The structure modification of the main proteins from oilseeds and legumes by means of alkali- or acid-denaturation and succinylation, respectively, and its influence on the protein functionality is discussed. This kind of modification enables to improve the functional properties with minimal energy input.
Casein forms gels after modification by dialdehyde starch (DAS). The creep behavior of gels was studied with the Tolstoj apparatus. The total shear compliance and the plastic and elastic components there of were determined as a function of time. The influences of concentrations of casein and DAS, of pH, and of storage time were studied. Free amino groups and available lysine were determined, too. The processes of crosslinking of protein and of blocking of amino groups show different kinetics. At least two polypeptide chains of casein corresponds with one crosslink. This means that the crosslinking process is a supermolecular one.
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