Addition of NaCl or sucrose to egg albumen prior to high-pressure treatment (up to 10 min at 800 MPa) prevented insolubilization or gel formation after pressure treatment. As a consequence of protein unfolding, the treated albumen had increased viscosity but retained its foaming and heat-gelling properties. Susceptibility of egg albumen proteins to hydrolysis by trypsin increased dramatically after pressure treatment. The S-form of ovalbumin, the presence of which is an index of egg aging, was not found in any of the pressure-treated samples, which also did not display evidence for covalent protein aggregation. However, recognition of ovalbumin by an anti- ovalbumin antiserum was reduced to 40% of that of untreated sample.
Characterization of high-pressure-treated egg albumen / S. Iametti, E. Donnizzelli, P. Pittia, P.P. Rovere, N. Squarcina, F. Bonomi. - In: JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY. - ISSN 0021-8561. - 47:9(1999 Sep), pp. 3611-3616.
Characterization of high-pressure-treated egg albumen
S. Iametti;F. Bonomi
1999
Abstract
Addition of NaCl or sucrose to egg albumen prior to high-pressure treatment (up to 10 min at 800 MPa) prevented insolubilization or gel formation after pressure treatment. As a consequence of protein unfolding, the treated albumen had increased viscosity but retained its foaming and heat-gelling properties. Susceptibility of egg albumen proteins to hydrolysis by trypsin increased dramatically after pressure treatment. The S-form of ovalbumin, the presence of which is an index of egg aging, was not found in any of the pressure-treated samples, which also did not display evidence for covalent protein aggregation. However, recognition of ovalbumin by an anti- ovalbumin antiserum was reduced to 40% of that of untreated sample.File | Dimensione | Formato | |
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