Protein Thermal Stability Essay

Protein Thermal Stability Essay

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Proteins have an important role in the nutritional, structural, chemical and functional properties of food. The food proteins provide the essential amino acids, which are needed for growth and various metabolic pathways (Murad, 2007). Proteins are made up of carbon, hydrogen, nitrogen, oxygen and/ or sulfur (Barret, 1985).
Proteins present in dairy products have a significant impact on the flavor profile of the products. Milk proteins are used to improve the smoothness, whippability and texture of frozen dairy desserts (Damodaran, 1997). Milk contains six major gene products of the mammary gland, which are αs1-, αs2-, β-, and κ-caseins, β-lactoglobulin, and α-lactalbumin. Protease-peptones and γ-caseins are formed due to the presence of blood plasmin and plasminogen in milk ( Swaisgood, 1995). Rowland (1938) developed one of the first chemical methods to determine the distribution of nitrogen among five milk fractions. The method involved precipitation by saturation with magnesium sulfate and it was concluded that mature bovine milk had nitrogen distributed as follows: 78.3 % casein, 9.1 % albumin, 3.5 % globulin, 4.1 % protease peptone and 5 % non protein.
The αs1-, αs2-, β-, and κ-casein are the major casein proteins. Apart from dairy products like cheese and yogurt, isolated casein is used in a variety of non-dairy foods like beverages, dessert-types, bakery, pasta, confectionery and meat products, pharmaceutical and health care products (Mulvihill and Ennis, 2003). It was observed by Warner (1944), that casein could be precipitated from alkaline solution by acidification. Caseins exist in milk as polydisperse, almost spherical particles, called casein micelles. The caseins, as a whole, can be separated from the rest of the...


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...oteins. Pennylvania. Technomic Publishing Company.
Swaisgood HE. 1992. Chemistry of the caseins. Advanced Dairy Chemistry 1: Proteins, ed. P. F. Fox. London and New York. Elsevier Applied Science. pp 63-110.
Swaisgood HE. 1995. Protein and amino acid composition of bovine milk. Hand-book of milk composition, ed. Jensen RG. San Diego. Academic Press.
Thompson LD, Dinh T. 2009. FDSC 4303/5303 food chemistry laboratory manual. Lubbock, Tx.: Texas Tech University, Department of Animal and Food Sciences.
Warner RC. 1944. J. Am. Chem. Soc. 66: 1725.
Watanabe K and Klostermeyer H. 1976. Heat-induced changes in sulphydryl and disulfide levels of β-lactoglobulin A and formation of polymers. J. Dairy Res. 43: 411-418.
Wolf WJ, Babcock GE, Smith AK. 1962. Purification and stability studies of the 11S component of soybean proteins. Arch. Biochem. Biophys. 99:265-274.


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