摘要：In the present study, we aimed to investigate the effects of pH and sodium chloride (NaCl) concentration on the structure of β‐casein (β‐CN) purified from buffalo milk using circular dichroism (CD), intrinsic tryptophan, and anilino‐8‐naphthalene sulfonate (ANS) fluorescence spectroscopy. We found that NaCl concentration played a critical role in the stability of the secondary structure of β‐CN. The CD negative peak had a redshift as the NaCl concentration was increased and accompanied by a decrease of β‐sheet content and an increase of α‐helix content. ANS fluorescence spectroscopy also indicated that higher NaCl concentration and lower pH significantly affected the tertiary structure of β‐CN. Dynamic light scattering (DLS) results showed that the particle size of buffalo β‐CN had a blueshift, and then a redshift within the pH range of 5.0–7.5, and it showed a redshift when the NaCl concentration was increased.
