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Seminar Presentation
Analyzing the Effects of Heat Treatments on the Structure and Oxidation of Whey Protein Phospholipid Concentrate
Rebecca Goodman1, Mitchell T. Armstrong1, Fatemeh Jalil Mozhdehi1, Luis McDougall2, Jerina Rugji1, Audrey Girard1, Mark P. Richards1,3, Gulustan Ozturk1
1 Department of Food Science, University of Wisconsin-Madison, Madison, Wisconsin, 53706, United States
2 Department of Integrative Biology, University of Wisconsin-Madison, Madison, Wisconsin, 53706, United States
3 Animal Science Department, University of Wisconsin-Madison, Madison, Wisconsin, 53706, United States
Whey protein phospholipid concentrate (WPPC) is an underutilized co-product of whey protein isolate manufacturing. As WPPC is an enriched source of milk fat globule membrane components, there is growing interest in using whole WPPC and/or its valuable protein and lipid fractions in human nutrition applications. However, WPPC undergoes multiple thermal treatments during processing, which may induce structural changes, promote oxidation, and hinder downstream fractionation efficiency, potentially limiting its nutritional and functional value.
This study compares two commercial production styles of WPPC with a minimal-heat production style to characterize heat-induced structural and oxidative modifications, which may inform improved processing strategies. Spray-dried WPPC showed significant microstructural changes at the micrometer scale but not at the nanometer scale. Post-filtration heating increased b-turn content in proteins as determined by FTIR analysis. While primary lipid oxidation was unaffected by heat intensity, secondary oxidation products decreased following HTST or spray drying; conversely, protein carbonyl levels increased, indicating enhanced protein oxidation. These findings suggest that intense heat can simultaneously mitigate certain lipid oxidation pathways while promoting protein oxidation.
Free b-lactoglobulin content was consistent between the different commercial-production style WPPCs, but significantly higher in the minimal-heat WPPC, suggesting that thermal processing induces b-lactoglobulin unfolding and aggregation. Collectively, these results demonstrate the substantial influence of heat treatment on WPPC structure and oxidation. A better understanding of these heat-induced changes can inform optimized processing and fractionation strategies to improve the functional and nutritional utilization of WPPC as a protein- and lipid-rich ingredient.