Journal
FOOD CHEMISTRY
Volume 211, Issue -, Pages 235-242Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2016.05.062
Keywords
Pea protein; Protein-flavour binding; Molecular forces; Flavour retention and release
Funding
- Natural Science and Engineering Research Council of Canada (NSERC - Canada)
- University of Manitoba Faculty of Graduate Studies
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Molecular interactions between heterologous classes of flavour compounds with salt-extracted pea protein isolates (PPIs) were determined using various bond disrupting agents followed by GC/MS analysis. Flavour bound by proteins decreased in the order: dibutyl disulfide > octanal > hexyl acetate > 2-octanone = benzaldehyde. Benzaldehyde, 2-octanone and hexyl acetate interacted non-covalently with PPIs, whereas octanal bound PPIs via covalent and non-covalent forces. Dibutyl disulfide reacted with PPIs covalently, as its retention was not diminished by urea and guanidine hydrochloride. Using propylene glycol, H-bonding and ionic interactions were implicated for hexyl acetate, benzaldehyde, and 2-octanone. A protein -destabilising salt (Cl3CCOONa) reduced bindings for 2-octanone, hexyl acetate, and benzaldehyde; however, retention for octanal and dibutyl disulfide increased. Conversely, a protein stabilising salt (Na2SO4) enhanced retention for benzaldehyde, 2-octanone, hexyl acetate and octanal. Formation of a volatile flavour by-product, 1-butanethiol, from dibutyl disulfide when PPIs were treated with dithiothreitol indicated occurrence of sulfhydryl-disulfide interchange reactions. (C) 2016 Elsevier Ltd. All rights reserved.
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