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Structural Identification and Antioxidant Activity of Loach Protein Enzymatic Hydrolysates

Loach, rich in nutrients, such as proteins, amino acids, and mineral elements, is being gradually favored by consumers. Therefore, in this study, the antioxidant activity and structural characteristics of loach peptides were comprehensively analyzed. The loach protein (LAP) with a molecular weight b...

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Autores principales: Mao, Jinrong, Li, Shunqin, Yun, Liyuan, Zhang, Min
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10254627/
https://www.ncbi.nlm.nih.gov/pubmed/37298867
http://dx.doi.org/10.3390/molecules28114391
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author Mao, Jinrong
Li, Shunqin
Yun, Liyuan
Zhang, Min
author_facet Mao, Jinrong
Li, Shunqin
Yun, Liyuan
Zhang, Min
author_sort Mao, Jinrong
collection PubMed
description Loach, rich in nutrients, such as proteins, amino acids, and mineral elements, is being gradually favored by consumers. Therefore, in this study, the antioxidant activity and structural characteristics of loach peptides were comprehensively analyzed. The loach protein (LAP) with a molecular weight between 150 and 3000 Da was graded by ultrafiltration and nanofiltration processes, which exhibited excellent scavenging activity against DPPH radical (IC50 2.91 ± 0.02 mg/mL), hydroxyl radical (IC50 9.95 ± 0.03 mg/mL), and superoxide anion radical (IC50 13.67 ± 0.33 mg/mL). Additionally, LAP was purified by gel filtration chromatography, and two principal components (named as LAP-I and LAP-II) were isolated. A total of 582 and 672 peptides were identified in LAP-I and LAP-II, respectively, through structural analysis. The XRD results revealed that LAP-I and LAP-II had an irregular amorphous structure. The 2D-NMR spectroscopy results suggested that LAP-I had a compact stretch conformation in the D(2)O solution, while LAP-II had a folded conformation. Overall, the study results suggested that loach peptide could be a potential antioxidant agent and might provide valuable information for chain conformation and antioxidant mechanism research further.
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spelling pubmed-102546272023-06-10 Structural Identification and Antioxidant Activity of Loach Protein Enzymatic Hydrolysates Mao, Jinrong Li, Shunqin Yun, Liyuan Zhang, Min Molecules Article Loach, rich in nutrients, such as proteins, amino acids, and mineral elements, is being gradually favored by consumers. Therefore, in this study, the antioxidant activity and structural characteristics of loach peptides were comprehensively analyzed. The loach protein (LAP) with a molecular weight between 150 and 3000 Da was graded by ultrafiltration and nanofiltration processes, which exhibited excellent scavenging activity against DPPH radical (IC50 2.91 ± 0.02 mg/mL), hydroxyl radical (IC50 9.95 ± 0.03 mg/mL), and superoxide anion radical (IC50 13.67 ± 0.33 mg/mL). Additionally, LAP was purified by gel filtration chromatography, and two principal components (named as LAP-I and LAP-II) were isolated. A total of 582 and 672 peptides were identified in LAP-I and LAP-II, respectively, through structural analysis. The XRD results revealed that LAP-I and LAP-II had an irregular amorphous structure. The 2D-NMR spectroscopy results suggested that LAP-I had a compact stretch conformation in the D(2)O solution, while LAP-II had a folded conformation. Overall, the study results suggested that loach peptide could be a potential antioxidant agent and might provide valuable information for chain conformation and antioxidant mechanism research further. MDPI 2023-05-28 /pmc/articles/PMC10254627/ /pubmed/37298867 http://dx.doi.org/10.3390/molecules28114391 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Mao, Jinrong
Li, Shunqin
Yun, Liyuan
Zhang, Min
Structural Identification and Antioxidant Activity of Loach Protein Enzymatic Hydrolysates
title Structural Identification and Antioxidant Activity of Loach Protein Enzymatic Hydrolysates
title_full Structural Identification and Antioxidant Activity of Loach Protein Enzymatic Hydrolysates
title_fullStr Structural Identification and Antioxidant Activity of Loach Protein Enzymatic Hydrolysates
title_full_unstemmed Structural Identification and Antioxidant Activity of Loach Protein Enzymatic Hydrolysates
title_short Structural Identification and Antioxidant Activity of Loach Protein Enzymatic Hydrolysates
title_sort structural identification and antioxidant activity of loach protein enzymatic hydrolysates
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10254627/
https://www.ncbi.nlm.nih.gov/pubmed/37298867
http://dx.doi.org/10.3390/molecules28114391
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