Role of the N‑Terminal Amphiphilic Region of Ovalbumin during Heat-Induced Aggregation and Gelation

Abstract

Ovalbumin (OVA), a major globular protein in egg white, forms semiflexible fibrillar aggregates during heat-induced gelation. The N-terminal amphiphilic region (pN_1–22) of OVA is removed after treatment with pepsin at pH 4 to leave a large OVA fragment (pOVA). The conformation and thermal stability of pOVA and OVA are similar, but the rheological strength of the heat-induced gel of pOVA is much lower compared to that of OVA. The aggregation rate of pOVA, which forms spherical aggregates, was lower than that of OVA. These results suggest that the N-terminal amphiphilic region of OVA facilitates the α-to-β conformational transition, which triggers OVA fibril formation. Heat treatment of OVA in the presence of pN_1–22 consistently resulted in the formation of straight fibrils. The strength of OVA and collagen gels was increased when prepared in the presence of pN_1–22, suggesting that pN_1–22 may be used to control the properties of protein gels