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| pH-Shift dissolving the aggregates during soybean protein enzymolysis |
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| DOI： |
| KeyWord:soybean protein peptide aggregates pH-shift amino acid analysis alkaline protease |
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| Abstract: |
| The enzymatic hydrolysis of soybean protein produces a variety of bioactive peptides. However, due to the self-aggregation of peptides in the enzymatic hydrolysis process, insoluble aggregates are produced and protein utilization rate is reduced. The pH-shift dissolving the soybean peptide aggregates was studied. The results showed that the insoluble precipitate obtained by Alcalase enzymatic hydrolysis of soybean protein was peptide aggregates with hydrophobic interaction as the main intermolecular force. The charge repulsion provided by the pH-shift technology promoted the depolymerization and rearrangement of the soybean peptide aggregation system. The soybean peptide protein utilization rate increased from 74% at pH 7 to 85% at pH 12, and the average particle size of soy protein peptides reduced from 243 nm to 103 nm. At the same time, pH-shift caused hydrophobic amino acids to accumulate in insoluble aggregates, increasing the random coil content in the secondary structure, but did not affect the relative molecular weight distribution of the insoluble aggregates. Therefore, the pH-shift technology could safely and effectively promote the depolymerization of insoluble aggregates of soybean peptides. |
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