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Foaming characteristics of oat protein and modification by partial hydrolysis

Brückner-Gühmann, Monika, Heiden-Hecht, Theresia, Sözer, Nesli, Drusch, Stephan
European food research & technology 2018 v.244 no.12 pp. 2095-2106
foaming, foaming properties, food research, hydrolysis, hydrophobic bonding, ingredients, oat protein, pH, peptides, protein isolates, rheology, solubility, subtilisin, trypsin, viscoelasticity
Foaming ability of oat protein isolate (OPI) was analysed at pH 4 and 7. Foaming properties were influenced by partial hydrolysis with trypsin (OPT) and alcalase (OPA). The viscoelasticity of the protein film, the interactions between the protein molecules, and the network forming within the protein film were analysed by interfacial rheology. At pH 7, foams made of OPI and OPT were found to be stable with OPI showing the fastest foaming ability. At pH 4, the foaming properties of OPI were found to be poor due to limited solubility. The specific cleavage pattern of trypsin resulted in peptides with improved foaming properties, especially at pH 4, resulting in a homogenous foam structure, a fast foaming ability, and a highly viscoelastic interfacial film. The formation of a thick steric protein layer at pH 7 and the formation of strong hydrophobic interactions at pH 4 were found to be the dominating foam stabilisation mechanisms. In conclusion, oat protein may serve as a food ingredient with targeted functional properties.