Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2087111 | Innovative Food Science & Emerging Technologies | 2013 | 9 Pages |
The effect of high pressure treatment on whole egg white was examined using in vitro pepsin digestion and proteomic methods. Pepsin incubations conducted with an enzyme to protein ratio of 3:1 following high pressure treatment (400–800 MPa and 9 °C) resulted in increased hydrolysis of egg white proteins. Pressure treatment of egg white at 800 MPa resulted in greater susceptibility to pepsin hydrolysis than did thermal treatment at 95 °C. The effect of 800 MPa pressure treatment on egg white proteins was additionally examined by incubation with pepsin at an enzyme to protein ratio of 1:20 followed by 2-D electrophoresis. Results of these experiments showed extensive hydrolysis of most egg white proteins. Subsequent LC-MS/MS investigation of the low Mr fraction (< 3.0 kDa) derived from pepsin digested 800 MPa treated egg white contained numerous peptides previously shown to have bioactive and/or immunological properties.Industrial RelevanceShort time high pressure treatment of whole egg white at relatively low temperature (9 °C) resulted in increased pepsin digestibility equivalent to or better than heat treatment at 95 °C. Examination of the peptides resulting from high pressure treatment and pepsin digestion revealed sequences with known biological activities. Thus high pressure treatment represents a promising technology for enhancing egg white's healthiness and contributing to its role as a functional food.
► Greater pepsin digestibility compared to thermal treatment ► Extensive protein hydrolysis by pepsin ► Bioactive and immunologically important peptide products