Identification of bioactive compounds in Brassica oleracea var. capitata L. with enzyme-inhibitory activity against postprandial hyperglycemia.

Postprandial hyperglycemia is a hallmark of diabetes, and inhibition of key carbohydrate digestion enzymes such as α-amylase (α-AMY) and α-glucosidase (α-GLU) is an effective therapeutic target. A potential unexplored source of inhibitory compounds of these enzymes is Brassica oleracea var. capitata L (BOCE). This study explored the in vitro inhibition mechanism of BOCE and studied in silico the interaction of its compounds identified and quantified by UPLC-QTOF-MS on α-AMY and α-GLU. BOCE demonstrated IC values of 3.08 mg/mL for α-AMY and 22.63 mg/mL for α-GLU, indicating competitive and mixed-type inhibitions, respectively. Untargeted metabolomics identified 21 compounds, primarily phenolic acids such as t-cinnamic, sinapic, and caffeoylquinic acid. In the targeted analysis, 11 compounds were quantified, mainly phenolic acids. The most impactful biosynthetic pathways identified were phenylpropanoids and brassinosteroids. In silico analysis revealed that for α-AMY and α-GLU, castasterone and 26-hydroxybrassinolide displayed the lowest binding free energies with specific hydrogen bond patterns to catalytic residues in the binding site, respectively. B. oleracea is a promising source of compounds with the ability to modulate key enzymes related to hyperglycemia. Specifically, compounds such as castasterone and 26-hydroxybrassinolide show potential against α-AMY and α-GLU inhibition, offering a novel approach to diabetes.