Novel Antioxidant Peptides from <i>Grateloupia livida</i> Hydrolysates: Purification and Identification
<i>Grateloupia livida</i> protein was hydrolyzed with various proteases (alkaline protease, Protamex and neutral protease) to obtain anti-oxidative peptides. Antioxidant activity of the enzymatic hydrolysates was evaluated by the DPPH radical scavenging, ABTS radical scavenging and reduc...
Main Authors: | , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2022-05-01
|
Series: | Foods |
Subjects: | |
Online Access: | https://www.mdpi.com/2304-8158/11/10/1498 |
_version_ | 1797499924220215296 |
---|---|
author | Xiao Hu Chuang Pan Miaomiao Cai Laihao Li Xianqing Yang Huan Xiang Shengjun Chen |
author_facet | Xiao Hu Chuang Pan Miaomiao Cai Laihao Li Xianqing Yang Huan Xiang Shengjun Chen |
author_sort | Xiao Hu |
collection | DOAJ |
description | <i>Grateloupia livida</i> protein was hydrolyzed with various proteases (alkaline protease, Protamex and neutral protease) to obtain anti-oxidative peptides. Antioxidant activity of the enzymatic hydrolysates was evaluated by the DPPH radical scavenging, ABTS radical scavenging and reducing power assays. The results suggested that hydrolysates obtained by neutral protease 1 h hydrolysis displayed the highest antioxidant activity (DPPH IC<sub>50</sub> value of 3.96 mg/mL ± 0.41 mg/mL, ABTS IC<sub>50</sub> value of 0.88 ± 0.13 mg/mL and reducing power of 0.531 ± 0.012 at 8 mg/mL), and had low molecular weight distribution (almost 99% below 3 kDa). Three fractions (F1–F3) were then isolated from the hydrolysates by using semi-preparative RP-HPLC, and the fraction F3 showed the highest antioxidant ability. Four antioxidant peptides were identified as LYEEMKESKVINADK, LEADNVGVVLMGDGR, LIDDSFGTDAPVPERL, and GLDELSEEDRLT from the F3 by LC-MS/MS. Online prediction showed that the four peptides possessed good water solubility, non-toxic and non-allergenic characteristics. Moreover, the LYEEMKESKVINADK exhibited the highest antioxidant ability. Molecular docking revealed that these peptides could all well bind with Kelch-like ECH-associated protein 1 (Keap1), among which LYEEMKESKVINADK had the lowest docking energy (−216.878 kcal/mol). These results demonstrated that the antioxidant peptides from <i>Grateloupia livida</i> could potentially be used as natural antioxidant. |
first_indexed | 2024-03-10T03:54:26Z |
format | Article |
id | doaj.art-ba9ca32308fc488394508e4c69d06e17 |
institution | Directory Open Access Journal |
issn | 2304-8158 |
language | English |
last_indexed | 2024-03-10T03:54:26Z |
publishDate | 2022-05-01 |
publisher | MDPI AG |
record_format | Article |
series | Foods |
spelling | doaj.art-ba9ca32308fc488394508e4c69d06e172023-11-23T11:00:01ZengMDPI AGFoods2304-81582022-05-011110149810.3390/foods11101498Novel Antioxidant Peptides from <i>Grateloupia livida</i> Hydrolysates: Purification and IdentificationXiao Hu0Chuang Pan1Miaomiao Cai2Laihao Li3Xianqing Yang4Huan Xiang5Shengjun Chen6Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, ChinaKey Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, ChinaKey Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, ChinaKey Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, ChinaKey Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, ChinaKey Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, ChinaKey Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China<i>Grateloupia livida</i> protein was hydrolyzed with various proteases (alkaline protease, Protamex and neutral protease) to obtain anti-oxidative peptides. Antioxidant activity of the enzymatic hydrolysates was evaluated by the DPPH radical scavenging, ABTS radical scavenging and reducing power assays. The results suggested that hydrolysates obtained by neutral protease 1 h hydrolysis displayed the highest antioxidant activity (DPPH IC<sub>50</sub> value of 3.96 mg/mL ± 0.41 mg/mL, ABTS IC<sub>50</sub> value of 0.88 ± 0.13 mg/mL and reducing power of 0.531 ± 0.012 at 8 mg/mL), and had low molecular weight distribution (almost 99% below 3 kDa). Three fractions (F1–F3) were then isolated from the hydrolysates by using semi-preparative RP-HPLC, and the fraction F3 showed the highest antioxidant ability. Four antioxidant peptides were identified as LYEEMKESKVINADK, LEADNVGVVLMGDGR, LIDDSFGTDAPVPERL, and GLDELSEEDRLT from the F3 by LC-MS/MS. Online prediction showed that the four peptides possessed good water solubility, non-toxic and non-allergenic characteristics. Moreover, the LYEEMKESKVINADK exhibited the highest antioxidant ability. Molecular docking revealed that these peptides could all well bind with Kelch-like ECH-associated protein 1 (Keap1), among which LYEEMKESKVINADK had the lowest docking energy (−216.878 kcal/mol). These results demonstrated that the antioxidant peptides from <i>Grateloupia livida</i> could potentially be used as natural antioxidant.https://www.mdpi.com/2304-8158/11/10/1498<i>Grateloupia livida</i>hydrolysatesantioxidant peptidespurificationidentification |
spellingShingle | Xiao Hu Chuang Pan Miaomiao Cai Laihao Li Xianqing Yang Huan Xiang Shengjun Chen Novel Antioxidant Peptides from <i>Grateloupia livida</i> Hydrolysates: Purification and Identification Foods <i>Grateloupia livida</i> hydrolysates antioxidant peptides purification identification |
title | Novel Antioxidant Peptides from <i>Grateloupia livida</i> Hydrolysates: Purification and Identification |
title_full | Novel Antioxidant Peptides from <i>Grateloupia livida</i> Hydrolysates: Purification and Identification |
title_fullStr | Novel Antioxidant Peptides from <i>Grateloupia livida</i> Hydrolysates: Purification and Identification |
title_full_unstemmed | Novel Antioxidant Peptides from <i>Grateloupia livida</i> Hydrolysates: Purification and Identification |
title_short | Novel Antioxidant Peptides from <i>Grateloupia livida</i> Hydrolysates: Purification and Identification |
title_sort | novel antioxidant peptides from i grateloupia livida i hydrolysates purification and identification |
topic | <i>Grateloupia livida</i> hydrolysates antioxidant peptides purification identification |
url | https://www.mdpi.com/2304-8158/11/10/1498 |
work_keys_str_mv | AT xiaohu novelantioxidantpeptidesfromigrateloupialividaihydrolysatespurificationandidentification AT chuangpan novelantioxidantpeptidesfromigrateloupialividaihydrolysatespurificationandidentification AT miaomiaocai novelantioxidantpeptidesfromigrateloupialividaihydrolysatespurificationandidentification AT laihaoli novelantioxidantpeptidesfromigrateloupialividaihydrolysatespurificationandidentification AT xianqingyang novelantioxidantpeptidesfromigrateloupialividaihydrolysatespurificationandidentification AT huanxiang novelantioxidantpeptidesfromigrateloupialividaihydrolysatespurificationandidentification AT shengjunchen novelantioxidantpeptidesfromigrateloupialividaihydrolysatespurificationandidentification |