Quinoa (Chenopodium quinoa Willd.) protein hydrolysates with in vitro dipeptidyl peptidase IV (DPP-IV) inhibitory and antioxidant properties

- Quinoa protein hydrolysates (QPHs) were generated with two enzyme preparations.
- The DPP-IV inhibitory and ORAC activities of the QPHs were studied.
- The QPHs were more potent DPP-IV inhibitors and antioxidants than the QPIs.
- Quinoa proteins may find use as a source of antidiabetic and antioxidant peptides.

The potential of quinoa to act as a source of dipeptidyl peptidase IV (DPP-IV) inhibitory and antioxidant peptides was studied. A quinoa protein isolate (QPI) with a purity of 40.73 ± 0.90% was prepared. The QPI was hydrolysed at 50 °C for 3 h with two enzyme preparations: papain (P) and a microbial papain-like enzyme (PL) to yield quinoa protein hydrolysates (QPHs). The hydrolysates were evaluated for their DPP-IV inhibitory and oxygen radical absorbance capacity (ORAC) activities. Protein hydrolysis was observed in the QPI control, possibly due to the activity of quinoa endogenous proteinases. The QPI control had significantly higher DPP-IV half maximal inhibitory concentrations (IC50) and lower ORAC values than QPH-P and QPH-PL (P < 0.05). Both QPH-P and QPH-PL had similar DPP-IV IC50 and ORAC values. QPH-P had a DPP-IV IC50 value of 0.88 ± 0.05 mg mL−1 and an ORAC activity of 501.60 ± 77.34 μmol Trolox equivalent (T.E.) g−1. To our understanding, this is the first study demonstrating the in vitro DPP-IV inhibitory properties of quinoa protein hydrolysates. QPHs may have potential as functional ingredients with serum glucose lowering properties.