<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Adjonu R</submitter><funding>Charles Sturt University Higher Degree by Research scholarship</funding><pagination>1812</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9222674</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>11(12)</volume><pubmed_abstract>Whey protein isolate (WPI)-derived bioactive peptide fractions (1-3, 3-5, 5-10, 1-10, and &amp;gt;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 &amp;lt;10 kDa fractions were either poorly surface-active or weak stabilizers in nanoemulsions. The moderately bioactive &amp;gt;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) temperat</pubmed_abstract><journal>Foods (Basel, Switzerland)</journal><pubmed_title>Whey Protein Peptides Have Dual Functions: Bioactivity and Emulsifiers in Oil-In-Water Nanoemulsion.</pubmed_title><pmcid>PMC9222674</pmcid><funding_grant_id>IPRS, CSUPRS and Writing Up Award</funding_grant_id><pubmed_authors>Sampson GO</pubmed_authors><pubmed_authors>Agboola SO</pubmed_authors><pubmed_authors>Torley P</pubmed_authors><pubmed_authors>Adjonu R</pubmed_authors><pubmed_authors>Doran GS</pubmed_authors></additional><is_claimable>false</is_claimable><name>Whey Protein Peptides Have Dual Functions: Bioactivity and Emulsifiers in Oil-In-Water Nanoemulsion.</name><description>Whey protein isolate (WPI)-derived bioactive peptide fractions (1-3, 3-5, 5-10, 1-10, and &amp;gt;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 &amp;lt;10 kDa fractions were either poorly surface-active or weak stabilizers in nanoemulsions. The moderately bioactive &amp;gt;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) temperat</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Jun</publication><modification>2025-04-19T07:08:57.582Z</modification><creation>2025-02-19T03:22:29.407Z</creation></dates><accession>S-EPMC9222674</accession><cross_references><pubmed>35742010</pubmed><doi>10.3390/foods11121812</doi></cross_references></HashMap>