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Foaming characteristics of oat protein and modification by partial hydrolysis

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Abstract

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.

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Acknowledgements

The project is part of the ERA-NET SUSFOOD “OATPRO, Engineering of oat proteins: Consumer driven sustainable food development process”. The authors thank the Federal Ministry of Education and Research (BMBF), Germany Projektträger Jülich for the financial support (project no. 031A661). The authors acknowledge Cornelia Rauh and Daniel Baier for assistance in foaming experiments.

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Authors and Affiliations

  1. Food Technology and Food Material Science, Technische Universität Berlin, Königin-Luise-Strasse 22, 14195, Berlin, Germany

    Monika Brückner-Gühmann, Theresia Heiden-Hecht & Stephan Drusch

  2. VTT Technical Research Centre of Finland Ltd., P.O. Box 1000, 02044, Espoo, Finland

    Nesli Sözer

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  1. Monika Brückner-Gühmann
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Brückner-Gühmann, M., Heiden-Hecht, T., Sözer, N. et al. Foaming characteristics of oat protein and modification by partial hydrolysis. Eur Food Res Technol 244, 2095–2106 (2018). https://doi.org/10.1007/s00217-018-3118-0

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