Basic introduction Chinese name: gliadin mbth: gliadin alias: gliadin source: wheat, corn classification: wheat gliadin, zein application: food, medicine, etc. Introduction, function, classification, extraction technology, introduction 18 gliadin was found in corn and wheat seeds. Wheat gliadin is a single-chain protein, and single peptides interact through hydrogen bonds and hydrophobic bonds. These two bonds have low energy and are easily "broken", so wheat gliadin makes gluten sticky and malleable, and flour with high gliadin content is suitable for making noodles. Gliadin in plant seeds is not widely used in biology because of the lack of lysine and other essential amino acids, but it has attracted much attention in other fields. In addition to the application of wheat gliadin in the processing of flour products, zein also shows its characteristics in food preservation and is also used in drug sustained-release agents. Glutenin in glutinous rice has also made remarkable achievements in the pharmaceutical industry and is used to treat stomach diseases. In addition, the existence of gliadin in coconut meat makes coconut milk have the function of beauty and skin care. Gliadin has strong water resistance, heat resistance and fat resistance, and is widely used in food, medicine, textile, paper making and other industries. In addition, gliadin can also produce bioactive peptides by enzymatic method, which can be used in pharmacy. Therefore, the production and development of gliadin is a very potential development direction. Glutamine in gliadin used to treat stomach diseases can guide the synthesis of muscle protein and glycogen in human gastrointestinal tract, and can greatly improve the formation of human gastric mucosa. It is the most effective natural protein known at present to solve gastrointestinal diseases such as intractable gastritis and gastric ulcer, and its clinical effect is remarkable. Gliadin can maintain the normal function and metabolism of cells, and gliadin in coconut meat can promote whitening. Coconut whitening mask: Squeeze coconut meat with a blender, remove residues, add a little flour and 1 egg white, stir well, apply it on your face 10 minutes and then wash it off. It has whitening and hydrating effects and is suitable for dry skin. Essential amino acids for nutritional supplement refer to amino acids that the human body can't synthesize by itself or the speed of synthesis can't meet the needs of the human body, and must be ingested from food. There are 8 kinds of amino acids to be ingested, including lysine, methionine, leucine, isoleucine, threonine, valine, tryptophan and phenylalanine. For people, gliadin contains essential lysine, arginine and histidine, which can supplement nutrition in time. Classification of gliadin in wheat gliadin accounts for about 4%-5% of the whole wheat flour, which is the main storage protein of endosperm and has high heterogeneity and complexity in composition. Under the condition of one-way A-PAGE electrophoresis, a variety can separate 15-30 components, while under the condition of two-way electrophoresis, up to 50 components can be separated. The molecular weight of gliadin is about 30,000-80,000 U, and it can be divided into four gliadin types: α, β, γ and ω according to its mobility in electrophoresis. They account for 25%, 30%, 30% and 15% of the total gliadin respectively. Gliadin is one of the main components of wheat gluten, which endows gluten with ductility and is an important factor affecting the baking quality of wheat bread. Up to now,11wheat gliadin alleles have been identified and named according to the new naming method, which brings great convenience to the research work. It is considered that alleles Gli -B 1b, GliB-2c and Gli-A2b are significantly related to gluten strength. Some gliadin bands related to quality were also found in the study. Gliadin band 45 found in durum wheat is associated with good gluten quality, while its allele band 42 is associated with poor gluten quality. In common wheat, gliadin bands 43.5 and 59.0 are associated with good gluten quality, while allele bands 40.0 and 58.0 are associated with poor gluten quality. At present, gliadin has been widely used in wheat quality improvement, seed purity identification, variety classification, heterosis prediction and other production and scientific research. Zein Zein is insoluble in water and anhydrous ethanol, but soluble in 60%-95% ethanol aqueous solution by volume. Although the amino acid composition of zein is unbalanced, its solubility, molecular shape and molecular structure are unique, and it can form a transparent, soft and uniform preservative film, which is an ideal natural preservative film material. In addition, zein has good emulsification, water retention, ductility and elasticity, and has broad application prospects in food. In the pharmaceutical field, zein is often used as the coating material of tablets. In recent years, it has been widely and deeply studied as a drug sustained-release material and biodegradable material. 65% gliadin colloidal solution was prepared with 95% ethanol solution, and zein bars were prepared by molding. The degradation process of zein in vivo and in vitro was studied by intrinsic viscosity, mass change and scanning electron microscope observation. It is found that zein can be degraded in vivo and in vitro, but the surface of zein strips degraded in vivo and in vitro is rough, but the overall shape remains unchanged, and the degradation rate in vivo is greater than in vitro. With the progress of degradation, the surface of the rod body gradually becomes rough, and concave absorption occurs in the body. The degradation of gliadin blank tablets in artificial gastrointestinal fluid was investigated by mass reduction rate and degradation rate. It was found that the mass reduction rate and degradation rate of zein in artificial gastrointestinal fluid increased with time, and the mass reduction rate lagged behind the degradation rate. It is considered that zein is degradable in artificial gastrointestinal fluid. However, the lack of nonpolar amino acids, hydrophobic amino acids and basic and acidic amino acids in its structure determines the dissolution behavior of zein, and it also contains more thioamino acids, which determines that zein has strong lipophilicity and solubility, can be dissolved in a certain concentration of alcohol solution, and has good film-forming characteristics. As a biodegradable material, it has broad application prospects, but it also determines that it must be modified to improve its solubility. Decolorization in the extraction process: weigh a certain amount of corn yellow powder, add 95% ethanol solution according to the material-liquid ratio of 1: 12, heat it to 80℃ in water bath, stir it at 300 r/min, put it in an ultrasonic cleaner for shock decolorization for 30 min, pour off the supernatant, and dry the precipitate to obtain decolorized corn yellow powder. Deodorization: Weigh 30 g of decolorized corn yellow powder into a beaker, add 4% β- cyclodextrin, adjust the pH to 6.0, soak at 40℃ for 4 h, and deodorize. Then centrifuge at 1000 r/min, discard the supernatant, wash with distilled water twice, discard the supernatant, and dry at 60℃. Sieving the zein corn flour extract, accurately weighing 3.0 g, adding a certain concentration of ethanol solution according to a certain material-liquid ratio, keeping the temperature at 50-60℃ for 30 min, adjusting the pH value with 1 mol/LNaOH solution, and performing ultrasonic treatment for a certain time. Centrifuge at 3000 rpm for 5 minutes, and collect supernatant. Add 30 mL distilled water to the supernatant, let it stand for 65438+/-0h, centrifuge to obtain wet zein, wash it with distilled water for three times, dry it at constant temperature and then crush it.