Measured effect of encapsulation and freeze-drying on the structural organisation of β-Lactoglobulin–pectin complex coacervates with curcumin and folic acid
Year: 2025
Type: article
Abstract: Encapsulation systems based on protein-polysaccharide complex coacervates have important applications in the food industry. They deliver bioactives and impart desired structural and textural properties. In this study, complex coacervates composed of β-Lactoglobulin (βLg) and pectin at a molar ratio of 20:1, pH 4, and ionic strength of 20 mM encapsulated two bioactive molecules, curcumin and folic acid. The bioactives were bound to βLg A (1:1 M ratio) prior to forming the complex coacervates with pectin. The complex coacervates were freeze-dried to show the impact of this common preparation method for sensitive bioactives on the physicochemical properties and structure of the complex coacervates. Small and ultra-small angle neutron scattering give the complex coacervate structure on multi-length scales ranging from the primary particles of 100 nm to the fractal network of 10 μm. Our work shows that the hierarchical structures formed by the complex coacervates are preserved both on encapsulation and freeze-drying.
Source: Food Chemistry
Authors: Sunandita Ghosh, Laurence D. Melton, Shinji Kihara, Amy Y. Xu, Jitendra Mata, Andrew E. Whitten, Agata Rekas, Duncan J. McGillivray
Institutions: University of Auckland, Victoria University of Wellington, Riddet Institute, Massey University, MacDiarmid Institute for Advanced Materials and Nanotechnology, University of Copenhagen, Louisiana State University, National Institute of Standards and Technology, NIST Center for Neutron Research, Australian Nuclear Science and Technology Organisation, UNSW Sydney, Australian Centre for Neutron Scattering, National Deuteration Facility
Language: English
Topic: Proteins in Food Systems
Subfield: Food Science
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $4,930
Awards: G377931325, G4801316472
OpenAlex ID: W4411399714