Abstract:
The objective of this study was to show that biologically active hydrolysates can be obtained by simulated human gastrointestinal digestion (HGD) of transglutaminase cross-linked pumpkin oil cake protein (Tg-C) which was previously reported as a potential functional food additive. A two-stage in vitro digestion model system (by pepsin and α chymotrypsin and trypsin, simultaneously) was used to simulate the process of HGD on native and Tg-C major storage pumpkin oil seed/cake protein, cucurbitin (C). The biologically active potential of the digests was evaluated, measuring the angiotensin-converting-I enzyme (ACE) inhibitory and anti-oxidant capacity. The ACE inhibitory activity was determined in both final digests, with IC50 = 0.30 ± 0.04 mg/ml for C and IC50 = 0.28 ± 0.01 for Tg-C. The anti-oxidant potency of the examined proteins was enhanced by the digestion process. The 2,2-diphenyl-1-picrylhydrazyl and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) radical cation activities and reducing power testing showed that all the hydrolysates act as a radical quencher and reducing agents. Overall, the results showed that the cross-linking by Tg did not influence the digestion process, as well as having no effect on the biological activity of the hydrolysates. These also indicate that Tg-C, if used as functional food additive, after food consumption can be digested and become a source of peptides exerting positive effects on human health.
