Glycation of soy proteins leads to a range of fractions with various supramolecular assemblies and surface activities

Jilu Feng, Claire C. Berton-Carabin, Burçe Ataç Mogol, Karin Schroën, Vincenzo Fogliano*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

1 Citation (Scopus)

Abstract

Dry and subsequent wet heating were used to glycate soy proteins with dextran or glucose, followed by fractionation based on size and solubility. Dry heating led to protein glycation (formation of furosine, Nε-(carboxymethyl)-L-lysine, Nε-(carboxyethyl)-L-lysine, and protein-bound carbonyls) and aggregation (increased particle size); while subsequent wet heating induced partial unfolding and de-aggregation. The measurable free amino group content of soy proteins changed from 0.77 to 0.14, then to 0.62 mmol/g upon dry and subsequent wet heating; this non-monotonic evolution is probably due to protein structural changes, and shows that this content should be interpreted with caution as a glycation marker. After both heating steps, the smaller-sized water-soluble fractions showed higher surface activity than the larger insoluble ones, and dextran conjugates exhibited a higher surface activity than their glucose counterparts. We thereby achieved a comprehensive understanding of the properties of various fractions in plant protein fractions, which is essential when targeting applications.

Original languageEnglish
Article number128556
JournalFood Chemistry
DOIs
Publication statusE-pub ahead of print - 5 Nov 2020

Keywords

  • Furosine
  • Interfacial tension
  • Nε-(carboxymethyl)--lysine (CML)
  • Protein glycation
  • Protein oxidation
  • Protein-carbohydrate conjugates
  • Soy protein isolate

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