Effect of removal of phenolic compounds on structural and thermal properties of sunflower protein isolate.

The present study evaluated the effect of removal of polyphenols on the structural properties of protein isolates extracted from sunflower seed and kernel. The structural and thermal changes in protein upon phenolic interaction were studied using circular dichroism, differential scanning calorimetry, thermal gravimetric analysis, X-ray diffraction, sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), and Fourier Transform Infrared (FT-IR) spectroscopy. Presence of phenolic compounds in proteins decreased the ordered structure content with parallel increase in unordered structure content. Denaturation temperature was higher for protein isolates with phenolic compounds while, enthalpy decreased upon phenolic interaction. In the presence of phenolic compounds, higher mass loss was observed upon heating. Crystalinity and crystal size got increased after removal of phenolic compounds. Protein isolates from kernels had higher percentage of crystalinity and crystal size as compared to seed protein isolates. Higher molecular weights were observed for protein isolates with phenolic compounds. Presence of polyphenols reduced the hydrophobicity as well the sulfhydryl content and increased the particle size of proteins.