The objective: To delay the digestion of carbohydrates by inhibiting the activity of carbohydrate digestive enzymes， thereby preventing and controlling the effects of diabetes has become a research hotspot across multiple fields. β-Conglycinin is the most abundant functional protein in soy protein， but it is unknown whether the peptides produced after gastrointestinal digestion possess the activity to inhibit carbohydrate digestive enzymes. Method: β-Conglycinin was subjected to simulated gastrointestinal digestion， and α-glucosidase inhibitory peptides and α-amylase inhibitory peptides were selected through virtual screening and ADMET prediction， and the inhibitory effects of the peptides on α-glucosidase and α-amylase were tested. Results: β-Conglycinin was virtually digested into 95 small molecular peptides by pepsin， trypsin， and chymotrypsin； eight α-glucosidase inhibitory peptides and α-amylase inhibitory peptides were selected； it was found that hydrogen bonds and electrostatic interactions play an important role in the binding of peptides with α-glucosidase and α-amylase； in vitro verification found that the tetrapeptide EASY has a strong inhibitory effect on α-glucosidase， with an IC50 value of 208.6 μg/mL， and no obvious inhibitory effect on α-amylase was observed. Conclusion: The α-glucosidase inhibitory peptide EASY possesses the activity to inhibit carbohydrate digestive enzymes and may become a potential inhibitor for controlling diabetes.