Structural Properties of Casein Micelles with Adjusted Micellar Calcium Phosphate Content.

Micellar calcium phosphate (MCP) content of skim milk was modified by pH adjustment followed by dialysis. Turbidity, casein micelle size and partitioning of Ca and caseins between the colloidal and soluble phases of milk were determined. Protein structure was characterised by Fourier transform infrared (FTIR) spectroscopy and proton nuclear magnetic resonance (H NMR), whereas organic and inorganic phosphorus were studied by phosphorus-31 nuclear magnetic resonance (P NMR).

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 β-casein as a function of temperature (4 and 20 °C) and pH (5.9 and 7.0).

Effects of pressurized thermal processing on native proteins of raw skim milk and its concentrate.

Heating, pressurization, and shearing can modify native milk proteins. The effects of pressurized heating (0.5 vs.

Unravelling Conformational Aspects of Milk Protein Structure-Contributions from Nuclear Magnetic Resonance Studies.

Changes in the molecular structure and association of milk proteins lead to many desirable (under controlled conditions) or undesirable characteristics of dairy products. Several methods have been used to study the structure of milk proteins and changes therein in different environments. Whey proteins are an excellent model for secondary structure studies using circular dichroism (CD), Fourier-transform infrared spectroscopy (FTIR) and tertiary structure studies using X-ray crystallography and nuclear magnetic resonance (NMR).