Relating the variation of secondary structure of gelatin at fish oil-water interface to adsorption kinetics, dynamic interfacial tension and emulsion stability

Journal article


Liu, Huihua, Wang, Bo, Barrow, Colin J. and Adhikari, Benu. (2014). Relating the variation of secondary structure of gelatin at fish oil-water interface to adsorption kinetics, dynamic interfacial tension and emulsion stability. Food Chemistry. 143, pp. 484-491. https://doi.org/10.1016/j.foodchem.2013.07.130
AuthorsLiu, Huihua, Wang, Bo, Barrow, Colin J. and Adhikari, Benu
Abstract

The objectives of this study were to quantify the relationship between secondary structure of gelatin and its adsorption at the fish-oil/water interface and to quantify the implication of the adsorption on the dynamic interfacial tension (DST) and emulsion stability. The surface hydrophobicity of the gelatin solutions decreased when the pH increased from 4.0 to 6.0, while opposite tend was observed in the viscosity of the solution. The DST values decreased as the pH increased from 4.0 to 6.0, indicating that higher positive charges (measured trough zeta potential) in the gelatin solution tended to result in higher DST values. The adsorption kinetics of the gelatin solution was examined through the calculated diffusion coefficients (Deff). The addition of acid promoted the random coil and β-turn structures at the expense of α-helical structure. The addition of NaOH decreased the β-turn and increased the α-helix and random coil. The decrease in the random coil and triple helix structures in the gelatin solution resulted into increased Deff values. The highest diffusion coefficients, the highest emulsion stability and the lowest amount of random coil and triple helix structures were observed at pH = 4.8. The lowest amount of random coil and triple helix structures in the interfacial protein layer correlated with the highest stability of the emulsion (highest ESI value). The lower amount of random coil and triple helix structures allowed higher coverage of the oil–water interface by relatively highly ordered secondary structure of gelatin.

Keywordsgelatin; protein adsorption kinetics; interfacial tension; emulsion stability; zeta potential
Year2014
JournalFood Chemistry
Journal citation143, pp. 484-491
PublisherElsevier Ltd
ISSN0308-8146
Digital Object Identifier (DOI)https://doi.org/10.1016/j.foodchem.2013.07.130
Scopus EID2-s2.0-84883170760
Research or scholarlyResearch
Page range484-491
Publisher's version
License
All rights reserved
File Access Level
Controlled
Output statusPublished
Publication dates
Online08 Aug 2013
Publication process dates
Accepted29 Jul 2013
Deposited17 Aug 2021
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