The interactions of a commercial soy protein isolate (SPI) and a 2:1 SPI:high methoxy pectin (PEC) complex were evaluated over a range of pH values (3-7). The SPI formed very large (> 50 > m) and largely insoluble aggregates (< 10%) close to its isoelectric point (IEP, pH 4 and 5) and smaller, more soluble (> 80%) particles at higher and lower pH values. The addition of PEC increased the solubility of SPI close to its IEP (pH 4 and 5) and prevented the formation of very large aggregates. However, PEC reduced the solubility of SPI at higher and lower pH values presumably via a depletion mechanism. The Ζ-potential of diluted SPI dispersions decreased from positive to negative with increasing pH, passing through zero at pH 4.6, the isoelectric point (IEP) of the protein. At pH < 6, the addition of PEC reduced the charge of the protein suggesting the formation of a complex while at pH 6 or 7 there was no evidence of complex formation. The increased SPI solubility in the IEP in the presence of PEC is probably due to the formation of charged complex which do not aggregate while the decreased solubility of protein in the presence at high and low PEC is probably due to the formation of insoluble complexes and a depletion interaction respectively. Thermal treatment (30 min, 90. °C) enhanced the solubility of the SPI:PEC complexes close to the IEP (pH 4 and 5), but reduces it at low pH (pH 3). The SPI:PEC complexes could be manufactured in the form of a beverage at pilot scale where their solubility was enhanced by homogenization.
All Science Journal Classification (ASJC) codes
- Food Science