Effects of heat and pH treatments and in vitro digestion on the biological activity of protein hydrolysates of Amaranthus hypochondriacus L. grain.

Abstract

The aim of this work was to assess the effects of temperature (T), time (t) and pH treatments and an in vitro digestion on the stability of the angiotensin I-converting-enzyme-inhibitory activity (ACEIA) and antithrombotic activity (ATA; assessed as inhibition of platelet aggregation) of selected protein hydrolysates of amaranth named Alb1H103 and GloH88 and GluH24 with dipeptidyl peptidase IV inhibitory activity (DPPIVIA). Heat treatment (40-100°C) for 1h showed no significant differences among ACEIA, DPPIVIA and ATA of the heated hydrolysates at pH 4 and 7. There was no statistically significant loss of any bioactivity under heat treatment for 3h at pH 4.0. Alb1H103 and GluH24 maintained the inhibitory activity of ACE and ATA at pH 7.0 for 3h, whereas GloH88 maintained ACEIA and ATA for 2.0h at pH 7.0. The pH effect on hydrolysates bioactivity was assessed in the range of 2.0-12.0. This was negligible on ACEIA, ATA and DPPIVIA. The in vitro digestion was performed using pepsin, trypsin (T) and α-chymotrypsin (C). A previous treatment of hydrolysates with pepsin improved the proteolytic activities of T and C. The hydrolysates kept at 100°C for 1h at pH 4.0, showed a significant increase in bioactivity. Conversely, a treatment at pH 7.0 showed no significant difference (p<0.05) in the hydrolysates bioactivities after their digestion. Thus, biological activity of hydrolysates may be preserved or enhanced, depending on their processing conditions.