Impact of Spray Drying and Fluidized Bed Drying on Whey Protein Phospholipid Concentrate: Microstructural Analysis, Bioactivity, and Functionality

Whey protein phospholipid concentrate (WPPC) is a valuable coproduct of whey protein isolate that represents a rich source of bioactive compounds with potential health-promoting benefits. Powdered forms of dairy ingredients are highly valued for their convenience and extended shelf life. However, drying is a crucial process that can affect microstructure, bioactivity, and physicochemical properties. This study investigated the effect of 2 drying methods, spray drying (SD) and fluidized bed drying (FBD), on the properties of SD-WPPC and FBD-WPPC, respectively, with an industry-scale spray-dried WPPC (I-SDWPPC) also included as a control to represent scaled-up production. After rehydration, FBD-WPPC exhibited a particle size (2.22 µm) comparable to SD-WPPC (1.72 µm) and I-SD WPPC (2.72 µm) and the mean milk fat globule diameters did not differ substantially among FBD-WPPC (10.93 µm), SD-WPPC (11.51 µm), and I-SD WPPC (11.29 µm). Furthermore, confocal laser scanning microscopy revealed larger aggregates of protein and fat in the SD-WPPC and I-SD WPPC, whereas FBD-WPPC showed a more uniform protein distribution with distinct fat clusters. FTIR analysis indicated that FBD-WPPC retained the most native-like protein secondary structure, SD-WPPC displayed moderate structural changes, and I-SD WPPC exhibited the most pronounced alterations, with decreased α-helix and random coil contents and increased β-sheet and β-turn contributions. Xanthine oxidase activity normalized to protein content was significantly higher in FBD-WPPC than in both spray-dried powders, which did not differ from one another, demonstrating the influence of drying method on MFGM-enzyme stability. Protein oxidation, as measured by carbonyl content, was determined to be the lowest in I-SD WPPC but significantly not different among samples. Both primary (lipid hydroperoxides; LOOH) and secondary (TBARS) lipid oxidation products showed no significant differences among FBD-WPPC, SD-WPPC, and I-SD WPPC. Overall, these results provide new insight into how different drying methods and processing scales influence the microstructure and physicochemical properties of WPPC, informing future development of functional dairy coproduct powders.

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Journal
Journal of Dairy Science
Published
2026-04-01
DOI
https://doi.org/10.3168/jds.2025-27557
Primary Topic
Microencapsulation and Drying Processes
Type
article
Field-Weighted Citation Impact
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article

Impact of Spray Drying and Fluidized Bed Drying on Whey Protein Phospholipid Concentrate: Microstructural Analysis, Bioactivity, and Functionality

Fatemeh Jalil Mozhdehi, Audrey L. Girard, Mark P. Richards, Rachel B. Dietrich et al.
Journal of Dairy Science
Microencapsulation and Drying Processes
article

Impact of Spray Drying and Fluidized Bed Drying on Whey Protein Phospholipid Concentrate: Microstructural Analysis, Bioactivity, and Functionality

Fatemeh Jalil Mozhdehi, Audrey L. Girard, Mark P. Richards, Rachel B. Dietrich, Jerina Rugji, Mitchel T. Armstrong, Sean Baker, Rebecca J. Goodman
article en

Abstract

Whey protein phospholipid concentrate (WPPC) is a valuable coproduct of whey protein isolate that represents a rich source of bioactive compounds with potential health-promoting benefits. Powdered forms of dairy ingredients are highly valued for their convenience and extended shelf life. However, drying is a crucial process that can affect microstructure, bioactivity, and physicochemical properties. This study investigated the effect of 2 drying methods, spray drying (SD) and fluidized bed drying (FBD), on the properties of SD-WPPC and FBD-WPPC, respectively, with an industry-scale spray-dried WPPC (I-SDWPPC) also included as a control to represent scaled-up production. After rehydration, FBD-WPPC exhibited a particle size (2.22 µm) comparable to SD-WPPC (1.72 µm) and I-SD WPPC (2.72 µm) and the mean milk fat globule diameters did not differ substantially among FBD-WPPC (10.93 µm), SD-WPPC (11.51 µm), and I-SD WPPC (11.29 µm). Furthermore, confocal laser scanning microscopy revealed larger aggregates of protein and fat in the SD-WPPC and I-SD WPPC, whereas FBD-WPPC showed a more uniform protein distribution with distinct fat clusters. FTIR analysis indicated that FBD-WPPC retained the most native-like protein secondary structure, SD-WPPC displayed moderate structural changes, and I-SD WPPC exhibited the most pronounced alterations, with decreased α-helix and random coil contents and increased β-sheet and β-turn contributions. Xanthine oxidase activity normalized to protein content was significantly higher in FBD-WPPC than in both spray-dried powders, which did not differ from one another, demonstrating the influence of drying method on MFGM-enzyme stability. Protein oxidation, as measured by carbonyl content, was determined to be the lowest in I-SD WPPC but significantly not different among samples. Both primary (lipid hydroperoxides; LOOH) and secondary (TBARS) lipid oxidation products showed no significant differences among FBD-WPPC, SD-WPPC, and I-SD WPPC. Overall, these results provide new insight into how different drying methods and processing scales influence the microstructure and physicochemical properties of WPPC, informing future development of functional dairy coproduct powders.

Journal of Dairy Science
University of Wisconsin–Madison (US)
University of Wisconsin-Madison, Dairy Management
Openalex Percentile: Top 24%
Microencapsulation and Drying Processes
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