1987
DOI: 10.1093/jn/117.3.508
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Nutritional Value and Safety in Mice of Proteins and Their Admixtures with Carbohydrates and Vitamin C after Heating

Abstract: When a nutritionally complete basal diet containing 10% protein from casein was supplemented with 20% protein from unheated casein, wheat gluten or soy protein isolate, weanling mice exhibited significantly increased weight gains. In contrast, weight gains were markedly reduced compared to those with the basal diet; that is, growth was inhibited, when the supplement was soy protein or gluten that had been heated at 200 or 215 degrees C for 72 min in the dry state to stimulate crust baking. Addition of various … Show more

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Cited by 24 publications
(36 citation statements)
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“…Effect of pH and Heat. Food can deteriorate during processing and storage due to both enzymatic and Maillard-type reactions of primary amino groups with reducing sugars and other enzymatic and nonenzymatic browning reactions with nonreducing carbohydrates (Ebersdobler et al, 1991;Friedman and Molnar-Perl, 1990;Friedman et al, 1987;Kratzer et al, 1990;Oste et al, 1991;Ziderman et al, 1989). High pH induces racemization of L-amino acid residues to D-isomers Gumbmann, 1984a,b, 1989) and formation of cross-linked amino acids such as lysinoalanine (Friedman and Pearce, 1989;Friedman et al, 1982a).…”
Section: Composition Digestibility and Availabilitymentioning
confidence: 99%
“…Effect of pH and Heat. Food can deteriorate during processing and storage due to both enzymatic and Maillard-type reactions of primary amino groups with reducing sugars and other enzymatic and nonenzymatic browning reactions with nonreducing carbohydrates (Ebersdobler et al, 1991;Friedman and Molnar-Perl, 1990;Friedman et al, 1987;Kratzer et al, 1990;Oste et al, 1991;Ziderman et al, 1989). High pH induces racemization of L-amino acid residues to D-isomers Gumbmann, 1984a,b, 1989) and formation of cross-linked amino acids such as lysinoalanine (Friedman and Pearce, 1989;Friedman et al, 1982a).…”
Section: Composition Digestibility and Availabilitymentioning
confidence: 99%
“…Food ingredients developed by this extrusion have improved texture with enhanced physical properties including ex-vivo or in-vivo functionality [5]. Texturization of proteins by extrusion processing occurs at temperatures ranging from 50 to 100°C at short residence times of approximately 2 min [6]. However, information of this processing treatment on the survival and viability loss of microbial organisms present on treated food items is limited.…”
Section: Introductionmentioning
confidence: 99%
“…An extruder is one device used to accomplish texturization of proteins through the actions of its internal rotating screws pressing the protein against the fixed heated barrel walls, and forcing the molten protein mass through a restriction die that aligns the protein mass in the direction of rotational flow. Extrusion texturization of proteins can occur at temperatures ranging from 50 to 100 °C and at short residence times (< 2 min), far below the range of thermochemical denaturation conditions for other proteins, for instance, wheat glutens in dry heat from about 200 to 215 °C for 72 min (Friedman and others 1987), or collagen in moist heat below 120 °C for 30 min (Meyer and others 2005).…”
Section: Introductionmentioning
confidence: 99%