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Detection of the End Point Temperature of Thermal Denatured Protein in Fish and Chicken Meat Through sds-page electrophoresis

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Journal of Ocean University of China 2009年第1期8卷 95-99页

作者： GAO Hongwei MAO Mao LIANG Chengzhu LIN Chao XIANG Jianhai ）Institute of Oceanology Chinese Academy of Sciences Qingdao 266003 P. R. China College of Food Science and Engineering Ocean University of China Qingdao 266003 P. R. China Shandong Entry-Exit Inspection and Quarantine Bureau of P. R. China Qingdao 266003 P. R. China

Sodium dodecyl sulfate polyacrylamide gel electrophoresis (sds-page) was applied in the detection of the end point temperature (EPT) of thermal denatured protein in fish and meat in this study. It was also used in studying the thermal denatured temperature range of proteins in salmon and chicken meat. The results show that the temperature ranges of denatured proteins were from 65 ℃ to 75 ℃ , and these temperature ranges were influenced by the processing methods. Through sds-page, the features of repeated heating thermal denatured proteins under the same temperature and processing time were studied. The electrophoresis patterns of thermal denatured proteins determined through repeated heating at the same temperature did not exhibit any change. For the detection of cooked fish and meat samples, they were subjected to applying the sds-page method, which revealed an EPT ranging from 60 ℃ to 80 ℃ .

关键词： end point temperature detection sds-page electrophoresis

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Effects of extrusion conditions on the physicochemical properties of soy protein/gluten composite

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International Journal of Agricultural and Biological Engineering 2018年第4期11卷 230-237页

作者： Min Wu Yang Sun Chonghao Bi Fang Ji Borui Li Junjie Xing College of Engineering China Agricultural UniversityBeijing 100083China School of Materials Science and Mechanical Engineering Beijing Technology and Business UniversityBeijing 100048China Chinese Academy of Agricultural Engineering Beijing 100125China

Soybean protein-gluten blend was extruded using a co-rotating twin-screw *** of different extrusion conditions on the textural properties of extrudates were analyzed by central composite design through the evaluation of texturization index,water holding capacity,and hardness of extruded protein *** process variables including feed moisture content(40%-60%),screw speed(12-20 Hz),extrusion temperature(120℃-180℃),and gluten content(16%-32%)were studied by the nonlinear regression equations *** extrusion process was also optimized using response surface methodology(RSM).The influence of moisture content on the hardness of extrudate was the most *** optimized results,including feed moisture content,extrusion temperature,screw speed and gluten content were 49.18%-50.15%,155.24℃-159.86℃,16.41-16.73 Hz,20.00%-20.03%,*** microstructures of TISP products were analyzed by scanning electron microscopy(SEM)and the changes of protein molecules before and after extrusion were also analyzed by sds-page electrophoresis.

关键词： soybean protein gluten extrusion response surface methodology(RSM) sds-page electrophoresis Microstructural properties

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Coconut Press Cake Alkaline Extract—Protein Solubility and Emulsification Properties

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Food and Nutrition Sciences 2013年第9期4卷 29-37页

作者： Borges Chambal Bjorn Bergenstahl Petr Dejmek Department of Chemical Engineering Faculty of EngineeringEduardo Mondlane UniversityMaputoMozambique Department of Food Technology Engineering and Nutrition Lund UniversityLundSweden

The solubility and the emulsification properties of a crude freeze dried alkaline protein extract (APE), 30% protein, obtained from coconut milk press cake by one step extraction at pH 11, were characterized at pH 2 to 11, and the cream and subnatant fractions of the emulsion studied by sds-page electrophoresis. The protein solubility followed U profile, showing a minimum at pH 3 to 4, close to but not identical to reported iso-electric points of 4 - 5 for many coconut protein fractions. The extract showed good capacity to form oil-in-water emulsion outside the low solubility pH range. The bands that appeared to play a role in the emulsification were found at 32 and 42 kDa in sds-page electrophoresis, but the most predominant absorbed band was at 23 kDa.

关键词： Coconut Proteins Coconut Milk Press Cake Alkaline Extraction Oil-in-Water Emulsions Solubility sds-page electrophoresis

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Extraction of TypeⅤCollagen From Bovine Cornea and Its Structural Analysis

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Chinese Journal of Biomedical Engineering(English Edition) 2011年第3期20卷 125-129页

作者： WU Ji-min LI Zhi-hong WANG Peng-fei LI Ying YUAN Xiao-yan School of Materials Science and Engineering Tianjin University Tianjin 300072 China Institute of Medical Equipment Academy of Military Medical Sciences Tianjin 300161 China

We used bovine cornea as starting material, pepsin treatment in acetic acid solution to extract the mixture of type I and V collagens, and salt precipitation and dialysis to purify and isolate each type of the collagens. The preparation was analyzed using sodium dodecyl sulphate polyacrylamide gel electrophoresis. 2-mercaptoethanol used as reducing agent cut off the disulfide bonds, which was utilized to analyze the structure of disulfide bonds involved between α chains in some types of collagens. At the same time, we discovered that the structure of disulfide bonds among α chains potentially existed in the type V collagen prepared from the pepsin-treatment extraction at 4℃. Through quantitative analysis, we obtained that, compared with those pepsin-treated at 4℃, the relative molecular weights of α1 （V） and α 2 （V） subunits pepsin-treated at room temperature decreased by 4.6% and 6.0%, respectively. It is concluded that type V collagen can be prepared from bovine coruea by use of pepsin treatment, salt precipitation and dialysis. The interchain and/or intermolecular disulfide bonds potentially lie near the edges of termini of type V collagen molecules existing in extracellular matrix, and there are few of the intermolecular and/or intramolecular crosslinks formed by lysine or hydroxylysine or histidine residues in type V collagen.

关键词： type V collagen salt precipitating method sds-page electrophoresis

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Effect of Low Temperature Stress on Protein Content of Toona Sinensis Seedlings and Expression of Specific Protein

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Agricultural Science & Technology 2011年第5期12卷 651-654,677页

作者： YANG Yu-zhen CHEN Gang PENG Fang-ren Department of Life Science Zhengzhou Normal CollegeZhengzhou 450044 College of Forest Resources and Environment Nanjing Forestry UniversityNanjing 210037

[Objective] The paper was to study the changes of protein content and component in leaves of Toona Sinensis under low-temperature stress.[Method] Potted experiment was adopted,and sds-page electrophoresis was also used to analyze the dynamic changes of protein in *** leaves.[Result] Low temperature stress could change the content and component in leaves of ***,but different provenances had different performance under different temperatures,so did the same provenance under different stress ***-page electrophoresis results indicated that the change law of provenances of Xixia of Henan and Nanjing of Jiangsu with stronger cold resistance was similar,showing the change trend of "increase-decrease-increase".Protein was greatly expressed after stress for 1 d,the color of band became darker;the content gradually decreased in the following second and third day,and the color of bands was lighter;the content began to increase at the forth *** provenances induced the specific proteins with molecular weights of 27.6 and 22.5 kD,*** soluble protein content of provenance of Xiapu of Fujian with relatively weak cold resistance was gradually increased,but no new protein bands were *** changes of protein band color of various provenances in sds-page electrophoresis was basically consistent with the changes of protein content,the provenance with stronger cold resistance could induce the production of specific proteins.[Conclusion] The study provided theoretical basis for under the molecular mechanism of plant cold resistance,which had great significance in theory and practice.

关键词： Provenances of Toona sinensis Soluble proteins Low temperature stress sds-page electrophoresis Cold resistance

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