MadSci Network: Cell Biology |
Hi Marie, I will answer your question based on my knowledge of Food Science and information provided in the text "Foundations of Food Preparation" 1996. 6th edition, J. Freeland-Graves & G. Peckham, Prentice Hall, Englewood Cliffs, NJ. As the temperature increases during cooking, enzymes in the interior of the meat that degrade muscle proteins are activated. Between 104-122 F, protein chains begin to unfold and denature (proteins lose their quaternary and tertiary structure. These changes eventually cause the structure of the myofibrils to break and shorten. As the protein molecules aggregate, immobilized water is freed, decreasing the ability of the meat to hold water. You referred to this change in your question. Protien denaturation and water loss from the muscle contribute to increase in toughness of meat during cooking. High temperatures results in the fat melting, and this fat can be absorbed by the meat or lost as drippings. The fat that covers the surface of the meat reduces water loss, which can aid in maintaining juiciness. Heat can also tenderize meat by breaking down connective tissue (collagen). The heat can denature the collagen resulting in the hydrolysis of the protien chains. The end product of this process is the formation of gelatin. Cooking at low temperatures for long periods of time causes two changes (1) Hydrolysis of collagen and (2) Breakdown of muscle fibers by proteolytic enzymes. These two processes result in meat that is more tender. This is why it is recommended that one use slow cooking methods for tougher cuts of meat (i.e. pot roast). The color change that occurs to meat on cooking is a results of myoglobin breakdown (pigment that causes fresh hamburger to be red - oxymyoglobin). The surface of cooked meat browns as a result of the partial brekdown of its proteins, fat, pigments and other constituents. The browning that occurs on the surface of fried meat is the result of the Maillard reaction (reaction between the carbonyl group of a reducing sugar and and amino acid or amino group (i.e. that found on lysine)of a protein or peptide. I hope this answers you question. Sincerely, Al Bushway Professor of Food Science
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