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Desirable characteristics of casein peptides with simultaneously enhanced emulsion forming ability and antioxidative capacity in O/W emulsion.
- Source :
-
Food Hydrocolloids . Oct2022, Vol. 131, pN.PAG-N.PAG. 1p. - Publication Year :
- 2022
-
Abstract
- This study aimed to explore the desirable characteristics of casein hydrolysates with simultaneously enhanced emulsion forming and antioxidative ability in oil-in-water (O/W) emulsion. Effects of physicochemical properties of casein hydrolysates prepared by trypsin, alcalase, and neutrase on physical and oxidative stability of O/W emulsion were studied, and potential antioxidant peptides were characterized by UPLC-MS/MS and bioinformatics analysis. Results showed that casein hydrolysates at a lower degree of hydrolysis (DH) produced by trypsin displayed higher zeta potential absolute values (−31.7 mV), smaller particle size (170.75 nm) and improved antioxidant properties compared to alcalase and neutrase, and could form more stable emulsion with d 4,3 of 0.39–0.41 μm at a broader range of DH. Additionally, compared with sodium caseinate (NaCas), the oxidation of emulsion was significantly retarded during the storage progress prepared by the trypsin hydrolysates at DH of 4.49% alone or with Tween 20. Peptidomics indicated that the trypsin hydrolysates contained more peptides with basic amino acids at C-terminal and aromatic amino acids at N-terminus, which exhibited cationic amphiphilic properties with grand average of hydrophilicity values (GRAVY) of −0.5 ∼ +0.5 and pI > pH 7.0. This could contribute to their better emulsion formation and inhibition of lipid oxidation ability by producing dense interfacial layers with peptides interactions or excluding metal ions in O/W emulsions. These results suggested that casein hydrolysates at lower DH prepared by trypsin owned potential amphiphilic antioxidant peptides, which were desired to enhance the stability and functional activity of O/W emulsion. [Display omitted] • Trypsin hydrolysates featured specificity in zeta value and particle size at low DH. • Casein hydrolysates exhibited better emulsion formation ability at low DH. • Trypsin hydrolysates at low DH effectively retarded lipid oxidation. • More cationic amphiphilic peptides were observed in trypsin hydrolysates. [ABSTRACT FROM AUTHOR]
- Subjects :
- *CASEINS
*TRYPSIN
*PEPTIDES
*EMULSIONS
*SODIUM caseinate
*Z bosons
*ZETA potential
Subjects
Details
- Language :
- English
- ISSN :
- 0268005X
- Volume :
- 131
- Database :
- Academic Search Index
- Journal :
- Food Hydrocolloids
- Publication Type :
- Academic Journal
- Accession number :
- 157524820
- Full Text :
- https://doi.org/10.1016/j.foodhyd.2022.107812