Academic literature on the topic 'Physicochemical properties of food proteins'

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Journal articles on the topic "Physicochemical properties of food proteins"

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Zia, Muhammad Bin, Serap Namli, and Mecit Halil Oztop. "Physicochemical properties of wet-glycated soy proteins." LWT 142 (May 2021): 110981. http://dx.doi.org/10.1016/j.lwt.2021.110981.

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Soares, Luís Henrique de Barros, Patrícia Melchionna Albuquerque, Francine Assmann, and Marco Antônio Záchia Ayub. "Physicochemical properties of three food proteins treated with transglutaminase." Ciência Rural 34, no. 4 (August 2004): 1219–23. http://dx.doi.org/10.1590/s0103-84782004000400039.

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Three sources of food proteins were treated with microbial transglutaminase (EC 2.3.2.13) in order to assess changes in the physicochemical properties of reactivity, solubility, emulsification, and free amino groups of the formed polymers. Samples of lactic casein (LC), isolated soy protein (ISP), and hydrolysed animal protein (HAP), were incubated with the enzyme for one or two hours. LC and ISP showed a reduced solubility of 15% and 24% respectively, with HAP showing no alteration on solubility. Amino nitrogen content was 7%, 3% and 2% reduced for HAP, LC and ISP respectively. LC and ISP demonstrated lower emulsifying activity when they were enzymatically treated but the formed emulsions were stable, contrasting with HAP, which exhibited no changes in emulsifying properties.
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Tandang-Silvas, Mary Rose G., Evelyn Mae Tecson-Mendoza, Bunzo Mikami, Shigeru Utsumi, and Nobuyuki Maruyama. "Molecular Design of Seed Storage Proteins for Enhanced Food Physicochemical Properties." Annual Review of Food Science and Technology 2, no. 1 (April 10, 2011): 59–73. http://dx.doi.org/10.1146/annurev-food-022510-133718.

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Li, Yangyang, Hua Jin, Xiaotong Sun, Jingying Sun, Chang Liu, Chunhong Liu, and Jing Xu. "Physicochemical Properties and Storage Stability of Food Protein-Stabilized Nanoemulsions." Nanomaterials 9, no. 1 (December 25, 2018): 25. http://dx.doi.org/10.3390/nano9010025.

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This study investigated the preparation and properties of corn oil nanoemulsions stabilized by peanut protein isolate (PPI), rice bran protein isolate (RBPI), soybean protein isolate (SPI), and whey protein isolate (WPI). The mean droplet diameter of four protein-stabilized nanoemulsions prepared via ultrasound method was less than 245 nm. PPI-stabilized nanoemulsions showed better stability for 4 weeks, while the mean droplet diameter of RBPI-stabilized nanoemulsions had exceeded 1000 nm during the third week of storage. Fourier transform infrared and interfacial tension (IT) analysis showed that the higher level of disordered structure and lower IT of proteins made the stability of nanoemulsions better. Moreover, bivariate correlation analysis discovered that α-helix (p < 0.01) and β-turn (p < 0.05) of proteins were related to the mean droplet diameter of nanoemulsions, the random coil (p < 0.05) was related to the zeta potential of nanoemulsions. This study provided new idea for the relationship between the structure of protein and properties of protein-stabilized nanoemulsions.
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Zeng, Yan, Enhui Chen, Xuewen Zhang, Demao Li, Qinhong Wang, and Yuanxia Sun. "Nutritional Value and Physicochemical Characteristics of Alternative Protein for Meat and Dairy—A Review." Foods 11, no. 21 (October 23, 2022): 3326. http://dx.doi.org/10.3390/foods11213326.

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In order to alleviate the pressure on environmental resources faced by meat and dairy production and to satisfy the increasing demands of consumers for food safety and health, alternative proteins have drawn considerable attention in the food industry. However, despite the successive reports of alternative protein food, the processing and application foundation of alternative proteins for meat and dairy is still weak. This paper summarizes the nutritional composition and physicochemical characteristics of meat and dairy alternative proteins from four sources: plant proteins, fungal proteins, algal proteins and insect proteins. The difference between these alternative proteins to animal proteins, the effects of their structural features and environmental conditions on their properties, as well as the corresponding mechanism are compared and discussed. Though fungal proteins, algal proteins and insect proteins have shown some advantages over traditional plant proteins, such as the comparable protein content of insect proteins to meat, the better digestibility of fungal proteins and the better foaming properties of algal proteins, there is still a big gap between alternative proteins and meat and dairy proteins. In addition to needing to provide amino acid composition and digestibility similar to animal proteins, alternative proteins also face challenges such as maintaining good solubility and emulsion properties. Their nutritional and physicochemical properties still need thorough investigation, and for commercial application, it is important to develop and optimize industrial technology in alternative protein separation and modification.
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Tang, Xiao, Yanting Shen, Yiqin Zhang, M. Wes Schilling, and Yonghui Li. "Parallel comparison of functional and physicochemical properties of common pulse proteins." LWT 146 (July 2021): 111594. http://dx.doi.org/10.1016/j.lwt.2021.111594.

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Barroso da Silva, Fernando Luís, Paolo Carloni, David Cheung, Grazia Cottone, Serena Donnini, E. Allen Foegeding, Muhammad Gulzar, et al. "Understanding and Controlling Food Protein Structure and Function in Foods: Perspectives from Experiments and Computer Simulations." Annual Review of Food Science and Technology 11, no. 1 (March 25, 2020): 365–87. http://dx.doi.org/10.1146/annurev-food-032519-051640.

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The structure and interactions of proteins play a critical role in determining the quality attributes of many foods, beverages, and pharmaceutical products. Incorporating a multiscale understanding of the structure–function relationships of proteins can provide greater insight into, and control of, the relevant processes at play. Combining data from experimental measurements, human sensory panels, and computer simulations through machine learning allows the construction of statistical models relating nanoscale properties of proteins to the physicochemical properties, physiological outcomes, and tastes of foods. This review highlights several examples of advanced computer simulations at molecular, mesoscale, and multiscale levels that shed light on the mechanisms at play in foods, thereby facilitating their control. It includes a practical simulation toolbox for those new to in silico modeling.
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Rahma, E. H., T. A. El-Adawy, R. Lásztity, M. A. Gomaa, A. A. El-Badawey, and J. Gaugecz. "Biochemical studies of some non-conventional sources of proteins Part 6. Physicochemical properties of apricot kernel proteins and their changes during detoxification." Food / Nahrung 38, no. 1 (1994): 3–11. http://dx.doi.org/10.1002/food.19940380103.

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Wang, Ronghan, Jing Jing Wang, Xiaobing Guo, Yufeng Li, Yi Wu, Haiquan Liu, and Yong Zhao. "Physicochemical and functional properties of the Antarctic krill proteins modified by succinylation." LWT 154 (January 2022): 112832. http://dx.doi.org/10.1016/j.lwt.2021.112832.

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XIONG, Y. L., and C. J. BREKKE. "Physicochemical and Gelation Properties of Pre- and Postrigor Chicken Salt-soluble Proteins." Journal of Food Science 55, no. 6 (November 1990): 1544–48. http://dx.doi.org/10.1111/j.1365-2621.1990.tb03564.x.

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Dissertations / Theses on the topic "Physicochemical properties of food proteins"

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Adavalli, Sharat Chandra. "Extrusion and physicochemical properties of soy-whey protein meat analog." Diss., Columbia, Mo. : University of Missouri-Columbia, 2007. http://hdl.handle.net/10355/6272.

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Thesis (M.S.)--University of Missouri-Columbia, 2007.
The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. Title from title screen of research.pdf file (viewed on January 16, 2008) Includes bibliographical references.
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Crockett, Rachel Lynn. "The Physicochemical Properties of Gluten-Free Dough with the Addition of Hydrocolloids and Proteins." The Ohio State University, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=osu1251825675.

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McCarthy, James Thomas. "Physicochemical Properties, Microstructure and Probiotic Survivability of Non-Fat Goat's Milk Yogurt Using Heat Treated Whey Protein Concentrate as a Fat Replacer." ScholarWorks @ UVM, 2015. http://scholarworks.uvm.edu/graddis/442.

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Probiotic dairy foods, especially non- and low-fat dairy products, are becoming popular in the US. A non-fat goat's milk yogurt containing probiotics (Lactobacillus acidophilus and Bifidobacterium spp.) was developed using heat-treated whey protein concentrate (HWPC) as a fat replacer and pectin as a thickening agent. Yogurts containing non-heat treated whey protein concentrate (WPC) and pectin as well as one with only pectin were also produced. A fat-free cow's milk yogurt with pectin was also used as a control yogurt. The yogurts were analyzed for chemical composition, water holding capacity (syneresis), microstructure, changes in pH and viscosity, mold, yeast and coliform counts, and probiotic survivability during storage at 4°C for 10 weeks. The results showed that the non-fat goat's milk yogurt made with 12% HWPC (12.5% WPC solution heated at 85°C for 30 min at pH 8.5) and 0.35% pectin, had a significantly higher viscosity (P<0.01) than any of the other yogurts and low syneresis than the goat’s yogurt with only pectin added (P<0.01). After 10 weeks in storage, viscosity and pH remained constant throughout all of the yogurts. Mold, yeast, and coliform counts were negative throughout the 10 week study. Bifidobacterium spp. remained stable and counts remained above 10⁶CFU g⁻ ¹ during the 10 week storage. However, the population of Lactobacillus acidophilus dropped below 10⁶CFU g⁻ ¹ after 2 weeks of storage. Microstructure analysis of the non - fat goat’s milk yogurt determined by scanning electron microscopy revealed that HWPC interacted with casein micelles to form a more comprehensive network in the yogurt gel. The results indicate that HWPC could be used as a fat replacer to improve the consistency of non - fat goat’s milk yogurt and other products alike.
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Puli, Goutham. "Effects of Xanthan/Locust Bean Gum Mixtures on the Physicochemical Properties and Oxidative Stability of Whey Protein Stabilized Oil-In-Water Emulsions." TopSCHOLAR®, 2013. http://digitalcommons.wku.edu/theses/1288.

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Scientific evidence shows that dietary intake of the omega-3 polyunsaturated fatty acids is beneficial to human health. Fish oil is a rich source of omega-3 fatty acids. However, fish oil with high levels of omega-3 PUFA is very susceptible to oxidative deterioration during storage. The objective of this study was to investigate the effect of xanthan gum (XG)-locust bean gum (LBG) mixtures on the physicochemical properties of whey protein isolate (WPI) stabilized oil-in-water (O/W) emulsions containing 20% v/v menhaden oil. The O/W emulsions containing XG/LBG mixtures were compared to emulsions with either XG or LBG alone. The emulsions were prepared using a sonicator by first mixing menhaden oil into the WPI solution and then either XG, LBG or XG/LBG mixtures were added. WPI solution (2 wt%) and gum solutions (0.0,0.05, 0.1, 0.15, 0.2 and 0.5 wt%) were prepared separately by dissolving measured quantities of WPI in distilled water. XG and LBG gums were blended in a synergistic ratios of 50:50 for the mixture. The emulsions were evaluated for apparent viscosity, microstructure, creaming stability and oxidative stability. Addition of 0.15, 0.2 and 0.5 wt% XG/LBG mixtures greatly decreased the creaming of the emulsion. The emulsion with 0.15, 0.2 and 0.5 wt% XG/LBG mixtures showed no visible serum separation during 15 d of storage. The apparent viscosity of the emulsions containing XG/LBG mixtures was significantly higher (p < 0.05) than the emulsions containing either XG or LBG alone. The viscosity was sharply enhanced at higher concentrations of XG/LBG mixtures. Microstructure images showed depletion flocculation for LBG (0.05-0.5 wt%), XG (0.05- 0.2 wt%) and XG/LBG mixtures (0.05 and 0.1 wt%) emulsions. Flocculation was decreased with the increased biopolymer concentration in the emulsion. The decrease in flocculation was much pronounced for the emulsion containing XG/LBG mixtures. The rate of lipid oxidation for 8 week storage was significantly (p < 0.05) lower in emulsions containing XG/LBG mixtures than in emulsions containing either of the biopolymer alone. The results suggested that the addition of XG/LBG mixtures greatly enhanced the creaming and oxidative stability of the WPI-stabilized menhaden O/W emulsion as compared to either XG or LBG alone.
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Wangsa-Wirawan, Norbertus Djajasantosa. "Physicochemical properties of protein inclusion bodies." Title page, contents and introduction only, 1999. http://web4.library.adelaide.edu.au/theses/09PH/09phw2465.pdf.

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Bibliography: leaves 182-198. Improvements in the current production system of inclusion bodies and the downstream processing sequence are essential to maintain a competitive advantage in the market place. Optimisation of fermentation is considered to improve production yield; then flotation as a possible inclusion body recovery method.
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Mhd, Sarbon Norizah. "Nutritional and physicochemical properties of chicken proteins and peptides." Thesis, University of Surrey, 2011. http://epubs.surrey.ac.uk/804305/.

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Kim, Young Duk. "Encapsulation properties of several food proteins /." The Ohio State University, 1995. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487868114110127.

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Tian, Susan Jane. "Varietal and environmental effects on the physicochemical properties of sweet potato starch." Thesis, University of Nottingham, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.339597.

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Pirogova, Elena 1968. "Examination of physicochemical properties of amino acids within the resonant recognition model." Monash University, Dept. of Electrical and Computer Systems Engineering, 2001. http://arrow.monash.edu.au/hdl/1959.1/8424.

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Kimura, Aiko. "Analysis of Structural Factors Contributing to Physicochemical Properties of Seed Storage Proteins." Kyoto University, 2010. http://hdl.handle.net/2433/120460.

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Kyoto University (京都大学)
0048
新制・課程博士
博士(農学)
甲第15416号
農博第1801号
新制||農||978(附属図書館)
学位論文||H22||N4515(農学部図書室)
27894
京都大学大学院農学研究科農学専攻
(主査)准教授 丸山 伸之, 教授 松村 康生, 教授 谷坂 隆俊
学位規則第4条第1項該当
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Books on the topic "Physicochemical properties of food proteins"

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Shuryo, Nakai, and Modler H. W, eds. Food proteins: Properties and characterization. New York, N.Y: VCH, 1996.

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M, Whitehead Dana, and Kinsella John E. 1938-, eds. Structure-function properties of food proteins. San Diego: Academic Press, 1994.

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E, Sikorski Zdzisław, ed. Chemical & functional properties of food proteins. Lancaster, Pa: Technomic Pub. Co., 2001.

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Mitchell, J. R., Ph. D. and Ledward D. A, eds. Functional properties of food macromolecules. London: Elsevier Applied Science Publishers, 1986.

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Suslyanok, Georgiy, Tat'yana Auerman, and Tat'yana Generalova. Fundamentals of biochemistry. ru: INFRA-M Academic Publishing LLC., 2021. http://dx.doi.org/10.12737/1003787.

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The textbook contains basic information about the structure, properties and biological functions of proteins, nucleic acids, carbohydrates, lipids, vitamins. The most important ways of transformation of substances and energy in a living organism are considered. The information about the use of biochemical processes in the food industry is given. Meets the requirements of the federal state educational standards of higher education of the latest generation. For university students studying in the areas of training 19.03.01 "Biotechnology", 19.03.02 "Food products from plant raw materials", 19.03.04 "Product technology and catering organization", as well as for students studying in other areas of training, and graduate students.
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Food Legumes: Physicochemical and Nutritional Properties. MDPI, 2021. http://dx.doi.org/10.3390/books978-3-0365-1149-8.

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Xiong, Youling. Physicochemical and gelation properties of chicken myofibrillar proteins. 1989.

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Nakai, Shuryo, and H. Wayne Modler. Food Proteins: Properties and Characterization. Wiley & Sons, Incorporated, John, 1996.

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(Editor), Shuryo Nakai, H. W. Modler (Editor), and S. Nakai (Editor), eds. Food Proteins: Properties and Characterization (Food Science and Technology). VCH Publishers, 1996.

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Phillips, Lance G., and Steve L. Taylor. Structure-Function Properties of Food Proteins. Elsevier Science & Technology Books, 2013.

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Book chapters on the topic "Physicochemical properties of food proteins"

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Kinsella, J. E., D. J. Rector, and L. G. Phillips. "Physicochemical properties of proteins: Texturization via gelation, glass and film formation." In Protein Structure-Function Relationships in Foods, 1–21. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2670-4_1.

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Friis, Dennis Steven, and Hans Ramløv. "Physicochemical Properties of Antifreeze Proteins." In Antifreeze Proteins Volume 2, 43–67. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-41948-6_3.

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Zayas, Joseph F. "Emulsifying Properties of Proteins." In Functionality of Proteins in Food, 134–227. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-59116-7_4.

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Zayas, Joseph F. "Foaming Properties of Proteins." In Functionality of Proteins in Food, 260–309. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-59116-7_6.

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Zayas, Joseph F. "Gelling Properties of Proteins." In Functionality of Proteins in Food, 310–66. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-59116-7_7.

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Ravula, Sudharshan R., Arepally, A. K. Datta, and T. K. Goswami. "Physicochemical and Thermal Properties of Bakery Products." In Food Processing and Preservation Technology, 245–63. Boca Raton: Apple Academic Press, 2022. http://dx.doi.org/10.1201/9781003153184-12.

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Kristo, Eleana, and Milena Corredig. "Functional Properties of Food Proteins." In Applied Food Protein Chemistry, 47–73. Chichester, UK: John Wiley & Sons, Ltd, 2015. http://dx.doi.org/10.1002/9781118860588.ch5.

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Niki, Ryoya, and Yoh Sano. "The Effects of Cooling on the Physicochemical Properties of Casein Micelle." In Food Hydrocolloids, 341–46. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2486-1_52.

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Martini, S. "Effect of Ultrasound on the Physicochemical Properties of Lipids." In Ultrasound in Food Processing, 464–84. Chichester, UK: John Wiley & Sons, Ltd, 2017. http://dx.doi.org/10.1002/9781118964156.ch18.

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Sousa, I. M. N., M. L. Beirão da Costa, S. E. Hill, J. R. Mitchell, and S. E. Harding. "Functional Properties of Lupinus luteus Proteins." In Developments in Food Engineering, 206–8. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2674-2_61.

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Conference papers on the topic "Physicochemical properties of food proteins"

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Alabi, Opeyemi, Eric AMONSOU, and George Annor. "Impact of plasma-activated water treatment on physicochemical and functional properties of Bambara globulin." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/mecr6198.

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The functional application of plant proteins as food ingredients can be improved by altering their composition and structure. In this study, the impact of plasma-activated water (PAW) on the structure composition and functionality of Bambara groundnut globulin was investigated. Bambara globulin was treated with PAW (pH 3.4 and conductivity of 200 mV) at 4 degrees C overnight. This was then analyzed by SDS-PAGE, amino acid profiling, hydrophobicity, zeta potential, FTIR, and intrinsic fluorescence emission in comparison with the untreated globulin. Functional properties analyses included solubility, emulsifying, and foaming to define its potential application in the food system. Plasma treatment resulted in the loss of helical structure and an over 3-folds increase in beta-turns. Amino acid data showed a 20% reduction in glutamic acid after treatment. PAW treated Bambara globulin showed a slight redshift in fluorescence intensity suggesting an unfolding of the protein structure, which also correlated with the observed increased hydrophobicity. Crosslinking was not evident in the gel electrophoresis and no major change in protein surface charge and solubility profiles. Average oil droplet sizes were increased with increasing protein concentrations from 10-20 mg/ml, suggesting that Bambara globulin had reduced emulsifying capacity after treatment with PAW. However, foaming capacities were significantly better and stable at up to 15 mg protein/mL. PAW modification could be a promising strategy for the enhancement of the foaming properties of plant proteins.
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Leite Nobrega De Moura Bell, Juliana. "Understanding the impact of proteolysis on extractability, physicochemical, and functional properties of proteins and lipids from almond flour." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/pyui3979.

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The extraction of lipids and proteins from food matrices has been challenged by the use of several sequential unit operations and the frequent use of hazardous and flammable solvents to produce defatted flours for subsequent protein extraction. The effects of aqueous (AEP) and enzymatic extraction (EAEP) on the simultaneous extraction of lipids and proteins from full-fat almond flour, insoluble microstructure, oil recovery from the oil-rich emulsion, and physicochemical and functional properties of the extracted protein were evaluated. Except for the use of 0.5% of protease in the EAEP, extraction parameters were similar for both processes (pH 9.0, 50 ºC, 1:10 solids-to-liquid ratio, and 60 min). Enzymatic extraction significantly improved the oil (from 62 to 67%) and protein (from 67 to 77%) extractability while generating smaller protein fragments and creating a more porous insoluble structure. EAEP followed by enzymatic destabilization of the oil-rich emulsion increased the degree of hydrolysis of the emulsion proteins from 8 to 22% while reducing its hydrophobicity from 1205 to 688, resulting in 93% oil recovery. EAEP also resulted in the production of protein extracts with higher protein content, a more unordered protein secondary structure with reduced surface hydrophobicity, and reduced thermostability. Importantly, proteolysis significantly enhanced the functionality of the hydrolysates at pH values close to the almond protein isoelectric point. At pH 5.0, the hydrolysates had higher solubility (47 vs 23%), emulsification capacity (492 vs 402 g oil/ g protein), emulsification activity index (35 vs 17 m2 40 /g), and foaming capacity (23 vs 41 11%) compared with unhydrolyzed proteins. These results highlight the effectiveness of this flammable solvent-free extraction approach to maximize lipid and protein extractability from almond flour with concurrent improvement in oil recovery and protein functionality, creating new opportunities for their application as food ingredients.
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Li, Yonghui, Shan Hong, and Yanting Shen. "Enhancing pea protein functionalities through "green" modifications for food applications." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/dpor5716.

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Pea protein is receiving significant interest. Modified pea proteins may be used as healthy and more functional ingredients in food products. This study aimed to enhance pea protein functional properties through neoglycosylation with guar gum or gum arabic and/or enzymatic modification with transglutaminase or protein glutaminase, understand the physicochemical properties of the modified proteins, and evaluate their applications in mayonnaise-like dressings as egg replacers and in beef patties as functional extenders. The proteins crosslinked with transglutaminase showed significantly improved water holding capacity (5.2 - 5.6 g/g protein) compared with the control pea protein isolate (2.8 g/g). The pea proteins conjugated with guar gum showed exceptional emulsifying capacity (EC) and stability (ES) of up to 100% compared with the control protein (EC of 58% and ES of 48%). Some sequentially modified pea proteins, such as transglutaminase crosslinking followed by guar gum conjugation had multiple functional enhancements (water holding, oil holding, emulsifying, and gelation). The functionally enhanced pea proteins had comparable descriptive sensory scores as the control protein. Beef patties containing 2.5-5% of the modified pea protein from sequential deamidation and conjugation demonstrated some advantageous features in terms of higher fat/water retention, cooking yield, and tender texture, which may be preferred by the elderly or some other consumers. The emulsions with the guar gum conjugated protein had significantly increased stability, apparent viscosity, and decreased droplet size, and mayonnaise-like dressing prepared with this protein at higher concentrations (6 and 8%) exhibited significantly better emulsification properties and viscoelasticity, compared with those containing the unmodified protein.
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Zubair, Muhammad, Aman Ullah, and Jianping Wu. "Spent hen proteins: An untapped bioresource for food packaging applications." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/wasw9203.

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Spent hens, a poultry by-product, have little economic value for processing due to poor meat quality and low yield. In North America alone, 150 million spent hens are produced every year which are either end up in landfill or burnt. However, there are concerns over disposal of spent hens; therefore, it is pertinent to find out alternative uses that are environmentally friendly. On the other hand, single-use plastic packaging is leading to a global environmental crisis. The development of hybrid bionanocomposite films from spent hen proteins using cellulose nanocrystals (CNCs) is a viable option for food packaging applications. In this study, proteins were harvested from spent hen using alkali aided extraction method. To develop protein derived bionanocomposite films, glycerol was used as a plasticizer and chitosan as a cross-linker agent. Furthermore, cellulose nanocrystals (1,3,5%) were incorporated into the proteins/glycerol/chitosan mixture and sonicated it for an hour. Finally, mixture was transformed into food packaging films using compression molding and characterized using FTIR, XRD, TEM, DMA, DSC and TGA.The results indicated that alkali aided method provided excellent proteins recovery yield (74%) and percentage purity (96%) from spent hen. The physicochemical analysis showed an improvement in the thermal, mechanical, and barrier properties of the prepared bionanocomposite films. A greater enhancement in mechanical strength (2.65± 0.50 to 8.48±0.98 MPa) of CNCs derived films was observed as compared to films without nanoparticles. Transmission electron microscopy images confirmed the dispersion of CNCs into the protein polymeric chains which resulted in good exfoliation/intercalation of CNCs and improved the overall properties of the films.The above results suggested that spent hen proteins have great future potential to develop protein/CNCs hybrid bionanocomposite films with improved functional properties for food packaging applications. The petro-based plastic environmental impacts can be reduced with the development of these environmentally benign bionanocomposite films.
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Munch, Katharina, Claire Berton-Carabin, Karin Schroen, and Simeon Stoyanov. "Plant protein-stabilized emulsions: Implications of protein and non-protein components for lipid oxidation." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/zznf4565.

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The use of plant proteins to stabilize oil-in-water (O/W) emulsions has been an increasing trend lately. The complexity of the available plant protein ingredients, along with the proteins’ physicochemical properties, require advanced processing that typically leads to substantial concentrations of non-protein components in the final isolates or concentrates. It is known that those components, such as polyphenols, phytic acid or phospholipids, can have a strong influence on the oxidative stability of emulsions. Thus, to understand the oxidative stability of plant protein-stabilized emulsions, the influence of the non-protein components also needs to be considered. Many food emulsions, such as mayonnaise or infant formula, are stabilized by not only proteins, but also phospholipids. Such an interfacial protein-phospholipid combination can also be found in oleosomes, natural lipid droplets which show a high oxidative stability. This stability has been attributed to their interfacial architecture in which oleosins and phospholipids form a tight physical barrier against pro-oxidant species. However, while the antioxidant properties of proteins are widely reported, the contribution of phospholipids to lipid oxidation in plant protein-based emulsions remains underexplored. In this work, we investigated how mixed interfacial plant proteins and phospholipids may be rationally used to control the oxidative stability of O/W emulsions. The interfacial composition was modulated by varying the ratio between pea proteins and sunflower phosphatidylcholine (PC) while keeping the total concentration of pea proteins constant. Increasing the phospholipid-to-protein ratio led to a monotonic decrease in the concentration of proteins and an increase of phospholipids at the interface, while the oxidative stability of those O/W emulsions changed in a non-monotonic pattern. The results were put in perspective by embedding them in a context of reviewing the potential implications of typical components in plant protein ingredients on lipid oxidation.
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Barouh, Nathalie, Claire Berton-Carabin, Thierry Chardot, Jean-Francois Fabre, Sabine D'andrea, Yann Gohon, Eric Lacroux, et al. "Exploring Plant Biodiversity to Extract Oil Bodies for Sustainable Food Applications." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/wmkj8057.

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Oleoproteaginous and cereal seeds enclose a wide range of nutriments such as lipids, proteins, polysaccharides and various mineral and organic micronutrients. These nutrients are found under the form of natural assemblies such as oil or protein bodies or starch granules, that have interesting functionalities (micronic sizes, surface activity, high physicochemical stability, etc.). These assemblies are extracted by various processes using energy, organic solvents, steam, alone or in combination. Thus, their natural structures are often strongly damaged, and some of their functionalities disappear. Storming through natural assemblies’ biodiversity to address the societal demand for more natural and minimally-processed food, seems promising. Indeed, the soft extraction of such assemblies could be an alternative to traditional intensive fractionation methods of plant raw materials to isolate target ingredients (sucrose, starch, refined oils, etc.). This would allow energy savings and avoid solvent use, but must be balanced with potential challenges of this new green refinery scheme. The purpose of the present work is to highlight the physicochemical properties of various oil bodies from diverse plant origins. A green refinery protocol is proposed for their extraction from various matrices. Then their size distribution, surface activity, resistance to oxidation and fatty acids and liposoluble vitamins bioaccessibility is also presented. Omega-3 rich sources (linseed, chia, hemp…) are of special interest to correct the low dietary intake of US and European population as well as the ω6/ω3 balance. Oil bodies from these plant species can thus constitute new dietary carriers of ω3 and other bioactive molecules. Moreover, the combination of oil bodies with specific features (fatty acid profiles, stabilities, vitamin contents) can help meeting the requirements of specific nutritional targets (infants, children, elderly, athletes, etc.). Altogether, we are convinced that the valorization of these diverse oil bodies can be a strategic route in the development of sustainable food systems.
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Gaivoronskaya, Irina, and Valenitna Kolpakova. "MATHEMATICAL MODELS FOR THE SYNTHESIS OF PLANT-BASED COMPOSITIONS WITH IMPROVED AMINO ACID COMPOSITION." In GEOLINKS Conference Proceedings. Saima Consult Ltd, 2021. http://dx.doi.org/10.32008/geolinks2021/b1/v3/12.

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The aim of the work was to optimize the process of obtaining multicomponent protein compositions with high biological value and higher functional properties than the original vegetable protein products. Was realized studies to obtain biocomposites on the base of pea protein-oat protein and pea protein-rice protein. Developed composites were enriched with all limited amino acids. For each of the essential amino acids, the amino acid score was 100% and higher. Protein products used in these compositions are not in major allergen list, which allows to use these compositions in allergen-free products and specialized nutrition. To determine biosynthesis parameters for compositions from pea protein and various protein concentrates with the use of transglutaminase enzyme, was studied effect of concentration and exposition time on the amount of amino nitrogen released during the reaction. Decreasing of amino nitrogen in the medium indicated the occurrence of a protein synthesis reaction with the formation of new covalent bonds. Were determined optimal parameters of reaction: the hydromodule, the exposure time, the concentration of EP of the preparation, were obtained mathematical models. Studies on the functional properties of composites, the physicochemical properties of the proteins that make up their composition, and structural features will make it possible to determine the uses in the manufacture of food products based on their ability to bind fat, water, form foam, gels, and etc.
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Hoke, John L., John G. Georgiadis, and Rafael Jimenez-Flores. "Freezing of Aqueous Solutions of Glycosylated Bovine Beta-Casein." In ASME 1998 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 1998. http://dx.doi.org/10.1115/imece1998-0813.

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Abstract Genetic engineering of milk proteins allows control of their physicochemical properties in foods and dairy products during processing, storage, and consumption. Robust methods for the estimation of the quality and function of the proteins during downstream processing are sought. The focus of this study is a systematic microscopic investigation of the freezing of sub-microliter pendent droplets of buffer solution of glycosylated bovine beta-casein. The freezing and crystallization is observed with a scanning confocal microscope fitted with a stage cooled with vapor boiled off a liquid nitrogen dewar. Four liquid samples (with glycosylated bovine beta-casein concentrations of 35, 125, 500, and 1000 μg/ml) are compared against the control (10 mg/ml of wild type non-glycosylated bovine beta-casein). The freezing of similar size samples consisting of de-ionized water, ice-nucleating mixture (Pseudomonas syringae), and pure buffer solution is also examined for comparison. Higher concentrations of the engineered-beta casein result in increasing antifreeze action, corresponding to depression of the freezing point, and thermal stabilization of the supercooled liquid. This conclusion is supported by a non-parametric statistical analysis based on the Jonckheere test. A freezing point assay can thus be made to assess the quality of glyco-bovine beta-casein.
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Hilal, Adonis, Anna Florowska, and Małgorzata Wroniak. "Evaluation of the Physicochemical and Textural Properties of Binary Protein-Polysaccharide Hydrogels." In Foods 2022. Basel Switzerland: MDPI, 2022. http://dx.doi.org/10.3390/foods2022-12969.

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Kontogianni, Vasiliki G., Alexandra V. Chatzikonstantinou, Marios Mataragas, Efthymia Kondyli, Haralambos Stamatis, and Loulouda Bosnea. "Evaluation of the Antioxidant and Physicochemical Properties of Microalgae/Whey Protein-Based Edible Films." In Foods 2021. Basel Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/foods2021-10926.

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Reports on the topic "Physicochemical properties of food proteins"

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Tuller, Markus, Asher Bar-Tal, Hadar Heller, and Michal Amichai. Optimization of advanced greenhouse substrates based on physicochemical characterization, numerical simulations, and tomato growth experiments. United States Department of Agriculture, January 2014. http://dx.doi.org/10.32747/2014.7600009.bard.

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Over the last decade there has been a dramatic shift in global agricultural practice. The increase in human population, especially in underdeveloped arid and semiarid regions of the world, poses unprecedented challenges to production of an adequate and economically feasible food supply to undernourished populations. Furthermore, the increased living standard in many industrial countries has created a strong demand for high-quality, out-of-season vegetables and fruits as well as for ornamentals such as cut and potted flowers and bedding plants. As a response to these imminent challenges and demands and because of a ban on methyl bromide fumigation of horticultural field soils, soilless greenhouse production systems are regaining increased worldwide attention. Though there is considerable recent empirical and theoretical research devoted to specific issues related to control and management of soilless culture production systems, a comprehensive approach that quantitatively considers all relevant physicochemical processes within the growth substrates is lacking. Moreover, it is common practice to treat soilless growth systems as static, ignoring dynamic changes of important physicochemical and hydraulic properties due to root and microbial growth that require adaptation of management practices throughout the growth period. To overcome these shortcomings, the objectives of this project were to apply thorough physicochemical characterization of commonly used greenhouse substrates in conjunction with state-of-the-art numerical modeling (HYDRUS-3D, PARSWMS) to not only optimize management practices (i.e., irrigation frequency and rates, fertigation, container size and geometry, etc.), but to also “engineer” optimal substrates by mixing organic (e.g., coconut coir) and inorganic (e.g., perlite, pumice, etc.) base substrates and modifying relevant parameters such as the particle (aggregate) size distribution. To evaluate the proposed approach under commercial production conditions, characterization and modeling efforts were accompanied by greenhouse experiments with tomatoes. The project not only yielded novel insights regarding favorable physicochemical properties of advanced greenhouse substrates, but also provided critically needed tools for control and management of containerized soilless production systems to provide a stress-free rhizosphere environment for optimal yields, while conserving valuable production resources. Numerical modeling results provided a more scientifically sound basis for the design of commercial greenhouse production trials and selection of adequate plant-specific substrates, thereby alleviating the risk of costly mistrials.
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Naim, Michael, Andrew Spielman, Shlomo Nir, and Ann Noble. Bitter Taste Transduction: Cellular Pathways, Inhibition and Implications for Human Acceptance of Agricultural Food Products. United States Department of Agriculture, February 2000. http://dx.doi.org/10.32747/2000.7695839.bard.

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Historically, the aversive response of humans and other mammals to bitter-taste substances has been useful for survival, since many toxic constituents taste bitter. Today, the range of foods available is more diverse. Many bitter foods are not only safe for consumption but contain bitter constituents that provide nutritional benefits. Despite this, these foods are often eliminated from our current diets because of their unacceptable bitterness. Extensive technology has been developed to remove or mask bitterness in foods, but a lack of understanding of the mechanisms of bitterness perception at the taste receptor level has prevented the development of inhibitors or efficient methods for reducing bitterness. In our original application we proposed to: (a) investigate the time course and effect of selected bitter tastants relevant to agricultural products on the formation of intracellular signal molecules (cAMP, IP3, Ca2+) in intact taste cells, in model cells and in membranes derived therefrom; (b) study the effect of specific bitter taste inhibitors on messenger formation and identify G-proteins that may be involved in tastant-induced bitter sensation; (c) investigate interactions and self-aggregation of bitter tastants within membranes; (d) study human sensory responses over time to these bitter-taste stimuli and inhibitors in order to validate the biochemical data. Quench-flow module (QFM) and fast pipetting system (FPS) allowed us to monitor fast release of the aforementioned signal molecules (cGMP, as a putative initial signal was substituted for Ca2+ ions) - using taste membranes and intact taste cells in a time range below 500 ms (real time of taste sensation) - in response to bitter-taste stimulation. Limonin (citrus) and catechin (wine) were found to reduce cellular cAMP and increase IP3 contents. Naringin (citrus) stimulated an IP3 increase whereas the cheese-derived bitter peptide cyclo(leu-Trp) reduced IP3 but significantly increased cAMP levels. Thus, specific transduction pathways were identified, the results support the notion of multiple transduction pathways for bitter taste and cross-talk between a few of those transduction pathways. Furthermore, amphipathic tastants permeate rapidly (within seconds) into liposomes and taste cells suggesting their availability for direct activation of signal transduction components by means of receptor-independent mechanisms within the time course of taste sensation. The activation of pigment movement and transduction pathways in frog melanophores by these tastants supports such mechanisms. Some bitter tastants, due to their amphipathic properties, permeated (or interacted with) into a bitter tastant inhibitor (specific phospholipid mixture) which apparently forms micelles. Thus, a mechanism via which this bitter taste inhibitor acts is proposed. Human sensory evaluation experiments humans performed according to their 6-n-propyl thiouracil (PROP) status (non-tasters, tasters, super-tasters), indicated differential perception of bitterness threshold and intensity of these bitter compounds by different individuals independent of PROP status. This suggests that natural products containing bitter compounds (e.g., naringin and limonin in citrus), are perceived very differently, and are in line with multiple transduction pathways suggested in the biochemical experiments. This project provides the first comprehensive effort to explore the molecular basis of bitter taste at the taste-cell level induced by economically important and agriculturally relevant food products. The findings, proposing a mechanism for bitter-taste inhibition by a bitter taste inhibitor (made up of food components) pave the way for the development of new, and perhaps more potent bitter-taste inhibitors which may eventually become economically relevant.
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