TY - JOUR
T1 - Whey Protein Peptides have dual functions
T2 - Bioactivity and emulsifiers in oil-in-water nanoemulsion
AU - Adjonu, Randy
AU - Doran, Gregory S.
AU - Torley, Peter
AU - Sampson, Gilbert O.
AU - Agboola, Samson O.
N1 - Funding Information:
Funding: Author, Randy Adjonu, was a recipient of the Charles Sturt University International Postgraduate Research Scholarship, Charles Sturt University Tri-Faculty Open Access Publishing Scheme and the Graham Centre for Agricultural Innovations Writing Up Award. These funding sources supported this research and publication.
Funding Information:
Acknowledgments: The authors would like to acknowledge the support of the Gulbali Institute that was formed in 2022 by the merger of the Graham Centre for Agricultural Innovations, the Institute for Land and Water Society (ILWS), and the National Wine and Grape Industry Centre (NWGIC) at Charles Sturt University. Unfortunately, Samson Agboola, who contributed significantly to this work, passed away before this paper was submitted. He is deeply missed.
Publisher Copyright:
© 2022 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2022/6/20
Y1 - 2022/6/20
N2 - 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.
AB - 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.
KW - Bioactive peptide
KW - Droplet size
KW - Nanoemulsions
KW - Storage stability
KW - Ultrafiltration
KW - Zeta potential
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U2 - 10.3390/foods11121812
DO - 10.3390/foods11121812
M3 - Article
C2 - 35742010
AN - SCOPUS:85132918683
SN - 2304-8158
VL - 11
JO - Foods
JF - Foods
IS - 12
M1 - 1812
ER -