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Envisioning Utilization of Super Grains for Healthcare
Published in Megh R. Goyal, Preeti Birwal, Santosh K. Mishra, Phytochemicals and Medicinal Plants in Food Design, 2022
Quinoa is a rich source of proteins, which range from 13.8 to 16.5% [126]. Unlike conventional cereals, prolamin content is low (0.5%–0.7%) and albumins and globulins are the major storage proteins present at 35% and 37% levels, respectively [1], thus it is a gluten-free grain. All the essential amino acids (EAAs) are present in balanced amounts and it is especially rich in lysine (2.4–7.8 g/100 g), threonine (2.1–8.9 g/100 g) and methionine (0.3–9.1 g/100 g), which are limiting in conventional cereals [57]. According to FAO/WHO recommendations, quinoa protein can supply over 180% of the daily recommended intake of essential amino acids for adult nutrition [193]. Quinoa protein digestibility ranges as high as 91.6% for raw seeds and 95.3% for cooked seeds [153].
Celiac Disease in Infancy and Childhood
Published in Tadeusz P. Chorzelski, Ernst H. Beutner, Vijay Kumar, Tadeusz K. Zalewski, Serologic Diagnosis of Celiac Disease, 2020
Thomas Rossi, Tadeusz Zalewski
The endosperm of wheat contains a heterogeneous group of proteins which are differentiated based upon their solubility properties. Gluten comprises about 90% of the protein contained in wheat flour. It is contained in the water-insoluble extraction fraction of wheat flour. The water-soluble portion contains starch, albumin, and globulin. Gluten itself is composed of many different protein moieties which are separated into two general classes based upon ethyl alcohol extraction. Gliadin is an alcohol-soluble protein group, whereas glutenin is found in the alcohol-insoluble portion. Prolamins are alcohol-soluble proteins similar to gliadin found in other grains. Those in rye are termed secalins, whereas horleins are contained in barley. The toxicity of cereals other than wheat is most likely associated with the latter, prolamins.8,38
Biomolecular and Clinical Aspects of Food Allergy
Published in Andreas L. Lopata, Food Allergy, 2017
The prolamins which are characterized by high levels of glutamine and proline residues are restricted to the grasses including major cereals such as wheat, barley and rye (Shewry et al. 1995). The prolamin seed storage proteins of wheat are the major components of gluten, which determines the quality of the flour for bread making. The complex mixture of cereal storage proteins, the gluten, consists of roughly equal amounts of gliadins and glutenins (Tatham and Shewry 2008). Gliadins are monomeric proteins, which interact by noncovalent forces. Based on their electrophoretic mobility they are divided into the fast moving α/β-gliadins, the intermediate γ-gliadins, and the slowly moving ω-gliadins. The glutenins are polymers of individual proteins that are linked by interchain disulfide bridges. Glutenins can be classified into high molecular weight (HMW) and low molecular weight (LMW) groups. The sulfur-rich prolamins are quantitatively the major prolamin group in wheat, barley and rye, and they include polymeric and monomeric proteins (Shewry and Tatham 1990). Wheat-dependent exercise-induced anaphylaxis (WDEIA) is associated with ω5-gliadins (Tatham and Shewry 2008) while both gliadins and glutenins appear to be implicated in baker’s asthma (Quirce and Diaz-Perales 2013).
The role of oxidative stress in pulmonary function in bakers exposed to flour dust
Published in International Journal of Occupational Safety and Ergonomics, 2022
Vahid Gharibi, Mohammad Hossein Ebrahimi, Esmaeel Soleimani, Narges Khanjani, Anahita Fakherpour, Majid Bagheri Hosseinabadi
Wheat flour dust is a complex organic compound containing various antigens and allergic compounds [1]. The antigens found in wheat flour include the enzymes in flour itself (e.g., α-amylase, cellulase, hemicellulose, maltase, protease, lipase, glucoamylase, glucosidase, lipoxygenase) or from additives (e.g., bakery yeast, egg powder, milk powder, sugar, flavors, spices), chemical compounds (e.g., preservatives, antioxidants, bleaching agents) and contaminants associated with storage (e.g., microbes, mites) [2]. In addition, wheat flour includes water-soluble albumin, saline-soluble globulins, gliadins and glutens [2]. Albumins and globulins are potentially allergic proteins. The allergic potential of prolamins and glutelins should also be considered. According to Sander et al. [3], flour dust has at least 40 allergens, which can cause harmful health effects in the exposed population. Exposure to flour dust occurs in a wide range of food industries, including flour mills and bakeries. The type of interaction between the bioaerosol particles and human cells depends on the part of the respiratory tract where the particles deposit.
A review on the relationship between gluten and schizophrenia: Is gluten the cause?
Published in Nutritional Neuroscience, 2018
Can Ergün, Murat Urhan, Ahmet Ayer
Celiac disease is a lifelong auto-immune disease diagnosed in patients who possess a genetic predisposition which shows susceptibility to gluten and disruptions in the small intestine. Gluten is found in wheat, barley, oat, and rye. Gluten is characterized as a protein, which stores prolamin and glutelin. The majority of proteins in foods that are responsible for immunological reactions, which lead to the onset of celiac disease, are prolamins. Prolamins are found in varying forms in several grains, such as gliadin in wheat, hordein in barley, secalin in rye, and zein in corn. Gliadin is an essential monomeric protein with a molecular weight ranging between 28 000 and 55 000. It consists of four types: α-, β-, Ɣ-, and ω-. They have high amounts of glutamine and are resistant to gastrointestinal proteolytic enzymes. The most toxic form of gliadin, α-gliadin 33mer, is one of the digestion-resistant gluten peptides that show high reactivity for isolated celiac T cells. It is the main immune-dominant toxic peptide. Other significant types that show toxic effects are α-gliadin p31–43.8–11
Overview on zein protein: a promising pharmaceutical excipient in drug delivery systems and tissue engineering
Published in Expert Opinion on Drug Delivery, 2018
Zea maysL. or corn is one of the most important crops for all populations throughout the world. It comprises high nutritive values due to the existence of several components including the proteins. It has from 6% to 12% protein based on its dry weight. Seventy-five percent of this protein lies in the tissues of endosperm while the 25% remaining are divided between the germ and barn. Corn protein is differentiated into four types, namely, albumins, globulins, glutelin, and zein [8]. John Gorham named zein in 1821. He was able to isolate and identify it in Zea on the same year [22]. It is mainly in the endosperm and believed to belong to prolamines protein class having a molecular weight of about 40 kDa [23]. However, a more recent study showed that α and δ zein are the only ones considered as prolamine proteins while β and γ zein are considered glutelin [24]. Although it has a low nutritive value as it lacks essential amino acids as lysine and tryptophan, zein comprises in its content several peptides that differ in solubility and molecular weights, and it is rich in glutamic acid, leucine, proline, and alanine [25]. The presence of these large molecular weight peptides renders it hydrophobic [26]. Pure zein is odorless, tasteless solid, water insoluble, alcohol soluble, biologically biodegradable, and most of all is edible [27]. These properties allowed for the diverse utility of zein in several industrial fields.