| dc.description |
Adjonu, R., School of Dentistry and Medical Science, Charles Sturt University, Wagga Wagga, NSW 2678, Australia, The Gulbali Institute, Charles Sturt University, Albert Pugsley Place, Wagga Wagga, NSW 2678, Australia; Doran, G.S., The Gulbali Institute, Charles Sturt University, Albert Pugsley Place, Wagga Wagga, NSW 2678, Australia, School of Agricultural, Environmental and Veterinary Sciences, Charles Sturt University, Wagga Wagga, NSW 2678, Australia; Torley, P., School of Science, RMIT University, Bundoora, VIC 3083, Australia; Sampson, G.O., Faculty of Vocational Education, University of Education Winneba, Kumasi Campus, P.O. Box 1277, Kumasi, Ghana; Agboola, S.O., The Gulbali Institute, Charles Sturt University, Albert Pugsley Place, Wagga Wagga, NSW 2678, Australia |
en_US |
| dc.description.abstract |
Whey protein isolate (WPI)-derived bioactive peptide fractions (1�3, 3�5, 5�10, 1�10, and >10 kDa) were for the first time used as emulsifiers in nanoemulsions. The formation and storage stability of WPI bioactive peptide-stabilized nanoemulsions depended on the peptide size, enzyme type, peptide concentration, and storage temperature. The highly bioactive <10 kDa fractions were either poorly surface-active or weak stabilizers in nanoemulsions. The moderately bioactive >10 kDa fractions formed stable nanoemulsions (diameter = 174�196 nm); however, their performance was dependent on the peptide concentration (1�4%) and enzyme type. Overall, nanoemulsions exhibited better storage stability (less droplet growth and creaming) when stored at lower (4 �C) than at higher (25 �C) temperatures. This study has shown that by optimizing peptide size using ultrafiltration, enzyme type and emulsification conditions (emulsifier concentration and storage conditions), stable nanoemulsions can be produced using WPI-derived bioactive peptides, demonstrating the dual-functionality of WPI peptides. � 2022 by the authors. Licensee MDPI, Basel, Switzerland. |
en_US |