ENZYMATICALLY AND CHEMICALLY MODIFIED ZEIN FOR IMPROVEMENT OF FUNCTIONAL-PROPERTIES

Limited specific hydrolysis of zein by trypsin was used to produce 1.42%, 1.70%, and 1.87% hydrolysates (percentage of peptide bonds cleaved), containing three to four polypeptides (by Fast Protein Liquid Chromatography (FPLC)) ranging in size from approximately 16,000 to 3,500 daltons. The mixtures of polypeptides has substantially increased solubilities at pH below 11, including at the isoelectric point of zein (pH 6-7). In general, the emulsifying activity index was less for the hydrolysates than for native zein; the emulsion stability was higher for the 1.70% hydrolysate than was the emulsion of native zein only at pH above 8. At lower pHs, the stability of the emulsions was similar for all samples. The foamability (% overrun) of the hydrolysates was higher than for native zein; the foam stability was higher for the 1.87% hydrolysate than for the other hydrolysates. Phosphorylation and deamidation of the hydrolysates markedly increased the water solubility in the pH range from 4 to 10. Chemical modification of the native zein improved the solubility at pH 2 to 9 after phosphorylation and pH 6 to 11 after deamidation as compared to the native protein. In general, the emulsifying activity index, as well as its stability, was less for the phosphorylated and deamidated hydrolysates than for native zein but the emulsifying activity index of deamidated native zein was higher at pH 7 to 11. Foaming activity and stability of chemically modified hydrolysates were similar to the 1.87% hydrolysate.