Biologically Active Digests from Pumpkin Oil Cake Protein: Effect of Cross-linking by Transglutaminase
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Date
2017-09-04
Authors
Popović, Ljiljana
Stolić, Žužana
Čakarević, Jelena
Torbica, Aleksandra 
Tomić, Jelena
Šijački, Mirjana
Journal Title
Journal ISSN
Volume Title
Publisher
Wiley
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.
Description
peer-reviewed
Keywords
ACE inhibition, anti-oxidant activity, Cucurbita pepo, In vitro digestion, transglutaminase
Citation
Lj. Popović, Ž. Stolić, J. Čakarević, A. Torbica, J. Tomić, M. Šijački. Biologically Active Digests from Pumpkin Oil Cake Protein: Effect of Cross-linking by Transglutaminase. Journal of the American Oil Chemists' Society, 94 (2017) 1245–1251.