In vitro digestion of rice bran proteins produces peptides with potent inhibitory effects on α‐glucosidase and angiotensin I converting enzyme

The bioactivities of peptides released from the digestion of rice bran protein under in vitro simulated human digestive conditions were investigated. Four protein fractions extracted from rice bran were digested and the hydrolysates were fractionated by ultrafiltration and anion exchange chromatography. α-Glucosidase and angiotensin converting enzyme (ACE) inhibitory activities of the crude hydrolysates and their fractions were determined.Peptides with molecular weight (MW) < 3 kDa gave markedly higher α-glucosidase inhibitory activities than the crude digests, while the ACE inhibitory activities of the MW < 3 kDa fractions were similar to those of the crude extracts. Peptides from albumin and glutelin exhibited the greatest inhibitory effects on α-glucosidase and ACE at 52.43 ± 2 mg acarbose equivalent and 170.13 ± 2.2 nmol captopril equivalent g-1 peptide respectively. Liquid chromatography/tandem mass spectrometry (LC/MS/MS) analysis identified 39 peptides in the most active fraction of the hydrolysates, and 37 of these contained peptide sequences that are known to exhibit antidiabetic or antihypertensive activities.Consumption of rice bran proteins can potentially lead to generation of bioactive peptides in the digestive tract with substantial health benefits. ACE and α-glucosidase inhibitory activities of the digests of rice bran proteins, and albumin and glutelin in particular, were especially strong, comparable to that of the standard drugs. © 2017 Society of Chemical Industry.