Preparation, Isolation and Antioxidant Function of Peptides from a New Resource of <i>Rumexpatientia L.</i> ×<i>Rumextianshanicus A. Los</i>
<i>Rumexpatientia L.</i> ×<i>Rumextianshanicus A. Los</i> (RRL), known as “protein grass” in China, was recognized as a new food ingredient in 2021. However, the cultivation and product development of RRL are still at an early stage, and no peptide research has been reported....
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MDPI AG
2024-03-01
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Series: | Foods |
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Online Access: | https://www.mdpi.com/2304-8158/13/7/981 |
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author | Chang Liu Jianing Wang Dan Hong Zhou Chen Siting Li Aijin Ma Yingmin Jia |
author_facet | Chang Liu Jianing Wang Dan Hong Zhou Chen Siting Li Aijin Ma Yingmin Jia |
author_sort | Chang Liu |
collection | DOAJ |
description | <i>Rumexpatientia L.</i> ×<i>Rumextianshanicus A. Los</i> (RRL), known as “protein grass” in China, was recognized as a new food ingredient in 2021. However, the cultivation and product development of RRL are still at an early stage, and no peptide research has been reported. In this study, two novel antioxidant peptides, LKPPF and LPFRP, were purified and identified from RRL and applied to H<sub>2</sub>O<sub>2</sub>-induced HepG2 cells to investigate their antioxidant properties. It was shown that 121 peptides were identified by ultrafiltration, gel filtration chromatography, and LC-MS/MS, while computer simulation and molecular docking indicated that LKPPF and LPFRP may have strong antioxidant properties. Both peptides were not cytotoxic to HepG2 cells at low concentrations and promoted cell growth, which effectively reduced the production of intracellular ROS and MDA, and increased cell viability and the enzymatic activities of SOD, GSH-Px, and CAT. Therefore, LKPPF and LPFRP, two peptides, possess strong antioxidant activity, which provides a theoretical basis for their potential as food additives or functional food supplements, but still need to be further investigated through animal models as well as cellular pathways. |
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issn | 2304-8158 |
language | English |
last_indexed | 2024-04-24T10:46:03Z |
publishDate | 2024-03-01 |
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series | Foods |
spelling | doaj.art-e1ef37cd875244f8ae103486c44e50612024-04-12T13:18:22ZengMDPI AGFoods2304-81582024-03-0113798110.3390/foods13070981Preparation, Isolation and Antioxidant Function of Peptides from a New Resource of <i>Rumexpatientia L.</i> ×<i>Rumextianshanicus A. Los</i>Chang Liu0Jianing Wang1Dan Hong2Zhou Chen3Siting Li4Aijin Ma5Yingmin Jia6School of Food and Health, Beijing Technology and Business University, Beijing 100048, ChinaSchool of Food and Health, Beijing Technology and Business University, Beijing 100048, ChinaSchool of Food and Health, Beijing Technology and Business University, Beijing 100048, ChinaSchool of Food and Health, Beijing Technology and Business University, Beijing 100048, ChinaSchool of Food and Health, Beijing Technology and Business University, Beijing 100048, ChinaSchool of Food and Health, Beijing Technology and Business University, Beijing 100048, ChinaSchool of Food and Health, Beijing Technology and Business University, Beijing 100048, China<i>Rumexpatientia L.</i> ×<i>Rumextianshanicus A. Los</i> (RRL), known as “protein grass” in China, was recognized as a new food ingredient in 2021. However, the cultivation and product development of RRL are still at an early stage, and no peptide research has been reported. In this study, two novel antioxidant peptides, LKPPF and LPFRP, were purified and identified from RRL and applied to H<sub>2</sub>O<sub>2</sub>-induced HepG2 cells to investigate their antioxidant properties. It was shown that 121 peptides were identified by ultrafiltration, gel filtration chromatography, and LC-MS/MS, while computer simulation and molecular docking indicated that LKPPF and LPFRP may have strong antioxidant properties. Both peptides were not cytotoxic to HepG2 cells at low concentrations and promoted cell growth, which effectively reduced the production of intracellular ROS and MDA, and increased cell viability and the enzymatic activities of SOD, GSH-Px, and CAT. Therefore, LKPPF and LPFRP, two peptides, possess strong antioxidant activity, which provides a theoretical basis for their potential as food additives or functional food supplements, but still need to be further investigated through animal models as well as cellular pathways.https://www.mdpi.com/2304-8158/13/7/981<i>Rumexpatientia L.</i> ×<i>Rumextianshanicus A. Los</i>antioxidant peptidespurificationidentificationH<sub>2</sub>O<sub>2</sub>HepG2 |
spellingShingle | Chang Liu Jianing Wang Dan Hong Zhou Chen Siting Li Aijin Ma Yingmin Jia Preparation, Isolation and Antioxidant Function of Peptides from a New Resource of <i>Rumexpatientia L.</i> ×<i>Rumextianshanicus A. Los</i> Foods <i>Rumexpatientia L.</i> ×<i>Rumextianshanicus A. Los</i> antioxidant peptides purification identification H<sub>2</sub>O<sub>2</sub> HepG2 |
title | Preparation, Isolation and Antioxidant Function of Peptides from a New Resource of <i>Rumexpatientia L.</i> ×<i>Rumextianshanicus A. Los</i> |
title_full | Preparation, Isolation and Antioxidant Function of Peptides from a New Resource of <i>Rumexpatientia L.</i> ×<i>Rumextianshanicus A. Los</i> |
title_fullStr | Preparation, Isolation and Antioxidant Function of Peptides from a New Resource of <i>Rumexpatientia L.</i> ×<i>Rumextianshanicus A. Los</i> |
title_full_unstemmed | Preparation, Isolation and Antioxidant Function of Peptides from a New Resource of <i>Rumexpatientia L.</i> ×<i>Rumextianshanicus A. Los</i> |
title_short | Preparation, Isolation and Antioxidant Function of Peptides from a New Resource of <i>Rumexpatientia L.</i> ×<i>Rumextianshanicus A. Los</i> |
title_sort | preparation isolation and antioxidant function of peptides from a new resource of i rumexpatientia l i i rumextianshanicus a los i |
topic | <i>Rumexpatientia L.</i> ×<i>Rumextianshanicus A. Los</i> antioxidant peptides purification identification H<sub>2</sub>O<sub>2</sub> HepG2 |
url | https://www.mdpi.com/2304-8158/13/7/981 |
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