Quantitative N-glycoproteomic analyses provide insights into the effects of thermal processes on egg white functional properties

Food Chem. 2021 Apr 16:342:128252. doi: 10.1016/j.foodchem.2020.128252. Epub 2020 Oct 8.

Abstract

This study tries to elucidate the different mechanisms of functional properties among pasteurized egg white (P-EW), spray-dried egg white (SD-EW) and fresh egg white (F-EW) via quantitative N-glycoproteomic analyses. The results showed that spray-drying increased the surface hydrophobicity (181.4%) and zeta potential (25.6%) of egg white, which contributed to the enhancement of emulsifying activity index (20.1%) and foaming capacity (35.2%). Pasteurization caused the disintegration of natural protein aggregates in F-EW and resulted in a "block-like" P-EW gel and higher water holding capacity (6.2%). Spray-drying caused formation of thermal aggregates and led to a "mesh-like" SD-EW gel and better cohesiveness (3.6%). Quantitative N-glycoproteomic analysis showed that the abundance of 32 N-glycosites from 18 N-glycoproteins (such as Mucin 5B) of SD-EW was significantly reduced comparing to F-EW, indicated that the N-glycans of egg white protein are likely to be covalently cross-linked during spray-drying and are involved in thermal aggregation.

Keywords: Egg white; Functional properties; N-glycosylation; Pasteurization; Spray-drying.

MeSH terms

  • Desiccation
  • Egg Proteins / metabolism*
  • Glycoproteins / metabolism*
  • Pasteurization
  • Proteomics*
  • Temperature*
  • Water / metabolism

Substances

  • Egg Proteins
  • Glycoproteins
  • Water