Solubility and conformational characterization of rice glutelin after high temperature treatment.

Enhancing the solubility of rice glutelin in neutral aqueous solution is the prerequisite for the development of rice protein drinks and ingredients. Herein, glutelin was first dissolved in an aqueous solution of pH 12, and then heated at 121 °C for 20 min. The results showed that the solubility of glutelin increased from 2.55 mg/mL to 20.7 mg/mL at pH 7. The size of glutelin aggregates at pH 7 decreased from 900 nm to 400 nm after high temperature treatment (HTT), which was confirmed by atomic force microscopy. The results of small angle X-ray scattering showed that HTT induced the conformational unfolding of glutelin, and the protein in the aggregate was rod like shape as well as the mean square rotation radius decreased from 64.9 to 54.8 Å. Furthermore, Raman spectrum results also agree with the unfolding of glutelin conformation, which was mainly reflected in the changes of tyrosine and tryptophan residues, as well as the decreasing of α-helix content and increasing of β-sheet content. After being freeze-dried, HTT glutelin has a re-solubilization capacity of 15.48 mg/mL in pH 7 aqueous solution, which was superior to that of spray dried glutelin powder (pH 7, 9.19 mg/mL). [ABSTRACT FROM AUTHOR]