Proteins are amazing chemical polymers. They serve a myriad of functions such as providing nutrition in the form of their constitutive amino acids as well as energy. They serve as reactants and enzymes in chemical reactions. Proteins contribute to the texture, viscosity and water holding capacity of foods that contain them. Proteins can be toxins or allergens or hormones, and they serve as transporters for vital molecules such as oxygen in the blood stream (Coultate 1984). These polymers have evolved to play a role in very specific physiological functions and this chemical reactivity can be used for very unique applications beyond a proteins evolutionary scope. A protein’s chemical and physical nature such as the isoelectric point, solubility and size, and its biological attraction to other molecules all can be exploited to separate a particular protein from the solution in which is resides. Typically several steps are used to purify a particular protein. These include heating, acidification, subjecting a solution to reducing conditions, and drying. More sophisticated techniques include chromatography, ultra filtration, reverse osmosis, and high-pressure liquid chromatography (Kinsella and Whitehead 2001). The isolation of proteins from their original matrices allows for their use in different food systems to improve such qualities as nutritional value, texture, and stability. In order for a protein to serve in the latter capacities it must have certain characteristics such as solubility, gelation, ligand-binding or film formation properties. Today there is extensive use of non-native proteins to improve food quality. Products include ice creams, beverages, cereals, baked goods, snack items and dairy items ... ... middle of paper ... ...1979. Functional properties of soy proteins. Journal America Oil Chemists’ Society 56:242-258. Kinsella JE and Whitehead. 1989. Proteins in whey: Chemical, physical and functional properties. Advances in food and nutrition research 33:343-439. McMahon DJ and Brown RJ. 1984. Composition, structure and integrity of casein micelles: A review. Journal of Dairy Science 67:499-512. Mendel F, and Brandon DL. 2001. Nutritional and health benefits of soy proteins. Journal of Agriculture and Food Chemistry 49(3):1069-1086. Southward CR. Casein Products. New Zealand Dairy Research Institute. Thompson LD., Dinh T. 2009. FDSC 4303/5305 food chemistry laboratory manual. Lubbock, TX: Texas Tech University, Department of Animal and Food Sciences. Walstra P. 1990. On the stability of casein micelles. Journal of Dairy Science 73:1965-1979.
While the tube for specimen Cb turned a tannish white in the lower half of the tube while the top stayed the lavender inoculated tube color. Do to this evidence I determined that both specimens Ca and Cb cannot use the process Casein hydrolysis or Casein coagulation due to lack of soft or firm curds in both tubes. Since there was no casein curds formed, I concluded that specimens Ca and Cb also cannot perform the process of proteolysis. My conclusion is supported by the fact that there was no clearing of the medium. I have also determine that neither of my organisms can make the enzymes rennin, proteolytic or even proteases. I know my specimens cannot produce proteases due to the fact that there was no blue coloring in the tubes which means that the byproduct Ammonia was not produced to increase the pH. Since neither of my specimens can make these enzymes, I concluded that my specimens cannot break down lactose or casein. Although I did learn that specimen Cb can reduce litmus due to the evidence that the lower part of the tube turned a tannish white color with a purple ring at the top. This color change from a purple to a white means that the litmus was reduced turning it clear and leaving the white of the milk to show. Finally I know that specimen Ca cannot reduce litmus due to the fact that the tube had no change in
The Effect of Temperature on an Enzyme's Ability to Break Down Fat Aim: To investigate the effect of temperature on an enzyme’s (lipase) ability to break down fat. Hypothesis: The graph below shows the rate increasing as the enzymes get closer to their optimum temperature (around 35 degrees Celsius) from room temperature. The enzyme particles are moving quicker because the temperature increases so more collisions and reactions occur between the enzymes and the substrate molecules. After this the graph shows the rate decreasing as the enzymes are past their optimum temperature (higher than). They are getting exposed to temperatures that are too hot and so the proteins are being destroyed.
Introduction: Within this experiment we wish to facilitate a greater understanding of the concepts of experimental design and quantifying techniques. Specifically, this lab will allow us to gain an enhanced understanding of the isolation of a protein using differential solubility, which allows us to separate and purify various proteins using high concentrations of a specific salt so that they may be studied in great detail. Last week we separated our desired protein using ammonium sulfate. Since we have already extracted the desired protein, we will begin quantifying the amount using the Bradford Protein Assay. Because it is a dye-binding assay, we will use the spectrophotometer to measure the absorbance of various dilutions of a protein: this will comprise our standard curve. We will then compare the absorbance of our extracted protein from l...
Bradford reagent is used to determine the concentration of protein in the experiment, it is a red brown acidic solution in the presence of protein. Bovine serum albumin (BSA) used for various biochemical applications include ELISA which is Enzyme-Linked Immunosorbent Assay, high content of screening assays, western blotting and immunohistochemistry. Furthermore, Bovine Serum Albumin can also be used to determine the quantity of other proteins which is by comparing an unknown quantity of protein to known amount of BSA. In this experiment, Bovine serum albumin (BSA) solution is used as protein concentration standard as the stability of bovine serum albumin will increase signal in the assays and lack of effect in biochemical reactions. Both of these solution are used in part 1 and part 2.
By Molecular Approaches." Journal Of Dairy Science 96.8 (2013): 4928-4937. Academic Search Complete. Web. 12 Nov. 2013.
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Milk Milk is an almost complete food. It consists of proteins (mainly casein), salts, fat and milk sugar, or lactose. It also contains vitamins A, C, D, certain B vitamins, and small amounts of others. Factors That May Affect The Reaction Ø The concentration of Rennin Ø
thousands of different ways to form thousands of different proteins. each with a unique function in the body. Both the amino acids manufactured in the liver and those derived from the breakdown of the The proteins we eat are absorbed into the blood stream and taken up by the cells and tissues to build new proteins as needed.... ... middle of paper ... ...denatured by boiling, their chains are shortened to form gelatine.
= Before conducting the experiment I would conduct a simple test for the protein by placing a sample of the albumen into a test tube and add biurett reagent. This contains copper (II) sulphate and sodium hydroxide.
1443 - 1460. Keener, K., Hoban, T. and Balasubramanian, R. 2014. Biotechnology and its applications. [online] Available at: http://www.ces.ncsu.edu/depts/foodsci/ext/pubs/bioapp.html [Accessed: 11 Apr 2014].
The production of cheese is an important contributor to economical sustainability of the dairy industry. Approximately one third of the milk produced globally is used for the manufacture of cheese, estimated at more than 20 million metric tonnes in 2011, with the revenue representing approximately 30% of the total dairy product sales revenue, according to the Food and Agriculture Organization of the United Nations (Farkye, 2004). Cheese consists primarily of fat and coagulated protein and is a highly nutritious food with diverse ranges of flavours and textures. The product finds wide applications within the food and culinary industries. In many instances cheese, as a concentrated dairy product, like milk powder and butter, is also used as a balance for milk preservation as milk is a highly perishable liquid.