Abstract
High pressure (HP) treatment of a casein micelle suspension at 250 and 300 MPa leads to an initial rapid increase of its light transmission, as measured in situ, indicating micellar disruption. Subsequently, a much slower, partial reversal of the HP‐induced increase in light transmission is observed, indicating re‐association of micellar fragments. Partial internal cross‐linking of the casein micelles by the enzyme transglutaminase prior to pressure treatment slows down both the disruption and the reassociation process considerably. It is proposed that covalent cross‐linking provides the micelle with extra stability against pressure‐induced disruption and also prevents a molecular reorganization process required to induce reassociation of micellar fragments during prolonged pressure treatment.
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