Wheat Proteins and Peptides

Kumagai, Hitomi

doi:10.1002/9780813811048.ch20

Cited by 12 publications

(3 citation statements)

References 106 publications

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“…The epitopes recognizable by the R5 and the G12 antibodies are likely to be present in higher amounts in the extracts derived from the hexaploid wheats than in those from the tetraploid and diploid wheat varieties. However, club wheat, a hexaploid wheat, tested comparatively low for apparent gluten content ( Table 3 ), a result that is predictable because club wheat has been known for its low gluten content [ 39 ]. The differences noted between the grain samples in this study suggest the evolution of polyploidies that contain multiple copies of genetically diverse proteins.…”

Section: Resultsmentioning

confidence: 99%

Challenges in Gluten Analysis: A Comparison of Four Commercial Sandwich ELISA Kits

Amnuaycheewa

Niemann

Goodman

et al. 2022

Foods

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Gluten is composed of prolamin and glutelin proteins from several related grains. Because these proteins are not present in identical ratios in the various grains and because they have some differences in sequence, the ability to accurately quantify the overall amount of gluten in various food matrices to support gluten-free labeling is difficult. Four sandwich ELISAs (the R-Biopharm AG R5 RIDASCREEN®, the Neogen Veratox® R5, the Romer Labs AgraQuant® G12, and the Morinaga Wheat kits) were evaluated for their performance to quantify gluten concentrations in various foods and ingredients. The Morinaga and AgraQuant® G12 tests yielded results comparable to the two R5 kits for most, but not for certain, foods. The results obtained with the Morinaga kit were lower when compared to the other kits for analyzing powders of buckwheat and several grass-based products. All four kits were capable of detecting multiple gluten-containing grain sources including wheat, rye, barley, semolina, triticale, spelt, emmer, einkorn, Kamut™, and club wheat. Users of the ELISA kits should verify the performance in their hands, with matrices that are typical for their specific uses. The variation in results for some food matrices between test methods could result in trade disputes or regulatory disagreements.

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Section: Resultsmentioning

confidence: 99%

Challenges in Gluten Analysis: A Comparison of Four Commercial Sandwich ELISA Kits

Amnuaycheewa

Niemann

Goodman

et al. 2022

Foods

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“…Wheat berries enhance subtly flavoured foods, such as chicken and shellfish. Wheat is a good source of bioactive peptides [51]. When combined with other whole-grain to form a well-balanced and healthy diet, wheat berry can significantly influence many aspects of overall health.…”

Section: Wheat Berriesmentioning

confidence: 99%

Nutritional Composition of Grain and Seed Proteins

Oso¹,

Ashafa²

2021

Grain and Seed Proteins Functionality

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Grains including wheat, brown rice, millet, oat, and seeds from crops such as pumpkins, almonds, cashew, peas are important staple foods in many parts of the world. Grains and seeds contain proteins and bioactive peptides classified as nutraceuticals. Proteins and peptides are essential components in man’s diet because they provide the raw materials needed for protein biosynthesis and are also a good source of energy. Incorporating grains and seeds into the human diet provide nutritional, functional health benefits, reducing contracting some chronic diseases. They avail the body with a balanced nutrient profile such as carbohydrate, fatty-acid, fibre, B vitamins, minerals and protein. The quest at exploring staples for their functional and health benefits, as well as reducing risks to diseases, has resulted in the investigation of the potentials of grains and seeds, especially the underutilised ones (African yam bean, pigeon pea, Bambara groundnut etc.) for consumption and as an alternative therapy against diseases. This chapter discusses grains and seeds as sources of nutrition protagonist, their nutritive property, health benefits, and the pharmacological properties of bioactive peptides in grains and seeds. However, some under-utilised grain and seed proteins would also be explored for their nutritive potentials.

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“…These properties of wheat protein are also useful for cosmetics such as soaps, shampoos, hair conditioners, skin moisturizers and facial creams to meet specified usages required [3]. Gluten, a protein composite of gliadin and glutenin, accounts for almost Foods 2020, 9, 635 2 of 14 86% of all wheat proteins, gliadin content being about 40%, and glutenin content being about 46% [4], and is often used for cosmetics after treatment with an acid like hydrochloric acid (HCl) [5]. However, despite the effectiveness of acid treatment to increase the solubility of gluten in water and improve its emulsifying and foaming properties [3], the produced peptides carry a risk of people developing an allergy to wheat when they use cosmetics containing acid-treated gluten [6].…”

Section: Introductionmentioning

confidence: 99%

Allergenicity of Deamidated and/or Peptide-Bond-Hydrolyzed Wheat Gliadin by Transdermal Administration

Abe

Matsukaze

Kobayashi

et al. 2020

Foods

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Hydrochloric acid (HCl)-treated wheat protein (HWP) is widely used in various products, including foods, cosmetics and shampoos. Recently, immediate hypersensitivity towards facial soap containing HWP has been reported. HCl treatment of protein causes hydrolysis not only of main-chain amide bonds (peptide-bond hydrolysis) but also of side-chain ones (deamidation). We have already reported that gliadin, the main allergen in wheat, reduces allergenicity and increases digestibility by deamidation, indicating that deamidation and peptide-bond hydrolysis are effective to reduce the allergenicity of wheat protein. However, transdermally administered HWP is assumed to induce sensitization to orally administered wheat protein even in those who have been taking wheat products daily before sensitization. The present study was conducted to examine which structural change is responsible for the induction of cutaneous sensitization by comparing the allergenicity of deamidated and/or peptide-bond-hydrolyzed wheat gliadin. Because we have developed a deamidation method without causing peptide-bond hydrolysis, only deamidated wheat gliadin is available. Therefore, after deamidated-only, hydrolyzed-only, and deamidated and hydrolyzed gliadins were transdermally administered to mice for several weeks, the corresponding gliadin was intraperitoneally administered and allergenicity was evaluated. Transdermal administration of deamidated and hydrolyzed gliadin induced severe allergic reaction, while that of deamidated-only and hydrolyzed-only gliadin showed almost no allergic response. This result indicates that both deamidation and peptide-bond hydrolysis are necessary to increase the allergenic potency of transdermally administered wheat gliadin.

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Wheat Proteins and Peptides

Cited by 12 publications

References 106 publications

Challenges in Gluten Analysis: A Comparison of Four Commercial Sandwich ELISA Kits

Challenges in Gluten Analysis: A Comparison of Four Commercial Sandwich ELISA Kits

Nutritional Composition of Grain and Seed Proteins

Allergenicity of Deamidated and/or Peptide-Bond-Hydrolyzed Wheat Gliadin by Transdermal Administration

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