Characterization of high-pressure-treated egg albumen.
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.
Iametti
S
S
Dipartimento di Scienze Molecolari Agroalimentari and Centro Interuniversitario per lo Studio delle Macromolecole Informazionali, University of Milan, Via Celoria 2, I-20133 Milan, Italy.
Donnizzelli
E
E
Pittia
P
P
Rovere
P P
PP
Squarcina
N
N
Bonomi
F
F
D000818:Animals; D002645:Chickens; D004529:Egg White; D004531:Eggs / Q000382:microbiology; D013293:Enterococcus faecalis / Q000302:isolation & purification; D004926:Escherichia coli / Q000302:isolation & purification; D010047:Ovalbumin / Q000737:chemistry*; D011312:Pressure; D011489:Protein Denaturation; D013211:Staphylococcus aureus / Q000302:isolation & purification; D014357:Trypsin / Q000378:metabolism; D014783:Viscosity
D010047:Ovalbumin; D014357:Trypsin