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| Purification and stability of walnut protein DPP-IV inhibitory peptides |
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| DOI：10.12166/j.zgyz.1003-7969/2020.11.013 |
| KeyWord:walnut meal walnut peptide DPP-IV inhibitory activity walnut protein hydrolysate purification stability |
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| Abstract: |
| Five proteases were used to hydrolyze walnut meal, and the DPP-IV inhibitory activities of the enzymatic hydrolysates were evaluated. According to the DPP-IV inhibitory activity, Alcalase was selected as the enzyme for hydrolysis. The optimal hydrolysis time for Alcalase was determined as 5 h. Then the Alcalase-derived hydrolysate was purified by ultrafiltration and SP-Sephadex C-25 cation exchange column chromatography to obtain DPP-IV inhibitory peptides. The thermal stability, pH stability and gastrointestinal digestive stability of the DPP-IV inhibitory peptide were determined. The results showed that the DPP-IV inhibitory activity(76.19%, 0.25 mg/mL) of the obtained peptide increased by about 3 times compared with the hydrolysate.The DPP-IV inhibitory peptide was rich in basic amino acids, accounting for 34.36%, and the content of arginine was as high as 25.93%.The DPP-Ⅳ inhibitory peptide showed good stability under high temperature (121 ℃), extreme pH (pH 1.0 and pH 11.0) and gastrointestinal digestion conditions, so it could be used as a natural functional ingredient in foods for blood sugar control. |
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