of a guinea pig. The sera of guinea pigs immunized with p33 expressed cell Iysate showed similar fluorescent antibody patterns and reacted with the same molecular weight protein of T. sergenti in immunoblotting analysis, thus indicating that this protein can be a promising candidate for a subunit vaccine in the future.

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Functional Properties of Modified Soybean Protein Isolate by Dimethylglutarylation (Dimethylglutarylation에 의한 변형대두단백질의 기능적 특성)

  • Choi, One-Kyun;Jung, Chul-Won
    • Journal of the Korean Society of Food Culture
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    • v.14 no.5
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    • pp.477-485
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    • 1999
  • This study was conducted to improve the functional properties of soybean protein isolate by dimethylglutarylation and acetylation. Amino acid composition and solubility of modified soybean protein by dimethylglutarylation were not changed, but lysine and trypsin inhibitor activity was decreased an isoelectric point was moved from pH5 to pH4 as a result of modification. Emulsification capacity and stability, foaming capacity and thermal stability were increased by the modification. In that 91% dimethylglutarylated protein did not coagulate when heating at $100^{\circ}C$ for 20 min. while its foaming stability was decreased. Whereas specific gravity was decreased by the modification of the soybean protein, relative viscosity and whiteness were improved. Generally, dimethylglutarylation produced more conformational changes in protein system than did in acetylation.

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Characteristics of ${\delta}$-Endotoxin Protein Produced from Bacillus thuringiensis subsp. kurstaki KB099 Isolate Showing High Bioactivity against Spodoptera litura (담배거세미나방(Spodoplera lilura)에 높은 살충활성을 나타내는 Bacillus thuringiensis subsp. kurstaki KB099 균주의 내독소 단백질 특성)

  • Jung, Sun-Young;Seo, Mi-Ja;Youn, Young-Nam;Yu, Yong-Man
    • The Korean Journal of Pesticide Science
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    • v.14 no.4
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    • pp.446-455
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    • 2010
  • The characteristics of parasporal inclusion body from Bacillus thuringiensis subsp. kurstaki KB099 isolate which is high bioactive to the tobacco cutworm, Spodoptera litura, were examined. Parasporal inclusion of B. thuringiensis subsp. kurstaki KB099 isolate showed only 1 band at 130 kDa compared with B. thuringiensis subsp. kurstaki HD-l isolate producing 2 protein bands at 130 kDa and 60 kDa from by SDS-PAGE analysis without any enzyme treatment. Also, we confirmed that gut extract of sensitive S. litura KB099 isolate had digested only 60 kDa ${\delta}$-endotoxin protein. When the digestive enzyme of sensitive insect responsible for parasporal inclusion from KB099 and HD-l isolate was treated to each of them, protein band 60 KDa of KB099 was maintained up to 12 hours but all bands of HD-l were disappeared within 6 hours. In KB099 isolate, 6 genes (Cry1Aa, Cry1Ab, Cry1Ac, Cry1C, Cry1D and Cry1I) were identified by PCR analysis. Also, $Cry^-$ mutant of KB099 isolate was investigated by phase- contrast microscope, SDS-PAGE and PCR.

Effects of Functional Properties of Soy Protein Isolate and Qualities of Soybean Curd upon Proteolytic Hydrolysis (효소처리가 대두단백질의 기능특성과 두부의 품질에 미치는 영향)

  • Han, Jin-Suk;Hwang, In-Kyeong
    • Korean Journal of Food Science and Technology
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    • v.24 no.3
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    • pp.294-299
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    • 1992
  • This study was to examine the effect of functional properties of soy protein isolate(SPI) and qualities of soybean curd upon proteolytic hydrolysis. SPI was hydrolyzed using proteolytic enzyme, bromelain. The protein content of SPI by microkjeldahl method was 84% and the degree of hydrolysis in modified soy protein isolate(MSPI) was 2.7%. The solubility of MSPI was higher than that of control at various pH tested and proteolytic hydrolysis was increased emulsion formation and foam expansion while decreased emulsion stability, foam stability and calcium precipitation. Modified soybean curdI, standard soybean milk: Modified soybean milk=3:1, was soft and springy soybean curd when the texture properties of soybean curd were tested by texture profile analysis using Instron and sensory evaluation. The rheological model of soybean curds was investigated by stress relaxation test. The analysis of relaxation curve revealed that the rheological behavior of soybean curds could be expressed by 7-element generalized Maxwell model. The equilibrium modulus and modulus of elasticity decreased as the ratio of modified soybean milk was increased.

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Effect of Red Bean Protein and Microbial Transglutaminase on Gelling Properties of Myofibrillar Protein (적소두단백질(Red Bean Protein)과 Transglutaminase를 첨가한 돈육 근원섬유 단백질의 물성 증진 효과)

  • Jang, Ho-Sik;Chin, Koo-Bok
    • Food Science of Animal Resources
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    • v.31 no.5
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    • pp.782-790
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    • 2011
  • The effects of soy protein isolate (SPI) and red bean protein isolate (RBPI) on gelling properties of pork myofibrillar protein (MP) in the presence of microbial transglutaminase (MTG) were studied at 0.45 M NaCl. MP paste was incubated with MTG (0.1%) at various levels (0.1, 0.3, 0.5, and 1%) of SPI and RBPI before incubating at $4^{\circ}C$ for 4 h. The rheological property results showed that MP gel shear stress increased with increasing RBPI concentration. Cooking yield (CY) of the MP gel increased with increasing RBPI and SPI, whereas gel strength (GS) was not affected by adding RBPI or SPI. Thus, effects of incubation time (0, 4, 8, 10, and 12 h) were measured at 0.1% SPI and RBPI. GS values of the MP gel at 10 and 12 h were similar and were higher than those of the others. CY values were highest when RBPI (0.1%) was added, regardless of incubation time. The protein patterns indicated that incubating the MP with MTG for 10 h resulted in protein crosslinking between MP and RBPI or SPI. Based on these results, RBPI and SPI could be used as an ingredient to increase textural properties and cooking yield of meat protein gel.

Evaluation of Porcine Myofibrillar Protein Gel Functionality as Affected by Microbial Transglutaminase and Red Bean [Vignia angularis] Protein Isolate at Various pH Values

  • Jang, Ho Sik;Lee, Hong Chul;Chin, Koo Bok
    • Food Science of Animal Resources
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    • v.35 no.6
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    • pp.841-846
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    • 2015
  • This study was investigated to determine the effect of microbial transglutaminase (MTG) with or without red bean protein isolate (RBPI) on the porcine myofibrillar protein (MP) gel functionality at different pH values (pH 5.75-6.5). Cooking yield (CY, %), gel strength (GS, gf), differential scanning calorimetry (DSC), and scanning electron microscopy (SEM) were determined to measure gel characteristics. Since no differences were observed the interaction between 1% RBPI and pH, data were pooled. CY increased with the addition of 1% RBPI, while it was not affected by pH values. GS increased with increased pH and increased when 1% RBPI was added, regardless of pH. There were distinctive endothermic protein peaks, at 56.55 and 75.02℃ at pH 5.75, and 56.47 and 72.43℃ at pH 6.5 in DSC results, which revealed decreased temperature of the first peak with the addition of 1% RBPI and increased pH. In SEM, a more compact structure with fewer voids was shown with the addition of 1% RBPI and increased pH from 5.75 to 6.5. In addition, the three-dimensional structure was highly dense and hard at pH 6.5 when RBPI was added. These results indicated that the addition of 1% RBPI at pH 6.5 in MTG-mediated MP represent the optimum condition to attain maximum gel-formation and protein gel functionality.

Effect of Phytate on the Electrophoretic Behavior of Rapeseed Protein Isolate (분리 유채단백의 전기영동 패턴에 미치는 Phytate의 영향)

  • Cho, Hee-Kyung;Yoon, Jae-Young;Lee, Su-Rae
    • Korean Journal of Food Science and Technology
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    • v.24 no.3
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    • pp.284-288
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    • 1992
  • This study was undertaken to investigate the effect of pH and phytate level on the solubility of the protein due to binding between phytate and low-phytate rapeseed protein isolate by means of SDS-polyacrylamide gel electrophoresis. Results showed that the number of protein bands decreased by the increasing amount of phytate added to the soluble extract at pH 2.0 and 5.0 whereas there was no change at pH 11.5. Among 18 bands of rapeseed proteins at pH 2.0, seven bands (105.8, 52.3, 37.3, 34.8, 26.3, 21.3, 18.4 KDa) were removed by precipitation with 100 mg phytate addition and six bands (78.8, 46.5, 19.4, 16.8, 11.7, 8.5 KDa) further disappeared by 150 mg phytate addition. Among 15 bands at pH 5.0, only four bands disappeared by phytate addition. It is suggested that the functionality of rapeseed protein isolate can be improved by lowering the phytate content.

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Technological Studies on Textured Soybean Protein (Part I) -Effect of Drying Process on Gelling Properties of Soybean Protein Isolate- (대두단백육(大豆蛋白肉)의 제조(製造)에 관한 연구(硏究) (제 1 보(第 1 報)) -건조공정(乾燥工程)이 분리대두단백(分離大豆蛋白)의 Gel 성질에 미치는 영향-)

  • Moon, Juhn-Woong
    • Korean Journal of Food Science and Technology
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    • v.2 no.2
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    • pp.49-55
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    • 1970
  • In preparation of textured soybean protein, drying process of the isolated protein affected its gelling property and other related characteristics such as water holding capacity and viscosity. In model systems, denaturation of the protein, as determined in terms of nitrogen solubility index (NSI), was appeared to be a parameter of the gel strength of soybean protein isolate. The gel strength was maximum when the protein was denatured properly during drying process of which the NSI was 43 in this experiment and decreased at either the higher or the lower NSI. It indicated that proper denaturation of the protein during drying operation is advantagous for the preparation of textured soybean protein but not neccesary to make highly undenatured one.

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Development and Comparative Evaluation of Imitated Fiber from Different Protein Sources Using Wet-Spinning

  • Swati Kumari;So-Hee Kim;Chan-Jin Kim;Yong Sik Chung;Young-Hwa Hwang;Seon-Tea Joo
    • Food Science of Animal Resources
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    • v.44 no.5
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    • pp.1156-1166
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    • 2024
  • Texture is a major challenge in addressing the need to find sustainable meat alternatives, as consumers desire alternative meat to have a sensory profile like meat. In this study, the fabrication of imitated muscle fiber (IMF) is performed by introducing different kinds of protein sources, with an effective bottom-up technique- wet spinning. Herein, the protein sources (pea protein isolate, wheat protein, and myofibrillar paste) were combined with sodium alginate to stimulate the bonding with the coagulation solution for fabrication. It has been found that the fabrication of IMF is possible using all the protein sources, however, due to the difference in protein structure, a significant difference was observed in quality characteristics compared to conventional meat. Additionally, combination of wheat protein and pea protein isolate has given similar values as conventional meat in terms of some of the texture profiles and Warner-Bratzler shear force. In general, the optimization of protein sources for wet spinning can provides a novel way for the production of edible fiber of alternative meat.