Trypsin-hydrolyzed Corn Silk Proteins: Antioxidant Activities, in vitro Gastrointestinal and Thermal Stability, and Hematoprotective Effects
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,...
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| Format: | Article |
| Language: | English |
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Wiley
2020-03-01
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| Series: | eFood |
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| Online Access: | https://www.atlantis-press.com/article/125937742/view |
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| author | Tsun-Thai Chai Shin-Yii Ang Kervine Goh You-Han Lee Jia-Min Ngoo Lai-Kuan Teh Fai-Chu Wong |
| author_facet | Tsun-Thai Chai Shin-Yii Ang Kervine Goh You-Han Lee Jia-Min Ngoo Lai-Kuan Teh Fai-Chu Wong |
| author_sort | Tsun-Thai Chai |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-12T11:51:25Z |
| format | Article |
| id | doaj.art-a7124a6896964858829af5eb911ce527 |
| institution | Directory Open Access Journal |
| issn | 2666-3066 |
| language | English |
| last_indexed | 2024-12-12T11:51:25Z |
| publishDate | 2020-03-01 |
| publisher | Wiley |
| record_format | Article |
| series | eFood |
| spelling | doaj.art-a7124a6896964858829af5eb911ce5272022-12-22T00:25:19ZengWileyeFood2666-30662020-03-011210.2991/efood.k.200323.001Trypsin-hydrolyzed Corn Silk Proteins: Antioxidant Activities, in vitro Gastrointestinal and Thermal Stability, and Hematoprotective EffectsTsun-Thai ChaiShin-Yii AngKervine GohYou-Han LeeJia-Min NgooLai-Kuan TehFai-Chu WongThe 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.https://www.atlantis-press.com/article/125937742/viewHematoprotectionlipid peroxidationprotein hydrolysatesimulated gastrointestinal digestionstigma maydisthermal stability |
| spellingShingle | Tsun-Thai Chai Shin-Yii Ang Kervine Goh You-Han Lee Jia-Min Ngoo Lai-Kuan Teh Fai-Chu Wong Trypsin-hydrolyzed Corn Silk Proteins: Antioxidant Activities, in vitro Gastrointestinal and Thermal Stability, and Hematoprotective Effects eFood Hematoprotection lipid peroxidation protein hydrolysate simulated gastrointestinal digestion stigma maydis thermal stability |
| title | Trypsin-hydrolyzed Corn Silk Proteins: Antioxidant Activities, in vitro Gastrointestinal and Thermal Stability, and Hematoprotective Effects |
| title_full | Trypsin-hydrolyzed Corn Silk Proteins: Antioxidant Activities, in vitro Gastrointestinal and Thermal Stability, and Hematoprotective Effects |
| title_fullStr | Trypsin-hydrolyzed Corn Silk Proteins: Antioxidant Activities, in vitro Gastrointestinal and Thermal Stability, and Hematoprotective Effects |
| title_full_unstemmed | Trypsin-hydrolyzed Corn Silk Proteins: Antioxidant Activities, in vitro Gastrointestinal and Thermal Stability, and Hematoprotective Effects |
| title_short | Trypsin-hydrolyzed Corn Silk Proteins: Antioxidant Activities, in vitro Gastrointestinal and Thermal Stability, and Hematoprotective Effects |
| title_sort | trypsin hydrolyzed corn silk proteins antioxidant activities in vitro gastrointestinal and thermal stability and hematoprotective effects |
| topic | Hematoprotection lipid peroxidation protein hydrolysate simulated gastrointestinal digestion stigma maydis thermal stability |
| url | https://www.atlantis-press.com/article/125937742/view |
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