Wheat Gluten Proteins, Amino Acid Composition of Proteins in Wheat Gluten

Woychik, J.H.; Boundy, Joyce A.; Dimler, R. J.

doi:10.1021/jf60116a020

Cited by 94 publications

(34 citation statements)

References 2 publications

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“…Furthermore, previous studies have shown that there is no difference between coeliac and non-coeliac duodenal mucosa in their prolidase or prolinase activities (Messer et al, 1961). It is nevertheless possible, as suggested by Krainick et al (1959), that the postulated coeliac-active peptide consists mainly of glutamine and proline, if only for the reason that these two amino-acids together constitute over 50 % of the protein (Woychik, Boundy, and Dimler, 1961). The apparent resistance of the coeliac-active constituent of gluten to a variety of proteases (pepsin, trypsin, pancreatin, pure papain, and probably also chymopapain) suggests that it has an unusual amino-acid composition; this could well be due to a high proline content.…”

Section: Discussionmentioning

confidence: 93%

Studies on the mechanism of destruction of the toxic action of wheat gluten in coeliac disease by crude papain

Messer¹,

Anderson²,

Hubbard³

1964

Gut

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EDITORIAL SYNOPSIS The toxic action of wheat gluten on two patients was eliminated after predigestion of gluten by crude papain. This change is thought to be due to an enzyme which liberates ammonia from gluten. It is not thought that this particular mechanism operates in the normal intestinal cell but it is envisaged that one of the peptide bonds of the coeliac active constituent (possibly a N-glutaminyl peptide) is normally split by a specific intestinal peptidase which is defective in coeliac patients.Previous authors have shown that the harmful action of dietary wheat gluten in coeliac disease or non-tropical sprue is not eliminated by predigesting the gluten with either pancreatin or pepsin or trypsin

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Section: Discussionmentioning

confidence: 93%

Studies on the mechanism of destruction of the toxic action of wheat gluten in coeliac disease by crude papain

Messer¹,

Anderson²,

Hubbard³

1964

Gut

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“…6 This scheme of referring to the fast-, medium-and low-mobility sections of the main gliadin group which runs ahead of the athin group2 as a-, p-, and y-gliadins respectively is useful. Unfortunately it was originally based on the limited resolution achieved on the Tiselius apparatus.…”

Section: Results and Discussion Nomenclaturementioning

confidence: 99%

Relationship between wheat proteins

Booth¹,

Ewart²

1970

J Sci Food Agric

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Recent evidence including amino acid analyses, immunological tests and fingerprinting suggests that the gliadins of wheat varieties have evolved from a common ancestral protein by a series of mutations. No evidence to support a relationship of this nature between the gliadin, albumin and globulin classes was found. Confirmation of the genetic link between wheat and barley is provided by the close structural affinity between purothionin and its barley counterpart. There are some similarities in amino acid composition between a barley trypsin inhibitor and a wheat albumin. Available evidence, though scanty, is significant enough to justify the generalisation that storage proteins of identical mobility in different wheat varieties have closely similar primary and tertiary structures. Although the individual gliadins within a given variety are mutationally linked, their tertiary structures as judged by immunological tests show characteristic differences.

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“…Wheat proteins are high in proline and during dough mixing form an extensive gluten network with large hydrophobic domains. 19 Thus, wheat-based products provide an excellent opportunity to investigate how protein interaction with PA may impact starch digestibility during food processing. Tortillas are an increasingly important baked product; they are popular because of their convenience and versatility as wraps for various foods and condiments.…”

Section: ■ Introductionmentioning

confidence: 99%

Interaction of Sorghum Tannins with Wheat Proteins and Effect on in Vitro Starch and Protein Digestibility in a Baked Product Matrix

Dunn¹,

Yang²,

Girard³

et al. 2015

J. Agric. Food Chem.

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Carbohydrates contribute the most dietary calories, which makes starchy foods a logical target for modifying calorie intake. This study investigated the interaction of sorghum bran proanthocyanidins (PA) with proteins during wheat flour tortilla processing and impact on in vitro starch digestibility. Brans from wheat, white (low in phenols), brown (high PA), and black (high monomeric flavonoids) sorghum were used. Changes in phenolic profile, starch, and proteins were evaluated. Dough mixing drastically decreased extractable PA (61-72%) but not monomeric phenolics; higher MW PA decreased the most. The high PA bran dough produced the highest insoluble proteins (460 vs 330 mg/g protein for other sorghum brans) at 25% baker's substitution. The high PA bran tortillas also had higher slow digesting starch and lower rapidly digesting starch than all other bran treatments. Significant sorghum PA-gluten interactions occur during dough mixing that may slow starch digestibility in the baked products.

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Wheat Gluten Proteins, Amino Acid Composition of Proteins in Wheat Gluten

Cited by 94 publications

References 2 publications

Studies on the mechanism of destruction of the toxic action of wheat gluten in coeliac disease by crude papain

Studies on the mechanism of destruction of the toxic action of wheat gluten in coeliac disease by crude papain

Relationship between wheat proteins

Interaction of Sorghum Tannins with Wheat Proteins and Effect on in Vitro Starch and Protein Digestibility in a Baked Product Matrix

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