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Influence of pH on Heat-Induced Changes in Skim Milk Containing Various Levels of Micellar Calcium Phosphate

The present study investigated the effect of micellar calcium phosphate (MCP) content and pH of skim milk on heat-induced changes in skim milk. Four MCP-adjusted samples, ranging from 67 to 113% of the original MCP content, were heated (90 °C for 10 min) at different pH values (6.3, 6.6, 6.9, and 7....

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Detalles Bibliográficos
Autores principales: Ahmadi, Elaheh, Vasiljevic, Todor, Huppertz, Thom
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10574568/
https://www.ncbi.nlm.nih.gov/pubmed/37836690
http://dx.doi.org/10.3390/molecules28196847
Descripción
Sumario:The present study investigated the effect of micellar calcium phosphate (MCP) content and pH of skim milk on heat-induced changes in skim milk. Four MCP-adjusted samples, ranging from 67 to 113% of the original MCP content, were heated (90 °C for 10 min) at different pH values (6.3, 6.6, 6.9, and 7.2), followed by determining changes in particle size, turbidity, protein distribution, and structure. The results demonstrate a strong effect of MCP level and pH on heat-induced changes in milk, with the MCP(67) samples revealing the greatest thermal stability. Specifically, decreasing MCP content by 33% (MCP(67)) led to a smaller increase in non-sedimentable κ-casein and a lower decrease in αs(2)-casein concentrations after heating compared to other samples. Lower MCP content resulted in a moderate rise in the average particle size and turbidity, along with lower loading of β-turn structural component after heating at low pH (pH 6.3). Notably, MCP(113) exhibited instability upon heating, with increased particle size, turbidity, and a significant decrease in non-sedimentable αs(2)-casein concentration, along with a slight increase in non-sedimentable κ-casein concentration. The FTIR results also revealed higher loading of intermolecular β-sheet, β-turn, and random coil structures, as well as lower loading of α-helix and β-sheet structures in MCP-enhanced skim milk samples. This suggests significant changes in the secondary structure of milk protein and greater formation of larger aggregates.