The significant (p < 0.05) decreases in protein yield and purity
were observed with prolonged hydrolysis time (>30 min), which
may be related to the difficulty in the precipitation of some small
molecular weight peptides at isoelectric point. Even so, these two
parameters are still in a acceptable range for industrial production
due to the recovery of a majority of unhydrolysed protein. In fact,
for SPI prepared by enzyme-assisted SW treatment, the possibility
of forming protein aggregates builted from unhydrolysed and/or
hydrolyzed fragment could not be ruled out due to heat- and/or
enzymic-induced aggregation (Kuipers et al., 2007; Lv et al., 2009).
Kuipers et al. (2007) reported that soy protein hydrolysates were
able to form protein aggregates due to the exposure of hydrophobic
groups during hydrolysis. In addition, the decrease in protein purity
may be attributed to SW- and/or enzymatic-released soluble carbohydrates and their Maillard reaction with soy protein during the
extraction process.
The significant (p < 0.05) decreases in protein yield and puritywere observed with prolonged hydrolysis time (>30 min), whichmay be related to the difficulty in the precipitation of some smallmolecular weight peptides at isoelectric point. Even so, these twoparameters are still in a acceptable range for industrial productiondue to the recovery of a majority of unhydrolysed protein. In fact,for SPI prepared by enzyme-assisted SW treatment, the possibilityof forming protein aggregates builted from unhydrolysed and/orhydrolyzed fragment could not be ruled out due to heat- and/orenzymic-induced aggregation (Kuipers et al., 2007; Lv et al., 2009).Kuipers et al. (2007) reported that soy protein hydrolysates wereable to form protein aggregates due to the exposure of hydrophobicgroups during hydrolysis. In addition, the decrease in protein puritymay be attributed to SW- and/or enzymatic-released soluble carbohydrates and their Maillard reaction with soy protein during theextraction process.
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