Modification of structural and functional properties of sunflower 11S globulin hydrolysates

Abstract

Ren J., Song Ch.-L., Wang P., Li S., Kopparapu N.-K., Zheng X.-Q. (2015): Modification of structural and functional properties of sunflower 11S globulin hydrolysates. Czech J. Food Sci., 33: 474-478.The structural and functional properties such as solubility, emulsifying properties, foaming properties, oil binding capacity, and surface hydrophobicity of sunflower 11S globulin hydrolysates generated by Alcalase at hydrolysis time of 30, 60, 90, and 120 min were evaluated. Circular dichroism analysis showed the hydrolysates possessed a decreased α-helix and β-structure. The hydrolysates exhibited lower surface hydrophobicity. Hydrolysates with shorter hydrolysis time showed the higher emulsifying activity index, but the same emulsion stability and oil binding capacity compared to the original 11S globulin. The longer hydrolysis resulted in lower foaming and emulsion stability. Thus it was demonstrated that by controlling the hydrolysis time of sunflower 11S globulin, hydrolysate with a desirable functional properties can be obtained.

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“…DH for SMP was estimated by the pH‐stat method outlined by Adler‐Nissen () as follows: where, B representing the amount of NaOH consumed (mL); N b is the NaOH concentration (mol/L); α denotes the mean dissociation degree of the α‐NH in sunflower protein, which is 0.885 for alcalase; M p denotes the mass of hydrolyzed protein (g); and h total representing the total content of peptide bonds in the protein (7.50 mmol/g sunflower protein) (Ren et al, ).…”

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