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

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, N epsilon-(carboxymethyl)-L-lysine, N epsilon-(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 watersoluble 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.

Automated summary

Dry and subsequent wet heating were used to glycate soy proteins with dextran or glucose, leading to changes in protein structure and measurable free amino group content. Smaller-sized water-soluble fractions exhibited higher surface activity, which is essential for targeted applications.