Heat-induced gel formation of plasma proteins: New insights by FTIR 2D correlation spectroscopy

Abstract Generalized 2D correlation spectroscopy (COS) has been applied to FTIR spectra of porcine plasma proteins to elucidate the sequence of events leading to pH- and/or thermal-induced protein unfolding and aggregation. Changes in the amide I′ region of the infrared spectra (in the pH range between 7.5 and 4.5, at 0.5 pH intervals) at 30 °C were especially evident as the pH approached the p I of serum albumin (4.8), with the globulin fraction in the plasma proteins undergoing denaturation prior to serum albumin. The effect of increasing temperature (from 30 to 90 °C, in increments of 5 °C) on the secondary structure of the plasma proteins at pHs in the range of 7.5–6.0 revealed that a decrease in alpha-helical structures is taken place previously to diminish native beta-sheets. So, the overall results of this study demonstrate that serum albumin and the globulin fraction differ in their sensitivity to pH and temperature.