Gluten amino acids

Amino Gluten MG. [Croda to. Croda Chem. Ltd.] Maize gluten amino acids, sodium chloride conditioner to skin and hair creams and lotions hu-mectant to cosmetics, pharmaceuti-cdls ... 

Amino Acid Geiatinization Agent. See Acyl glutamic acid diamide Amino acids, corn gluten. See Com gluten amino acids... 

Corn gluten. See Corn (Zea mays) meal Corn gluten amino acids CAS 65072-01-7... 

Glutens, corn. See Com (Zea mays) meal Glutens, corn, hydrolyzed. See Corn gluten amino acids... 

Clintonia borealis extract Clover (Trifolium pratense) extract Cocoa (Theobroma cacao) extract Coffee (Coffea arabica) extract Coltsfoot (Tussilago farfara) extract Comfrey (Symphytum officinale) extract Coriander (Coriandrum sativum) extract Corn (Zea mays) extract Corn gluten amino acids Corn (Zea mays) gluten protein Crataegus monogina extract Cumin (Cuminum cyminum) extract Cypress (Cupressus sempervirens) extract Dandelion (Taraxacum officinale) extract Elder (Sambucus nigra) flower extract... 

Nitrogen sources include proteins, such as casein, zein, lactalbumin protein hydrolyzates such proteoses, peptones, peptides, and commercially available materials, such as N-Z Amine which is understood to be a casein hydrolyzate also corn steep liquor, soybean meal, gluten, cottonseed meal, fish meal, meat extracts, stick liquor, liver cake, yeast extracts and distillers solubles amino acids, urea, ammonium and nitrate salts. Such inorganic elements as sodium, potassium, calcium and magnesium and chlorides, sulfates, phosphates and combinations of these anions and cations in the form of mineral salts may be advantageously used in the fermentation. 

Seven diets were constructed from purified natural ingredients obtained from either C3 (beet sugar, rice starch, cottonseed oil, wood cellulose, Australian Cohuna brand casein, soy protein or wheat gluten for protein) or C4 foodwebs (cane sugar, corn starch, com oil, processed corn bran for fiber, Kenya casein for protein) supplemented with appropriate amounts of vitamins and minerals (Ambrose and Norr 1993 Table 3a). The amino acid compositions of wheat gluten and soy protein differ significantly from that of casein (Ambrose and Norr 1993). 

Electrostatic charges due to ionized acidic or basic amino acids influence protein solubility. At extremes of pH, many poorly soluble proteins are dissolved and their molecular structures unfolded due to surplus of similar repelling charges. Gluten proteins have few charged groups and so are poorly soluble in neutral solution (15). Dispersions of other proteins must be adjusted to their isoelectric point or have salt added to optimize cohesion and adhesion. 

Friedman (21) studied the effect of pH on the amino acid composition of wheat gluten. At pH 10.6 and above (65 C, 3 hours) no cystine was present. LAL increased with pH above 10.6. Lysine decreased over the same range of pH s, while serine and threonine contents dropped sharply at pH 13.9. Friedman concluded that cystine is most sensitive to alkali and that LAL will form most readily if lysine residues are in proximity to the dehydroalanine formed from cystine. Thus, he explained that different steric considerations may explain the different susceptibilities of wheat gluten, casein, and lactalbumin to LAL formation. 

PER is a method to metabolize or determine the quality of protein in foods. Quality is measured by the amount of usable protein and the growth resulting from it through an animal assay. Formerly, this method was used as the standard method for all protein quality analysis. However, there is some question as to whether or not it is a valid measurement. This is because PER does not account for the differences in amino acid requirements between humans and rats (Seligson and Mackey, 1984), nor does PER account for the protein needed for cell maintenance. Therefore, PER results often overestimate the requirements for some amino acids and underestimate others. Specifically, PER tends to underestimate the protein quality of lysine-deficient proteins such as wheat gluten (Hackler, 1977). 

Amino acid storage Seed proteins (e.g., gluten), milk proteins (e.g., casein)... 

Recently, limiting essential amino acids have been attached covalently to soy protein isolates (24) and wheat gluten (52) by the water-soluble... 

Our results have been recapitulated with other proteins of varying nutritional value to S. exigua and H. zea they include soy protein, tomato foliar protein, corn gluten and zein. In all cases, more than 2.5% dietary protein was required to alleviate antinutritional effects, because these proteins are less nutritious than casein (Table III). The ability of a protein to alleviate the toxicity of o-quinones is proportional to its nutritional value to the insect (Table III). The proteins ability to function as an alkylatable sink (alleviation of antinutritive effects) is correlated with the relative amounts of alkylatable amino acids (e.g., lysine, cysteine, histidine, methionine Felton and Duffey, unpublished data). 

The percentage of D-enanticmers relative to the total amount of the amino acid residue can be calculated by the relation (D/DfL) x 100. D-Aspartic acid accounts for 30% of that residue (which is thus 60% racemized) in treated casein, Pranine-D, and wheat gluten. In these three proteins, 22-30% of the phenylalanine (an essential amino acid) is the D-enanticmer, and in wheat gluten, 26% of glutamic acid has been converted to the D-form. 

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