Abstract
AbstractDependent on the pH, time and temperature, increasing concentrations of aluminium chloride cause an increase of firmness and a decrease of solubility of Vicia faba protein/casein (1:1) fibers. This effect is accompanied by a loss of sulfhydryl and reactive disulfide groups as well as by a masking of reactive disulfide groups and it is interpreted by a formation of trivalent aluminium coordination complexes with carboxyl and sulfhydryl groups of the protein, thus resulting in a crosslinking.Dependent on sodium hydrogen carbonate concentration, time and temperature, an increasing sodium chloride concentration leads to a further improved firmness of the protein fibers. By this treatment a further masking of reactive disulfide groups does not take place and therefore the effect on the firmness of the protein fibers may be explained by a stabilization of the crosslinkages.
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