Biomolecular and Clinical Aspects of Food Allergy
Andreas L. Lopata in 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).
Envisioning Utilization of Super Grains for Healthcare
Megh R. Goyal, Preeti Birwal, Santosh K. Mishra in 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
John F. Pohl, Christopher Jolley, Daniel Gelfond in Pediatric Gastroenterology, 2014
Wheat, and the taxonomically related rye and barley, serve as the environmental trigger in celiac disease patients. Wheat gluten is a protein composite that remains after starch is washed from wheat flour dough. In baking, gluten is responsible for dough elasticity, viscosity (thickness), and increased moisture absorption; however, it is also used as a stabilizing agent in nonbaking products, such as ice cream and ketchup, and as an excipient in many medications. Gluten is a protein composite of gliadins (monomers) and glutenins (polymers), with the gliadin protein being the primary immunogenic and toxic fraction. Barley and rye both possess prolamin fractions equivalent to wheat gliadins (hordeins and secalines, respectively) and demonstrate the same toxic properties in celiac patients.
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
Coeliac disease: beyond genetic susceptibility and gluten. A narrative review
Published in Annals of Medicine, 2019
Giovanni Mario Pes, Stefano Bibbò, Maria Pina Dore
The importance of environmental exposures other than gluten is further strengthened by studies on migrants from low CD risk regions who acquire the higher prevalence of the receiving country [8,9]. In recent years, considerable efforts have been made to disentangle the complex interplay between genetic factors, gluten (and other prolamin- or glutenin-containing dietary proteins), and the gut mucosal immune system.
Bacterial outer membrane vesicles-cloaked modified zein nanoparticles for oral delivery of paclitaxel
Published in Pharmaceutical Development and Technology, 2023
Zeyu Wang, Yuqi Chu, Xu Tao, Jianchao Li, Lihong Wang, Yuli Sang, Xiuli Lu, Lijiang Chen
Recently, a broad range of new drug delivery systems has been developed, including liposomes, micelles, nanoemulsions, and nanogels (Arranja et al. 2017). Among these, amphiphilic protein biopolymers used to encapsulate and deliver bioactive compounds have attracted increasing attention. The availability of natural resources, inherent biocompatibility and biodegradability, and ease of binding to specific drugs and ligands are the key characteristics of natural proteins as potential efficient nanocarriers (Bhattacharya et al. 2021). More intriguingly, plant-derived proteins have emerged as strong contenders in a variety of pharmaceutical designs. Compared with animal-derived proteins, they are more dependable owing to being renewable and relatively affordable to prepare (Abdelsalam et al. 2021). Zein is an insoluble prolamin protein generated from corn (Parris and Dickey 2001) that is soluble in 60–85% ethanol, has two-thirds lipophilic and one-third hydrophilic amino acid residues (Argos et al. 1982; Zhong and Jin 2009), and is 50 times more hydrophobic than albumin or fibrinogen (Chen Y et al. 2014). Moreover, it is known that zein is columnar and self-assembles into particles and layers based on its molecular structure (Argos et al. 1982; Sousa et al. 2012). Thus, zein can easily self-assemble into nanoparticles that act as a solubility enhancer for poorly water-soluble nutrients and drugs (Zhao et al. 2020; Reboredo et al. 2021). However, zein nanoparticles are generally hydrophobic and easy to aggregate or precipitate. It is reported that modified nanoparticles with stabilizers such as sodium caseinate (CAS) (Luo, Teng, et al. 2013), pectin (Zhang et al. 2021), gum arabic (Spasojević et al. 2020), and carboxymethyl chitosan (Luo, Wang, et al. 2013) can effectively improve the stability of zein nanoparticles. Moreover, CAS stabilizes zein nanoparticles over a wide range of ionic strengths (Li H et al. 2018). CAS, a water-soluble salt of casein, consists of four main components (αs1-, αs2-, β-, and κ-casein) with high proportions of hydrophobic and hydrophilic amino acid residues. Casein-based formulations are widely used as emulsifiers, stabilizers (Urbánková et al. 2021), and drug delivery systems (Liu J et al. 2021) in the food and pharmaceutical industries due to the excellent surface activity and unique self-assembly properties of CAS as well as its low cost.