Succinylation Improves the Thermal Stability of Egg White Proteins

Molecules

Ying Lv¹  Dabo He¹  Qigen Tong¹ 

[1] College of Food Science and Engineering, Beijing University of Agriculture, 7 Beinong Lu, Changping District, Beijing 102206, China;

关键词: egg white protein;    succinylation;    thermal stability;    conformational structure;    aggregation;   

DOI  :  10.3390/molecules24203783

来源: DOAJ

【 摘 要 】

Succinylation can improve the thermal stability of various proteins. In this study, succinylated egg white protein (SEWP) samples with different succinylation degrees were prepared by adding various succinic anhydride additives to egg white protein (EWP). The thermal stability of SEWP and the conformational structure under various succinylation degrees were investigated. With the increase in succinylation degree, the turbidity of heated SEWP solution (90 °C for 30 min) markedly declined. The heated SEWP solution with high succinylation degree (37.63%, 66.57%, and 72.37%) was transparent. Moreover, the result of differential scanning calorimetry confirmed that the thermal stability of succinylated EWP increased. The results of intrinsic fluorescence spectra and Fourier-transform infrared spectroscopy illustrate that succinylation changed the conformational structure of EWP. Succinylation increased the electrostatic repulsion and decreased the surface hydrophobicity, and it changed the aggregation morphology of EWP. Cross-linked spherical aggregates of low succinylation degree transformed to thready aggregates of a high succinylation degree. Thus, succinylation improved the thermal stability of EWP.

【 授权许可】

Unknown