Effect of Temperature and Time of Storage on Protein Stability and Anti-Salmonella Activity of Egg White

Author:

REHAULT-GODBERT SOPHIE1,BARON FLORENCE2,MIGNON-GRASTEAU SANDRINE3,LABAS VALERIE4,GAUTIER MICHEL2,HINCKE MAXWELL T.5,NYS YVES1

Affiliation:

1. 1INRA, UR83 Recherches Avicoles, Fonction et Régulation des Protéines de l'Oeuf, F-37380 Nouzilly, France

2. 2UMR1253 Science et Technologie du Lait et de l'œuf, Agrocampus Ouest-centre de Rennes/INRA,Équipe d'hygiène alimentaire, 65 rue de Saint Brieuc, F-35042 Rennes, France

3. 3INRA, UR83 Recherches Avicoles, Génétique Avicole, F-37380 Nouzilly, France

4. 4INRA, UMR85 Physiologie de la Reproduction et des Comportements, Plate-forme d'Analyse Intégrative des Biomarqueurs, Laboratoire de Spectrométrie de Masse, F-37380 Nouzilly, France

5. 5Department of Cellular & Molecular Medicine, University of Ottawa, 451 Smyth Road, Ottawa, Ontario, Canada K1H 8M5

Abstract

Hen egg white contains numerous molecules of interest for human health, including antimicrobial proteins. Little information is available concerning changes in the antimicrobial activity of egg white during storage; therefore, we analyzed the potential of egg white to inhibit growth of Salmonella enterica serovar Enteritidis following storage at 4, 20, or 37°C for 30 days prior to inoculation. Egg white displayed higher anti-Salmonella activity after a few days of storage at 20 and 37°C. The rate of increase in activity was more rapid and pronounced at the higher temperature. However, egg white stored at 20°C retained higher antimicrobial activity than that of egg white stored at 4 or 37°C, when the entire storage period is taken in consideration. In contrast, storage of egg at 37°C for more than 14 days reduced the bacteriostatic potential of egg white. Statistical analyses revealed a correlation between pH and the antimicrobial activity of egg white. Moreover, diminished antimicrobial activity was associated with degradation of ovalbumin and ovotransferrin, as assessed by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and mass spectrometry. However, the fluctuation in anti-Salmonella activity of egg white could not be related to any variation of trypsin-like, chymotrypsin-like, or gelatinolytic activities that potentially account for degradation of antimicrobial egg white proteins.

Publisher

International Association for Food Protection

Subject

Microbiology,Food Science

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