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The interaction of milk sphingomyelin and proteins on stability and microstructure of dairy emulsions.
- Source :
-
Journal of dairy science [J Dairy Sci] 2022 May; Vol. 105 (5), pp. 3832-3845. Date of Electronic Publication: 2022 Mar 10. - Publication Year :
- 2022
-
Abstract
- The interaction between dairy proteins [micellar casein (MC) vs. whey protein isolate (WPI)] and phospholipids [PL; soy phosphatidylcholine (PC) vs. milk sphingomyelin (SM)] in an oil-in-water emulsion system was investigated. Sole PC-stabilized emulsion (1%, wt/vol) showed a significantly larger mean particle diameter (6.5 μm) than SM-stabilized emulsions (3.8 μm). The mean particle diameters of emulsions prepared by the combination of protein (1%, wt/vol) and PL (1%, wt/vol) did not significantly differ from the emulsions prepared with a single emulsifier (MC, WPI, and SM). Emulsion instability differed significantly among samples by a centrifugation-mediated accelerated stability test. Emulsion instability increased in the order of MC+SM < MC+PC, WPI+SM < WPI+PC < MC < SM < WPI < PC. Protein surface load determined by aqueous phase depletion was significantly decreased only in WPI+PC emulsion, whereas no significant difference was found between the MC+SM and WPI+SM emulsions. Topographic and phase images of emulsion surface by atomic force microscopy showed surface layers prepared by protein+PL combinations were composites with different mechanical properties, and PL formed a more compact domain than proteins. A smoother phase image was observed in MC+PL combinations than in WPI+PL counterparts. Based on the microstructure analysis using confocal laser scanning microscopy, combination and MC+SM formed a uniform and thick surface coating of fat droplets. More PC aggregates were observed in the emulsions containing PC (sole PC, MC+PC, and WPI+PC) compared with their SM counterparts. Based on these results, the appropriate selection of the PL matrix is important to modulate the emulsion stability of dairy emulsion products.<br /> (The Authors. Published by Elsevier Inc. and Fass Inc. on behalf of the American Dairy Science Association®. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).)
Details
- Language :
- English
- ISSN :
- 1525-3198
- Volume :
- 105
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Journal of dairy science
- Publication Type :
- Academic Journal
- Accession number :
- 35282910
- Full Text :
- https://doi.org/10.3168/jds.2021-21253