Slow triplet β‐gliadin from cappelle‐desprez

Ewart, J. A. D.

doi:10.1002/jsfa.2740340617

Cited by 4 publications

(1 citation statement)

References 7 publications

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“…The protein structure is stabilized by the disulphide bonds formed between the cysteine residues (Shewry and Tatham, 1997). About 90% of the AA residues in these gliadins are present as the glutamic and aspartic acid residues in amide form (Ewart, 1983). The repetitive domain is composed of repeat units of PQPQPFP and PQQPY (Shewry and Tatham, 1990).…”

Section: Alpha and Beta Gliadinsmentioning

confidence: 99%

Biochemical and Functional Properties of Wheat Gliadins: A Review

Barak

Mudgil

Khatkar

2014

Critical Reviews in Food Science and Nutrition

132

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Gliadins account for 40-50% of the total storage proteins of wheat and are classified into four subcategories, α-, β-, γ-, and ω-gliadins. They have also been classified as ω5-, ω1, 2-, α/β-, and γ-gliadins on the basis of their primary structure and molecular weight. Cysteine residues of gliadins mainly form intramolecular disulfide bonds, although α-gliadins with odd numbers of cysteine residues have also been reported. Gliadins are generally regarded to possess globular protein structure, though recent studies report that the α/β-gliadins have compact globular structures and γ- and ω-gliadins have extended rod-like structures. Newer techniques such as Mass Spectrometry with the development of matrix-assisted laser desorption/ionization (MALDI) in combination with time-of-flight mass spectrometry (TOFMS) have been employed to determine the molecular weight of purified ω- gliadins and to carry out the direct analysis of bread and durum wheat gliadins. Few gliadin alleles and components, such as Gli-B1b, Gli-B2c and Gli-A2b in bread wheat cultivars, γ-45 in pasta, γ-gliadins in cookies, lower gliadin content for chapatti and alteration in Gli 2 loci in tortillas have been reported to improve the product quality, respectively. Further studies are needed in order to elucidate the precise role of gliadin subgroups in dough strength and product quality.

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Section: Alpha and Beta Gliadinsmentioning

confidence: 99%

Biochemical and Functional Properties of Wheat Gliadins: A Review

Barak

Mudgil

Khatkar

2014

Critical Reviews in Food Science and Nutrition

132

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Plant Protein‐based Nanoparticles

Orecchioni

Duclairoir

Irache

et al. 2003

Nanotechnologies for the Life Sciences

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The sections in this article are Introduction Description of Plant Proteins Pea Seed Proteins Wheat Proteins Preparation of Protein Nanoparticles Preparation of Legumin and Vicilin Nanoparticles Preparation of Gliadin Nanoparticles Drug Encapsulation in Plant Protein Nanoparticles RA Encapsulation in Gliadin Nanoparticles VE Encapsulation in Gliadin Nanoparticles Lipophilic, Hydrophilic or Amphiphilic Drug Encapsulation Preparation of Ligand–Gliadin Nanoparticle Conjugates Bioadhesive Properties of Gliadin Nanoparticles Ex Vivo Studies with Gastrointestinal Mucosal Segments In Vivo Studies with Laboratory Animals Future Perspectives Size Optimization Immunization in Animals Conclusion

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Exploring genetic variability for developing celiac disease safe wheat

Chhuneja

Arora

2020

Wheat and Barley Grain Biofortification

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Slow triplet β‐gliadin from cappelle‐desprez

Cited by 4 publications

References 7 publications

Biochemical and Functional Properties of Wheat Gliadins: A Review

Biochemical and Functional Properties of Wheat Gliadins: A Review

Plant Protein‐based Nanoparticles

Exploring genetic variability for developing celiac disease safe wheat

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