Isolation and characterization of proteins from soymilk residue (okara)

Abstract

Protein was extracted from okara at pH 9.0 and 80°C for 30 min, giving a recovery of 53% protein. The extracted protein was isolated by isoelectric precipitation at pH 4.5, and the dried, defatted protein isolates (prepared at 25 and 80°C) had over 80% protein. The okara protein isolates have essential amino acid profiles similar to the FAO scoring pattern, and high in vitro protein digestibility, with methionine and cysteine as the limiting amino acids. Polyacrylamide gel electrophoresis in sodium dodecyl sulfate showed that okara protein isolates had a large quantity of high molecular weight components suggesting protein aggregation. Differential scanning calorimetry and hydrophobicity data suggested extensive protein unfolding in the okara products. Okara protein isolates had lower solubility than a commercial soy protein isolate at both acidic and alkaline pH, probably due to protein aggregation. Other functional properties, including emulsifying, water and fat binding, and foaming properties, were found to be comparable to the commercial soy isolate.