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Protein-protein interactions of a whey-pea protein co-precipitate

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DOI

The aim of this study was to investigate the mechanisms behind protein-protein interactions in a co-precipitate of whey protein isolate (WPI) and pea protein isolate (PPI). A co-precipitate and blend, consisting of 80% WPI and 20% PPI, were compared. Covalent disulphide interactions were studied by blocking of free thiols with N-Ethylmaleimide (NEM), while electrostatic interactions were studied in systems with 0.5 m NaCl and hydrophobic interactions with 0.2% SDS. Protein solubility, stability and secondary, tertiary and quaternary protein structures were analysed. Co-precipitation did not introduce different protein-protein interactions than the direct blending of proteins. SDS affected solubility (P < 0.05), secondary and tertiary structure. However, the effects of NEM and NaCl were significant greater (P < 0.05) on the same parameters and thermal stability, especially when combined (P < 0.01). Thus, the protein-protein interactions in a whey-pea co-precipitate and protein blend consisted of disulphide bonds and electrostatic interactions.

Original languageEnglish
JournalInternational Journal of Food Science and Technology
Number of pages14
ISSN0950-5423
DOIs
Publication statusE-pub ahead of print - Jun 2021

    Research areas

  • co-precipitates, pea protein isolate, Pisum sativum L, protein-protein interactions, whey protein isolate, SODIUM DODECYL-SULFATE, BETA-LACTOGLOBULIN-A, ALPHA-LACTALBUMIN, THERMAL-STABILITY, SECONDARY STRUCTURE, N-ETHYLMALEIMIDE, MILK, AGGREGATION, MECHANISMS, ISOLATE

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