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Main Title: Partitioning behavior and interfacial activity of phenolic acid derivatives and their impact on β-Lactoglobulin at the oil-water interface
Author(s): Bock, Alina
Steinhäuser, Ulrike
Drusch, Stephan
Type: Article
Language Code: en
Abstract: Proteins are able to stabilize dispersed food systems due to their amphiphilic nature, acting as emulsifiers. Their interfacial properties can be influenced by different methods, including the formation of protein-phenol nanocomplexes. In this study, the interfacial behavior of phenolic compounds and protein-phenol nanocomplexes was first characterized according to the oil-water partitioning behavior of phenolic acid derivatives according to their molecular structure and its impact on interfacial tension. The influence of the phenolic compounds on protein film formation and its properties by dilatational rheology was then evaluated. The most phenolic acid derivatives are predominantly present in the aqueous phase. Despite their hydrophobic benzene body, weak interfacial activity was observed depending on their chemical structure. This result supports possible protein-phenol nanocomplex formation in the aqueous phase and possible interactions at the oil-water interface. Protein-phenol nanocomplexes showed decreased interfacial adsorption properties and decreased viscoelastic interfacial behavior, depending on the expansion of the delocalized π-electrons in the phenol.
Issue Date: 4-Jan-2021
Date Available: 18-Mar-2021
DDC Class: 540 Chemie und zugeordnete Wissenschaften
Subject(s): dilatational rheology
interfacial tension
phenolic acid derivatives
Sponsor/Funder: TU Berlin, Open-Access-Mittel – 2020
Journal Title: Food Biophysics
Publisher: SpringerNature
Publisher Place: London [u.a.]
Publisher DOI: 10.1007/s11483-020-09663-7
EISSN: 1557-1866
ISSN: 1557-1858
Appears in Collections:FG Lebensmittelchemie und Analytik » Publications

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