Solubility, Tensile, and Color Properties of Modified Soy Protein Isolate Films

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Abstract
Protein solubility (PS) values of different soy protein isolate (SPI) films were determined in water, 0.01 N HCl, 0.01 N NaOH, 4 M urea, and 0.2 M 2-mercaptoethanol. Tensile and color (L, a, and b values) properties of films also were determined. Control films were cast from heated (70 °C for 20 min), alkaline (pH 10) aqueous solutions of SPI (5 g/100 mL of water) and glycerin (50% w/w of SPI). Additional films were cast after incorporation of dialdehyde starch (DAS) at 10% w/w of SPI or small amounts of formaldehyde in the film-forming solutions. Also, control film samples were subjected to heat curing (90 °C for 24 h), UV radiation (51.8 J/m2), or adsorption of formaldehyde vapors. PS of control films was highest (P < 0.05) in 2-mercaptoethanol, confirming the importance of disulfide bonds in SPI film formation. All treatments were effective in reducing (P < 0.05) film PS in all solvents. Both DAS and adsorbed formaldehyde rendered the protein in films practically insoluble in all solvents. Adsorption of formaldehyde vapors and heat curing also substantially increased (P < 0.05) film tensile strength from 8.2 to 15.8 or 14.7 MPa, respectively. However, heat curing decreased (P < 0.05) film elongation at break from 30 to 6%. Most treatments had small but significant (P < 0.05) effects on b color values, with DAS-containing films having the greatest (P < 0.05) mean b value (most yellowish). Also, DAS-containing, heat-cured, and UV-irradiated films were darker, as evidenced by their lower (P < 0.05) L values, than control films. It was demonstrated that PS of SPI films can be notably modified through chemical or physical treatments prior to or after casting. Keywords: Protein films; soy protein; dialdehyde starch; formaldehyde; cross-linking