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• W1990386831 abstract "Hydrolyzed plant proteins are widely used as ingredients in culinary products for their glutamate-like (“umami”) taste. Three hydrolysates were prepared from wheat gluten using different enzymatic approaches. Comparison of their taste profiles revealed the enzymatic hydrolysate of an acid-deamidated wheat gluten (WGH-3) to be the least bitter of all and to elicit an intense glutamate-like taste. Its umami taste intensity was similar to that of an enzymatic hydrolysate in which glutaminase had been employed to convert free glutamine to glutamic acid and which had a 3-fold higher concentration of free glutamate. Reconstitution studies based on the results of the chemical analysis of WGH-3 and sensory comparison of the model solution and WGH-3 indicated that other components in addition to glutamate and organic acids contribute to its glutamate-like taste. WGH-3 was fractionated by gel permeation chromatography and reversed phase high-performance liquid chromatography, and two fractions with a pronounced glutamate-like taste were obtained. In one of them four pyroglutamyl peptides were tentatively identified: pGlu-Pro-Ser, pGlu-Pro, pGlu-Pro-Glu, and pGlu-Pro-Gln. Apparently, these peptides were formed by cyclization of the N-terminal glutamine residues during the preparation of the hydrolysates. Keywords: Wheat gluten; umami; taste; peptides; taste profile; taste-active compounds; gel permeation chromatography; HPLC; LC-MS; deamidation" @default.
• W1990386831 created "2016-06-24" @default.
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• W1990386831 date "2002-02-16" @default.
• W1990386831 modified "2023-10-11" @default.
• W1990386831 title "Analysis of Taste-Active Compounds in an Enzymatic Hydrolysate of Deamidated Wheat Gluten" @default.
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• W1990386831 doi "https://doi.org/10.1021/jf010989o" @default.
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