The in vitro digestibility of alcalase enzymatic hydrolysates of β-conglycinin was studied. The results showed that the zeta potentials of β-conglycinin hydrolysates decreased and their electronegativity increased w...The in vitro digestibility of alcalase enzymatic hydrolysates of β-conglycinin was studied. The results showed that the zeta potentials of β-conglycinin hydrolysates decreased and their electronegativity increased when digested with pepsin and trypsin. Furthermore, the content of peptides with molecular weight from 10 kDa to 20 kDa remained stable, while those with higher molecular weight （〉20 kDa） decreased, and those with lower molecular weight （〈10 kDa） increased. The proportion of highly hydrophobic peptides decreased in the process of the in vitro digestion, but no significant change in the surface hydrophobicity indices of digestion products was observed （P 〈 0.05）. These results indicate that the β-conglycinin hydrolysates were degraded through in vitro digestion, but the degree of degradation was relatively low. Peptides with molecular weight from 10 kDa to 20 kDa in the β-conglycinin hydrolysates resisted the digestion by pepsin and trypsin and they remained stable during the in vitro digestion processes.展开更多
基金the financial support from the National Natural Science Foundation of China(No.30972046)the National Key Technologies Research and Development Program(No.2012BAD34B04)
文摘The in vitro digestibility of alcalase enzymatic hydrolysates of β-conglycinin was studied. The results showed that the zeta potentials of β-conglycinin hydrolysates decreased and their electronegativity increased when digested with pepsin and trypsin. Furthermore, the content of peptides with molecular weight from 10 kDa to 20 kDa remained stable, while those with higher molecular weight （〉20 kDa） decreased, and those with lower molecular weight （〈10 kDa） increased. The proportion of highly hydrophobic peptides decreased in the process of the in vitro digestion, but no significant change in the surface hydrophobicity indices of digestion products was observed （P 〈 0.05）. These results indicate that the β-conglycinin hydrolysates were degraded through in vitro digestion, but the degree of degradation was relatively low. Peptides with molecular weight from 10 kDa to 20 kDa in the β-conglycinin hydrolysates resisted the digestion by pepsin and trypsin and they remained stable during the in vitro digestion processes.
