The interaction of milk sphingomyelin and proteins on stability and microstructure of dairy emulsions
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...
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| Format: | Article |
| Language: | English |
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Elsevier
2022-05-01
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| Series: | Journal of Dairy Science |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022030222001473 |
| _version_ | 1828466148528619520 |
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| author | Nahyun Ahn Ji-Hwa Park Changhoon Chai Jee-Young Imm |
| author_facet | Nahyun Ahn Ji-Hwa Park Changhoon Chai Jee-Young Imm |
| author_sort | Nahyun Ahn |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-11T03:44:49Z |
| format | Article |
| id | doaj.art-ffbf9b765a3e4d9faed2580dd1660634 |
| institution | Directory Open Access Journal |
| issn | 0022-0302 |
| language | English |
| last_indexed | 2024-12-11T03:44:49Z |
| publishDate | 2022-05-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Dairy Science |
| spelling | doaj.art-ffbf9b765a3e4d9faed2580dd16606342022-12-22T01:22:03ZengElsevierJournal of Dairy Science0022-03022022-05-01105538323845The interaction of milk sphingomyelin and proteins on stability and microstructure of dairy emulsionsNahyun Ahn0Ji-Hwa Park1Changhoon Chai2Jee-Young Imm3Department of Interdisciplinary Program for Bio-health Convergence, Kookmin University, Seoul, 02707, KoreaDepartment of Foods and Nutrition, Kookmin University, Seoul, 02707, KoreaDepartment of Applied Animal Science, Kangwon National University, Chuncheon 24341, KoreaDepartment of Interdisciplinary Program for Bio-health Convergence, Kookmin University, Seoul, 02707, Korea; Department of Foods and Nutrition, Kookmin University, Seoul, 02707, Korea; Corresponding authorABSTRACT: 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.http://www.sciencedirect.com/science/article/pii/S0022030222001473oil-in-water emulsionemulsion stabilityprotein sphingomyelin-phosphatidylcholine combinationprotein surface loadmicrostructure |
| spellingShingle | Nahyun Ahn Ji-Hwa Park Changhoon Chai Jee-Young Imm The interaction of milk sphingomyelin and proteins on stability and microstructure of dairy emulsions Journal of Dairy Science oil-in-water emulsion emulsion stability protein sphingomyelin-phosphatidylcholine combination protein surface load microstructure |
| title | The interaction of milk sphingomyelin and proteins on stability and microstructure of dairy emulsions |
| title_full | The interaction of milk sphingomyelin and proteins on stability and microstructure of dairy emulsions |
| title_fullStr | The interaction of milk sphingomyelin and proteins on stability and microstructure of dairy emulsions |
| title_full_unstemmed | The interaction of milk sphingomyelin and proteins on stability and microstructure of dairy emulsions |
| title_short | The interaction of milk sphingomyelin and proteins on stability and microstructure of dairy emulsions |
| title_sort | interaction of milk sphingomyelin and proteins on stability and microstructure of dairy emulsions |
| topic | oil-in-water emulsion emulsion stability protein sphingomyelin-phosphatidylcholine combination protein surface load microstructure |
| url | http://www.sciencedirect.com/science/article/pii/S0022030222001473 |
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