eFood

Volume 1, Issue 2, April 2020, Pages 156 - 164

Trypsin-hydrolyzed Corn Silk Proteins: Antioxidant Activities, in vitro Gastrointestinal and Thermal Stability, and Hematoprotective Effects

Authors
Tsun-Thai Chai1, 2, *, Shin-Yii Ang1, Kervine Goh1, You-Han Lee1, Jia-Min Ngoo1, Lai-Kuan Teh2, 3, Fai-Chu Wong1, 2
1Department of Chemical Science, Faculty of Science, Universiti Tunku Abdul Rahman, 31900 Kampar, Malaysia
2Center for Biodiversity Research, Universiti Tunku Abdul Rahman, 31900 Kampar, Malaysia
3Department of Allied Health Sciences, Faculty of Science, Universiti Tunku Abdul Rahman, 31900 Kampar, Malaysia
*Corresponding author. Email: chaitt@utar.edu.my
Corresponding Author
Tsun-Thai Chai
Received 13 December 2019, Accepted 19 March 2020, Available Online 27 March 2020.
DOI
10.2991/efood.k.200323.001How to use a DOI?
Keywords
Hematoprotection; lipid peroxidation; protein hydrolysate; simulated gastrointestinal digestion; stigma maydis; thermal stability
Abstract

The aim of this study was to examine the antioxidant capacity of Trypsin-hydrolyzed corn silk proteins, specifically radical scavenging, ferric reducing and anti-lipid peroxidation activities, as well as stability after heating and simulated gastrointestinal digestion. Among the 1–5-h hydrolysates, the 1-h Trypsin hydrolysate (T1H) was the strongest. T1H exhibited stronger H2O2 [half maximal effective concentration (EC50) = 156.44 µg/mL] and superoxide (EC50 = 0.33 mg/mL) scavenging activities than glutathione, carnosine and N-acetylcysteine. Radical scavenging activities of T1H were heat-stable (25–100°C), although lost by 20–58% after gastrointestinal digestion. Ferric reducing activity of T1H was heat-stable, even enhanced by 20% after gastrointestinal digestion. Lecithin liposome assay found anti-lipid peroxidation activity of T1H resistant to gastrointestinal peptidases. By contrast, 100°C incubation reduced anti-lipid peroxidation activity of 0.5 mg/mL T1H to 3.5-fold lower than that of 25°C incubation. At 30 µg/mL, T1H (3% hemolysis) was stronger than glutathione (32% hemolysis) in protecting human red blood cells. T1H was 1.5-fold more potent than glutathione and carnosine in alleviating lipid peroxidation in the cells. Overall, T1H demonstrated strong, heat-stable radical scavenging activities, besides partial resistance to gastrointestinal peptidases. T1H was also hematoprotective. T1H is a promising antioxidant for the development of functional food ingredients and nutraceuticals.

Copyright
© 2020 International Association of Dietetic Nutrition and Safety. Publishing services by Atlantis Press International B.V.
Open Access
This is an open access article distributed under the CC BY-NC 4.0 license (http://creativecommons.org/licenses/by-nc/4.0/).

Download article (PDF)
View full text (HTML)

Journal
eFood
Volume-Issue
1 - 2
Pages
156 - 164
Publication Date
2020/03/27
ISSN (Online)
2666-3066
DOI
10.2991/efood.k.200323.001How to use a DOI?
Copyright
© 2020 International Association of Dietetic Nutrition and Safety. Publishing services by Atlantis Press International B.V.
Open Access
This is an open access article distributed under the CC BY-NC 4.0 license (http://creativecommons.org/licenses/by-nc/4.0/).

Cite this article

TY  - JOUR
AU  - Tsun-Thai Chai
AU  - Shin-Yii Ang
AU  - Kervine Goh
AU  - You-Han Lee
AU  - Jia-Min Ngoo
AU  - Lai-Kuan Teh
AU  - Fai-Chu Wong
PY  - 2020
DA  - 2020/03/27
TI  - Trypsin-hydrolyzed Corn Silk Proteins: Antioxidant Activities, in vitro Gastrointestinal and Thermal Stability, and Hematoprotective Effects
JO  - eFood
SP  - 156
EP  - 164
VL  - 1
IS  - 2
SN  - 2666-3066
UR  - https://doi.org/10.2991/efood.k.200323.001
DO  - 10.2991/efood.k.200323.001
ID  - Chai2020
ER  -