FUNCTIONAL TECHNOLOGICAL PROPERTIES AND ELECTROPHORETIC COMPOSITION OF MODIFIED WHEAT GLUTEN

This article provides data on correlation between functional technological properties of native and modified wheat gluten and its specific molecular weights, with an objective to develop control methods for adjustment of physical and chemical specifications of protein products. We used methods for chemical composition analysis in protein products, protein electrophoresis (PAGE), and DWG modifications. We used enzymatic preparations (EP) for DWG properties modification: endoprotease EP (Protamex®) and Flavourzyme 500 MG, which contains both endoprotease and endopeptidase simultaneously. It is shown that native DWG underperforms in its functional technological properties in comparison to sodium caseinate, soy flour, soy concentrate, and egg albumin, therefore its properties are modified by limited proteolysis with protein hydrolysis degree of 1.10-3.41%. Our findings indicate that hydrolysis duration might be used to control DWG properties: to increase solubility, foam forming capacity (FFS) up to the respective values demonstrated by egg albumin, and at the same time, to reduce water- and fat-binding capacity and fat emulsifying capacity. DWG with improved FFS contains single-chain polypeptides, both with low molecular weight (МE) (under 40 kDа), and with medium ME (40-60 kDа). Among multi-chain peptides with more pronounced foam-forming capacity, presence of single-chain peptides with low ME (12-16 kDа) seems more preferable than polypeptides with medium (27-39 kDа) and high ME (69-108 kDа). Revealed regularities in correlation of DWG functional properties and ME / composition specificity are intended to be used in DWG modification for further various applications in food industry, mostly for pastries production

Protective effect of dinitrosyl iron complexes with glutathione in red blood cell lysis induced by hypochlorous acid

Hypochlorous acid (HOCl), one of the major precursors of free radicals in body cells and tissues, is endowed with strong prooxidant activity. In living systems, dinitrosyl iron complexes (DNIC) with glutathione ligands play the role of nitric oxide donors and possess a broad range of biological activities. At micromolar concentrations, DNIC effectively inhibit HOCl-induced lysis of red blood cells (RBCs) and manifest an ability to scavenge alkoxyl and alkylperoxyl radicals generated in the reaction of HOCl with tert-butyl hydroperoxide. DNIC proved to be more effective cytoprotective agents and organic free radical scavengers in comparison with reduced glutathione (GSH). At the same time, the kinetics of HOCl-induced oxidation of glutathione ligands in DNIC is slower than in the case of GSH. HOCl-induced oxidative conversions of thiolate ligands cause modification of DNIC, which manifests itself in inclusion of other ligands. It is suggested that the strong inhibiting effect of DNIC with glutathione on HOCl-induced lysis of RBCs is determined by their antioxidant and regulatory properties