DOI: 10.1159/000394766
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Nutritional and Physiological Consequences of the Maillard Reaction

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Cited by 129 publications
(72 citation statements)
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“…Lys is most susceptible to Maillard reactions due to the presence of an ε-amino group on the molecule that can react directly with reducing sugars under moist, hot conditions. The loss of digestibility of the other amino acids indicated that advanced Maillard reactions such as Strecker degradations were also occurring (Adrian 1974). Desolventization toasting changed the colour of the meal from a light yellow to the characteristic brown of canola meal (visual observation, data not shown), which also indicates advanced Maillard reactions.…”
Section: Discussionmentioning
confidence: 95%
“…Lys is most susceptible to Maillard reactions due to the presence of an ε-amino group on the molecule that can react directly with reducing sugars under moist, hot conditions. The loss of digestibility of the other amino acids indicated that advanced Maillard reactions such as Strecker degradations were also occurring (Adrian 1974). Desolventization toasting changed the colour of the meal from a light yellow to the characteristic brown of canola meal (visual observation, data not shown), which also indicates advanced Maillard reactions.…”
Section: Discussionmentioning
confidence: 95%
“…At the present time, pediatric textbooks and the instructions from several infant formula companies recommend sterilization when mixing formula from concentrate or powder or when adding ready-to-feed formula to bottles (Gerber et al, 1983;Feder and Pugno, 1986). It is well established that, in the Maillard reaction after heat treatment, lysine is lost through its interaction with reducing sugars to form biologically unavailable deoxyketosyl derivatives (Adrian, 1974;Desrosiers and Savole, 1994). However, there is little published information on the reduced availability of amino acids other than lysine, especially in infant formulas.…”
Section: Discussionmentioning
confidence: 99%
“…The reduced availability observed for aspartic and glutamic acids, threonine, cystine, methionine, histidine, and lysine after severe heat treatment may be explained by interaction within protein segments. This advanced Maillard reaction may have additional undesirable consequences for nutrition (Kilshaw et al, 1982;Adrian, 1974;Rigo et al, 1994). The FAA composition or bioavailability in formulas may also be altered during processing and enzymatic hydrolysis (Donovan and Lonnerdal, 1989;Recio and Olieman, 1996;Needs et al, 2000).…”
Section: Discussionmentioning
confidence: 99%
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