Abstract: In this study, alcalase and papain were separately used to hydrolyze camel milk protein, and the hydrolysis process, α-amylase inhibitory activity, amino acid composition, molecular mass distribution and peptide sequence were comparatively investigated so as to obtain peptides with strong α-amylase inhibitory activity. The results showed that the α-amylase inhibitory activity of camel milk protein was enhanced after enzymatic hydrolysis. Compared with that obtained using alcalase (JX), the protein hydrolysate (MG) prepared using papain under the following optimum conditions: enzyme dosage, 4%; temperature, 55 ℃; pH, 7.0; and hydrolysis time, 2 h possessed higher α-amylase inhibitory activity. A total of 110 and 69 peptides were identified from JX and MG, respectively, of which IPLPLPLPLP and LPLPLPLR were the most effective α-amylase inhibitory peptides. Therefore, camel milk protein can be a potential source of anti-diabetes ingredients in functional foods or health products.

Key words: camel milk protein; enzymatic hydrolysis; bioactive peptides; α-amylase inhibitory activity; identification