Structural Changes of β-Casein Induced by Temperature and pH Analysed by Nuclear Magnetic Resonance, Fourier-Transform Infrared Spectroscopy, and Chemometrics

This study investigated structural changes in beta-casein as a function of temperature (4 and 20 & DEG;C) and pH (5.9 and 7.0). For this purpose, nuclear magnetic resonance (NMR) and Fourier-transform infrared (FTIR) spectroscopy were used, in conjunction with chemometric analysis. Both temperature and pH had strongly affected the secondary structure of beta-casein, with most affected regions involving random coils and alpha-helical structures. The alpha-helical structures showed great pH sensitivity by decreasing at 20 & DEG;C and diminishing completely at 4 & DEG;C when pH was increased from 5.9 to 7.0. The decrease in alpha-helix was likely related to the greater presence of random coils at pH 7.0, which was not observed at pH 5.9 at either temperature. The changes in secondary structure components were linked to decreased hydrophobic interactions at lower temperature and increasing pH. The most prominent change of the alpha-helix took place when the pH was adjusted to 7.0 and the temperature set at 4 & DEG;C, which confirms the disruption of the hydrogen bonds and weakening of hydrophobic interactions in the system. The findings can assist in establishing the structural behaviour of the beta-casein under conditions that apply as important for solubility and production of beta-casein.

Automated summary

The study found that temperature and pH significantly influenced the secondary structure of beta-casein, particularly affecting random coils and alpha-helical structures. Changes in structural components were associated with decreased hydrophobic interactions at lower temperature and increasing pH. The most noticeable alteration in the alpha-helix occurred when the pH was adjusted to 7.0 and the temperature set at 4°C, leading to disruption of hydrogen bonds and weakening of hydrophobic interactions.