The relationship between acylation degree and gelling property of NaOH-induced egg white gel: Efficient is better?

Abstract

In this study, succinic anhydride (SA) and octenyl succinic anhydride (OSA) were used to modify the egg white protein (EWP), and acylated EWP was further prepared as a gel by adding NaOH and heat modification. The results showed that the acylation degree for the SA- and OSA-added groups reached 57.68% and 26.95%, respectively, and the average size, the absolute value of ζ-potential, increased significantly with SA and OSA addition, indicating that acylation improved the stability of EWP solution. Furthermore, the surface hydrophobicity increased for the SA-added group while decreasing for the OSA-added group, and the acylation process exposed the flexibility part of the protein molecule. Acylated EWP prepared gel (EWG) showed a translucent and slightly yellow appearance (except for the sol state of the OSA-added 1:50 group), the gel strength, water-holding capacity and rheological properties for SA-added EWG were remarkably reduced while OSA-added EWG improved apparently. Intermolecular forces analysis indicated that the addition of SA promoted the formation of disulfide bonds and strengthened proteins interactions while adding OSA weakened the interactions. Microstructural observations revealed a rougher gel network structure and weaker protein cross-linking in the gel prepared after the acylation of proteins. However, the high efficiency of SA and promotion of protein-molecule interactions were unable to counteract the negative effect of SA on the extension of the gel network structure, and the interaction between OSA expanded the formation of the gel network structure.