4.6 Article

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

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MOLECULES
卷 28, 期 19, 页码 -

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MDPI
DOI: 10.3390/molecules28196847

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thermal stability; micellar calcium phosphate; adjustment; skim milk; FTIR

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The present study investigated the effect of micellar calcium phosphate (MCP) content and pH of skim milk on heat-induced changes in skim milk. The results demonstrated that reducing MCP content had a positive effect on the thermal stability of milk protein, while higher MCP content might lead to changes in protein structure and the formation of aggregates.
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( degrees)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 MCP67 samples revealing the greatest thermal stability. Specifically, decreasing MCP content by 33% (MCP67) led to a smaller increase in non-sedimentable kappa-casein and a lower decrease in alpha s2-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 beta-turn structural component after heating at low pH (pH 6.3). Notably, MCP113 exhibited instability upon heating, with increased particle size, turbidity, and a significant decrease in non-sedimentable alpha s2-casein concentration, along with a slight increase in non-sedimentable kappa-casein concentration. The FTIR results also revealed higher loading of intermolecular beta-sheet, beta-turn, and random coil structures, as well as lower loading of alpha-helix and beta-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.

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