Abstract
The effects of sodium bisulfite on the electrophoresis profile; turbidity; and thermal, surface, and adhesive properties of soy β-conglycinin protein were studied. Sodium bisulfite dissociated high-molecular-weight aggregates in the protein, and the aggregate percentage decreased with increasing sodium bisulfite concentration. Denaturation temperature of sodium-bisulfite-treated β-conglycinin increased as sodium bisulfite increased. However, at high sodium bisulfite concentration (i.e. 36 g/L), denaturation enthalpy decreased significantly. Sodium bisulfite caused changes in the β-conglycinin secondary structure and promoted ionization of lysine residues as indicated by FT-IR results. A sudden drop in turbidity at pH 4.8 was observed at the same salt level. The contact angle of β-conglycinin on cherry wood reached its minimum at 6 g/L sodium bisulfite and 24 g/L on glass. Water resistance of β-conglycinin was improved but not significantly by 6 g/L sodium bisulfite at pH 9.5. An obvious increase in adhesion strength of the protein occurred at 3 and 6 g/L sodium bisulfite at pH 4.8. A high sodium bisulfite concentration at 36 g/L sharply reduced the adhesive performance of β-conglycinin.
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X. S. Sun: Contribution No. 09-060-J from the Kansas Agricultural Experimental Station, Manhattan, KS 66506.
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Zhang, L., Sun, X.S. Sodium Bisulfite-Induced Changes in the Physicochemical, Surface and Adhesive Properties of Soy β-Conglycinin. J Am Oil Chem Soc 87, 583–590 (2010). https://doi.org/10.1007/s11746-009-1528-7
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DOI: https://doi.org/10.1007/s11746-009-1528-7