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Protein cooking

Oats lack protein quantity and quality. While dry oatmeal is about 14% protein, cooked oatmeal is only about 2% protein. Moreover, it is deficient in the essential amino acid lysine. [Pg.787]

Protein-Based Substitutes. Several plant and animal-based proteins have been used in processed meat products to increase yields, reduce reformulation costs, enhance specific functional properties, and decrease fat content. Examples of these protein additives are wheat flour, wheat gluten, soy flour, soy protein concentrate, soy protein isolate, textured soy protein, cottonseed flour, oat flour, com germ meal, nonfat dry milk, caseinates, whey proteins, surimi, blood plasma, and egg proteins. Most of these protein ingredients can be included in cooked sausages with a maximum level allowed up to 3.5% of the formulation, except soy protein isolate and caseinates are restricted to 2% (44). [Pg.34]

In traditional cooking of proteinaceous foods, the fundamental difference between Western and Oriental cultures is that the former cooks proteins with unseasoned fats and the latter cooks with many kinds of traditional seasonings that have tastes of amino acids. Western cultures have some traditional foods with amino acid taste such as cheese. Protein hydrolysates are popular as seasonings (225). [Pg.296]

Denaturation is accompanied by changes in both physical and biological properties. Solubility is drastically decreased, as occurs when egg white is cooked and the albumins unfold and coagulate. Most enzymes also lose all catalytic activity when denatured, since a precisely defined tertiary structure is required for their action. Although most denaturation is irreversible, some cases are known where spontaneous renaturation of an unfolded protein to its stable tertiary structure occurs. Renaturation is accompanied by a full recovery of biological activity. [Pg.1040]

Minke B, Cook B (2002) TRP channel proteins and signal transduction. Physiol Rev 82 429-472... [Pg.1245]

Sodium nitrite can react with proteins in the stomach or during cooking, especially in high heat (such as frying bacon), to form carcinogenic N-nitrosamines. To prevent this, ascorbic acid or erythor-bic acid is commonly added to cured meats. [Pg.40]

Free glutamates exist in certain cheeses (such as parmesan), in tomato products, and in soy sauce. These products are often used to enhance the flavor of meat dishes. Proteins can be hydrolyzed by heat, releasing free glutamates. Cooked meats, especially grilled meats, get some of their taste from free glutamates. [Pg.72]

A rate law summarizes the dependence of the rate on concentrations. However, rates also depend on temperature. The qualitative observation is that most reactions go faster as the temperature is raised (Fig. 13.22). An increase of 10°C from room temperature typically doubles the rate of reaction of organic species in solution. That is one reason why we cook foods heating accelerates reactions that lead to the breakdown of cell walls and the decomposition of proteins. We refrigerate foods to slow down the natural chemical reactions that lead to their decomposition. [Pg.676]

The loss of structure by a protein is called denaturation. This structural change may be a loss of quaternary, tertiary, or secondary structure it may also be degradation of the primary structure by cleavage of the peptide bonds. Even mild heating can cause irreversible denaturation. When we cook an egg, the protein called albumen denatures into a white mass. The permanent waving of hair, which consists primarily of long a helices of the protein keratin, is a result of partial denaturation. [Pg.893]

Few peptide bonds that are hydrolyzed by proteolytic enzymes are accessible without prior denaturation of dietary proteins (by heat in cooking and by the action of gastric acid). [Pg.477]

ANDERSON J w, JOHNSTONE B M and cooK-NEWELL M E (1995) Meta-analysis of the effects of soy protein intake on serum lipids. N Engl J Med. 333 (5) 276-82. [Pg.212]


See other pages where Protein cooking is mentioned: [Pg.84]    [Pg.108]    [Pg.318]    [Pg.143]    [Pg.84]    [Pg.108]    [Pg.318]    [Pg.143]    [Pg.21]    [Pg.134]    [Pg.150]    [Pg.476]    [Pg.480]    [Pg.433]    [Pg.32]    [Pg.32]    [Pg.33]    [Pg.33]    [Pg.368]    [Pg.368]    [Pg.274]    [Pg.334]    [Pg.337]    [Pg.185]    [Pg.297]    [Pg.304]    [Pg.5]    [Pg.28]    [Pg.449]    [Pg.449]    [Pg.454]    [Pg.190]    [Pg.230]    [Pg.71]    [Pg.157]    [Pg.432]    [Pg.307]    [Pg.224]    [Pg.139]    [Pg.49]    [Pg.295]    [Pg.159]   
See also in sourсe #XX -- [ Pg.75 ]

See also in sourсe #XX -- [ Pg.109 ]




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