Succinylation Improves the Thermal Stability of Egg White Proteins.

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ID: 63635
2019
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Abstract
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.
Reference Key
he2019succinylationmolecules Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors He, Dabo;Lv, Ying;Tong, Qigen;
Journal molecules
Year 2019
DOI
E3783
URL
Keywords
thermal stability aggregation conformational structure egg white protein succinylation

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