Abstract
Effects of high-pressure treatment on the modifications of soy protein in soy milk were studied using various analytical techniques. Blue shifts of λ max could be observed in the fluorescence spectra. Spectrofluorimetry revealed that the soy protein exhibited more hydrophobic regions after high-pressure treatment. Electrophoretic analysis showed the change of soy protein clearly and indicated that soy proteins were dissociated by high pressure into subunits, some of which associated to aggregate and became insoluble. High-pressure denaturation occurred at 300 MPa for β-conglycinin (7S) and at 400 MPa for glycinin (11S) in soy milk. High pressure-induced tofu gels could be formed that had gel strength and a cross-linked network microstructure. This provided a new way to process soy milk for making tofu gels.
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