[Wheat protein disulfide reductase].
Proteindisulphide reductase is isolated and partially purified from wheat seedlings and some properties of the enzyme are studied: pH optimum is 7.4; temperature optimum - 37 degrees C; Km = 2.6-10(-4)M for the substrate (wheat albumin); Km = 7.5-10(-5) M for coenzyme (NADP-H). The enzyme is specific for NADP-H and is not active in the presence of NAD-H. Maximal activity of proteindisulphide reductase is developed in anaerobic conditions. A technique of the estimation of proteindisulphide reductase activity using wheat albumin as a substrate is worked out. The enzyme activity decreases regularly in the corn ripening and increases under germination. It is accompanied by the respective increase or decrease in the amount of disulphide bonds in gluten protein and by changes of physico-chemical characteristics of gluten. Incubation of gluten with the enzyme preparation affects reological properties of gluten (it becomes weaker) and decreases the gluten viscosity of gluten solution.
[Wheat protein disulfide reductase]. Proteindisulphide reductase is isolated and partially purified from wheat seedlings and some properties of the enzyme are studied: pH optimum is 7.4; temperature optimum - 37 degrees C; Km = 2.6-10(-4)M for the substrate (wheat albumin); Km = 7.5-10(-5) M for coenzyme (NADP-H). The enzyme is specific for NADP-H and is not active in the presence of NAD-H. Maximal activity of proteindisulphide reductase is developed in anaerobic conditions. A technique of the estimation of proteindisulphide reductase activity using wheat albumin as a substrate is worked out. The enzyme activity decreases regularly in the corn ripening and increases under germination. It is accompanied by the respective increase or decrease in the amount of disulphide bonds in gluten protein and by changes of physico-chemical characteristics of gluten. Incubation of gluten with the enzyme preparation affects reological properties of gluten (it becomes weaker) and decreases the gluten viscosity of gluten solution.