Wheat embryo globulin protects against acute alcohol-induced liver injury in mice.

Wheat Embryo Globulin (WEG) is a high-quality plant-derived protein with anti-inflammatory, antioxidant, and immunity enhancement effects. WEG was prepared and characterized using free amino acid analysis, circular dichroism (CD), and scanning electron microscope (SEM). The liver protection effect of WEG on mice after acute alcohol stimulation was also investigated. Male KM mice were randomly divided into four groups (n = 10). Animals were orally administrated with WEG (60 mg/kg), silymarin (50 mg/kg), and the same volume of saline solution daily for 30 days, before administering an alcohol-intragastric injection. Results displayed that the liver index, the levels of serum total cholesterol (TC), serum triglyceride (TG), liver malondialdehyde (MDA) and the mRNA expression of CYP2E1were significantly decreased in WEG-treated mice compared with the model group. Meanwhile, the levels of serum high-density lipoprotein-cholesterol (HDL-C), hepatic reduced glutathione (GSH), superoxide dismutase (SOD) and the mRNA expression of ADH2 and ALDH2 were remarkably increased. Effect of WEG on histopathology of liver tissue confirmed its protective function. Meanwhile, GSH level of ileal was significantly increased, MDA was remarkably decreased in WEG-treated mice, which also indicated that WEG possessed a positive effect on intestinal micro ecological environment health to some extent. In conclusion, WEG is a promising agent for the prevention of acute alcoholic liver injury.

Digestive characteristics and peptide release from wheat embryo proteins in vitro.

Due to the scarcity of the data on digestion and metabolism of wheat embryo proteins WEP, a simulated gastrointestinal digestion (SGID) scheme in vitro was utilized to explain the protein hydrolysis and biological activity of WEP during the digestion process. WEP had a certain degree of resistance to gastric digestion, especially the protein with a molecular weight of 50 kDa. In all the samples, no visually intact protein band emerged in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) during the intestinal phase, which was consistent with a gradually increasing content of released free amino acids. Moreover, the resistant digestion peptides (the amino acid sequences were ISQFXX and GTVX) were identified at the end of the gastrointestinal digestion (GID) product by high performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS). Although the complete protein in the sample was degraded, the antioxidant activity was not negatively affected, rather it showed an increasing trend and maintained a higher level of activity. The amount of the ß-sheet gradually increased as that of the α-helix declined, the random coil decreased, whereas no obvious change was noticed in ß-turn content. The results provide a better understanding for optimal selection of peptide candidates for designing protein products in the food processing industry as well as for WEP digestion and metabolism in the human body.