Behaviour of partially cross-linked casein micelles under high pressure |
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Authors: | THOM HUPPERTZ MARY A SMIDDY |
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Affiliation: | Department of Food and Nutritional Sciences, University College Cork, Cork, Ireland,; NIZO Food Research, PO Box 20, 6710 BA, Ede, the Netherlands |
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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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Keywords: | Casein micelle High pressure Milk Transglutaminase |
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