Journal
JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY
Volume 83, Issue 1, Pages 71-78Publisher
WILEY
DOI: 10.1007/s11746-006-1178-y
Keywords
cellulase; beta-conglycinin; functional properties; glycinin; pectinase; protein extraction; soy protein
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This study investigated the potential of enzymes to increase soy protein extractability without causing protein degradation. The aqueous extraction of protein was performed from defatted soy flakes on a laboratory- and pilot-plant scale. Yields of protein and reducing sugars were determined in the alkali extracts obtained with cellulases and pectinase, added alone or as cocktails. Using 5% (wt/g of protein) Multifect pectinase resulted in the best improvement of protein yields, which were 50 and 17% greater than the controls in laboratory- and pilot-plant-scale trials, respectively. This enhanced protein extraction was accompanied by an increased reducing sugar content in the aqueous extract compared with the control. Under the conditions tested, no enzyme cocktail markedly increased the protein yield compared with the use of single enzymes. The solubility curve for Multifect pectinase-treated soy protein isolate (SPI) was typical of SPI at pH 2-10. Its foam stability significantly improved, but the emulsification properties declined. Multifect pectinase markedly reduced the viscosity of SPI. SDS-PAGE showed that the alpha' and alpha subunits of beta-conglycinin were modified, and glycoprotein staining showed that these modifications were probably due to a protease secondary activity in the pectinase preparation. One cellulase and one pectinase were identified as effective in modifying the protein and reducing sugar extractability from the defatted soy flakes.
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