Original papers
Effects of Lanthionine and Lysinoalanine on Heat-induced Gelation of Egg White
2020 年 26 巻 6 号 p. 789-795
詳細
2020 年 26 巻 6 号 p. 789-795
Egg white gelation is caused by protein unfolding and aggregation. Intermolecular disulfide bonds have been reported to contribute significantly to the formation and strengthening of gel networks. The covalent crosslinks lanthionine and lysinoalanine, which are collectively known as isopeptide bonds, are also generated in heated egg white proteins. However, little is known regarding the relationship between the isopeptide bonds and the gel properties. Here, we investigated the effect of isopeptide bonds produced during the heating of egg white on the protein aggregation and gel texture. Egg white proteins formed isopeptide bonds, and the number of the bonds increased with increasing temperature. These were mainly composed of lanthionine, which were easily formed in ovotransferrin and lysozyme. A significant correlation coefficient of 0.99 was found between the gel hardness and lanthionine content. These results suggested that lanthionine hardens the egg white gel through strengthening intermolecular crosslinks, resulting in network fortification.
