While hypoglycemic protein hydrolysates have been widely studied for single-target enzyme inhibition, multi-mechanistic candidates with improved gastrointestinal bioavailability remain essential for effective glycemic regulation. In this study, chickpea protein hydrolyzed by Aspergillus oryzae protease (CP_AoN) was digested in vitro, and a potent fraction 7 (F7) was isolated to show strong concurrent inhibitions of dipeptidyl peptidase IV (DPP-IV, IC₅₀ of 0.09 mg/mL), α-glucosidase (0.12 mg/mL), and α-amylase (0.06 mg/mL). Based on Caco-2 cell model, F7 exhibited great in situ inhibitions of DPP-IV (1.86 × 10⁵ luminescence units), sucrase (42.22%), maltase (51.44%), and glucose transport (50.65%) at 0.20 mg/mL. It crossed the intestinal epithelium via paracellular diffusion and identified 120 antidiabetic peptides, with 105 stable against brush border peptidases and 32 transported intact. Peptides bearing N-terminus of tyrosine and C-terminus of tryptophan/leucine contributed to superior intestinal stability and permeability. CP_AoN could be used as a promising hypoglycemic ingredient for glycemic control. 

This study obtained a strain producing high yield of exopolysaccharide (EPS), which was identified as Lactiplantibacillus plantarum HZB-30. The strain produced 230.66 mg/L of EPS after fermentation for 28 h. The molecular mass of EPS produced by HZB-30 was 14639 Da, which was composed of several monosaccharides, such as glucose (37.76%) and galactose (19.15%). The EPS had high inhibitory activity against xanthine oxidase (XO) with an inhibition rate of 80.2%. After in vitro simulated digestion, the digestibility of the EPS was 20.7%, and 43.3% of the initial xanthine oxidase inhibitory activity remained. In an HK-2 cell model of hyperuricemia, the EPS at 20–60 μg/mL effectively decreased the levels of tumor necrosis factor-α (TNF-α), interleukin-1β (IL-1β), IL-6, and IL-8 and inhibited the accumulation of uric acid. The findings from this study are both theoretically and practically important for the application of HZB-30-derived EPS to develop anti-hyperuricemic food products.