Proteomic characterisation of hydrothermal redox damage

Abstract

Peptide and protein damage contributes to the loss of quality and value in protein-based food and textile products as well as to the degeneration of biological tissues such as hair and skin. The effects of elevated temperature on such substrates at the molecular level are, however, relatively unknown. This paper examines the response of peptides and proteins to hydrothermal damage using mass spectrometry and reports the location of molecular markers of hydrothermal damage within wool proteins. The hydrothermal exposure of model peptides containing the oxidatively sensitive residues tryptophan and tyrosine revealed the formation of a number of products such as hydroxytryptophan and dihydrophenylalanine. A variety of degradation products were also observed in intermediate filament proteins, including products arising from deamidation and from oxidation of histidine, tyrosine and tryptophan residues. The products observed to form during hydrothermal exposure indicated the involvement of reactive oxygen species. Molecular markers were identified within a proteinaceous system to allow the evaluation of damage type or severity. These findings have important implications for the thermal processing of foods and textiles.