Identifying Endogenous Proteins of Perennial Ryegrass (<i>Lolium perenne</i>) with <i>Ex Vivo</i> Antioxidant Activity
<b>Background</b>: During the initial steps of green biorefining aimed at protein recovery, endogenous proteins and enzymes, along with, e.g., phytochemical constituents, are decompartmentalized into a green juice. This creates a highly dynamic environment prone to a plethora of reaction...
Saved in:
| Main Authors: | , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-02-01
|
| Series: | Proteomes |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2227-7382/13/1/8 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1849339841443004416 |
|---|---|
| author | Kathrine Danner Aakjær Pedersen Line Thopholm Andersen Mads Heiselberg Camilla Agerskov Brigsted Freja Lyngs Støvring Louise Mailund Mikkelsen Sofie Albrekt Hansen Christian Enrico Rusbjerg-Weberskov Mette Lübeck Simon Gregersen Echers |
| author_facet | Kathrine Danner Aakjær Pedersen Line Thopholm Andersen Mads Heiselberg Camilla Agerskov Brigsted Freja Lyngs Støvring Louise Mailund Mikkelsen Sofie Albrekt Hansen Christian Enrico Rusbjerg-Weberskov Mette Lübeck Simon Gregersen Echers |
| author_sort | Kathrine Danner Aakjær Pedersen |
| collection | DOAJ |
| description | <b>Background</b>: During the initial steps of green biorefining aimed at protein recovery, endogenous proteins and enzymes, along with, e.g., phytochemical constituents, are decompartmentalized into a green juice. This creates a highly dynamic environment prone to a plethora of reactions including oxidative protein modification and deterioration. Obtaining a fundamental understanding of the enzymes capable of exerting antioxidant activity <i>ex vivo</i> could help mitigate these reactions for improved product quality. <b>Methods</b>: In this study, we investigated perennial ryegrass (<i>Lolium perenne</i> var. Abosan 1), one of the most widely used turf and forage grasses, as a model system. Using size exclusion chromatography, we fractionated the green juice to investigate <i>in vitro</i> antioxidant properties and coupled this with quantitative bottom-up proteomics, GO-term analysis, and fraction-based enrichment. <b>Results</b>: Our findings revealed that several enzymes, such as superoxide dismutase and peroxiredoxin proteoforms, already known for their involvement in <i>in vivo</i> oxidative protection, are enriched in fractions displaying increased <i>in vitro</i> antioxidant activity, indicating retained activity <i>ex vivo</i>. Moreover, this study provides the most detailed characterization of the <i>L. perenne</i> proteome today and delivers new insights into protein-level partitioning during wet fractionation. <b>Conclusions</b>: Ultimately, this work contributes to a better understanding of the first steps of green biorefining and provides the basis for process optimization. |
| format | Article |
| id | doaj-art-6297e52e0b5a43afb63d3393baa8cb34 |
| institution | Kabale University |
| issn | 2227-7382 |
| language | English |
| publishDate | 2025-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Proteomes |
| spelling | doaj-art-6297e52e0b5a43afb63d3393baa8cb342025-08-20T03:44:02ZengMDPI AGProteomes2227-73822025-02-01131810.3390/proteomes13010008Identifying Endogenous Proteins of Perennial Ryegrass (<i>Lolium perenne</i>) with <i>Ex Vivo</i> Antioxidant ActivityKathrine Danner Aakjær Pedersen0Line Thopholm Andersen1Mads Heiselberg2Camilla Agerskov Brigsted3Freja Lyngs Støvring4Louise Mailund Mikkelsen5Sofie Albrekt Hansen6Christian Enrico Rusbjerg-Weberskov7Mette Lübeck8Simon Gregersen Echers9Department of Chemistry & Bioscience, Aalborg University, Fredrik Bajers Vej 7H, DK-9220 Aalborg, DenmarkDepartment of Chemistry & Bioscience, Aalborg University, Fredrik Bajers Vej 7H, DK-9220 Aalborg, DenmarkDepartment of Chemistry & Bioscience, Aalborg University, Fredrik Bajers Vej 7H, DK-9220 Aalborg, DenmarkDepartment of Chemistry & Bioscience, Aalborg University, Fredrik Bajers Vej 7H, DK-9220 Aalborg, DenmarkDepartment of Chemistry & Bioscience, Aalborg University, Fredrik Bajers Vej 7H, DK-9220 Aalborg, DenmarkDepartment of Chemistry & Bioscience, Aalborg University, Fredrik Bajers Vej 7H, DK-9220 Aalborg, DenmarkDepartment of Chemistry & Bioscience, Aalborg University, Fredrik Bajers Vej 7H, DK-9220 Aalborg, DenmarkDepartment of Chemistry & Bioscience, Aalborg University, Fredrik Bajers Vej 7H, DK-9220 Aalborg, DenmarkDepartment of Chemistry & Bioscience, Aalborg University, Fredrik Bajers Vej 7H, DK-9220 Aalborg, DenmarkDepartment of Chemistry & Bioscience, Aalborg University, Fredrik Bajers Vej 7H, DK-9220 Aalborg, Denmark<b>Background</b>: During the initial steps of green biorefining aimed at protein recovery, endogenous proteins and enzymes, along with, e.g., phytochemical constituents, are decompartmentalized into a green juice. This creates a highly dynamic environment prone to a plethora of reactions including oxidative protein modification and deterioration. Obtaining a fundamental understanding of the enzymes capable of exerting antioxidant activity <i>ex vivo</i> could help mitigate these reactions for improved product quality. <b>Methods</b>: In this study, we investigated perennial ryegrass (<i>Lolium perenne</i> var. Abosan 1), one of the most widely used turf and forage grasses, as a model system. Using size exclusion chromatography, we fractionated the green juice to investigate <i>in vitro</i> antioxidant properties and coupled this with quantitative bottom-up proteomics, GO-term analysis, and fraction-based enrichment. <b>Results</b>: Our findings revealed that several enzymes, such as superoxide dismutase and peroxiredoxin proteoforms, already known for their involvement in <i>in vivo</i> oxidative protection, are enriched in fractions displaying increased <i>in vitro</i> antioxidant activity, indicating retained activity <i>ex vivo</i>. Moreover, this study provides the most detailed characterization of the <i>L. perenne</i> proteome today and delivers new insights into protein-level partitioning during wet fractionation. <b>Conclusions</b>: Ultimately, this work contributes to a better understanding of the first steps of green biorefining and provides the basis for process optimization.https://www.mdpi.com/2227-7382/13/1/8perennial ryegrassgreen biorefiningwet fractionationantioxidant activitysize fractionationbottom-up proteomics |
| spellingShingle | Kathrine Danner Aakjær Pedersen Line Thopholm Andersen Mads Heiselberg Camilla Agerskov Brigsted Freja Lyngs Støvring Louise Mailund Mikkelsen Sofie Albrekt Hansen Christian Enrico Rusbjerg-Weberskov Mette Lübeck Simon Gregersen Echers Identifying Endogenous Proteins of Perennial Ryegrass (<i>Lolium perenne</i>) with <i>Ex Vivo</i> Antioxidant Activity Proteomes perennial ryegrass green biorefining wet fractionation antioxidant activity size fractionation bottom-up proteomics |
| title | Identifying Endogenous Proteins of Perennial Ryegrass (<i>Lolium perenne</i>) with <i>Ex Vivo</i> Antioxidant Activity |
| title_full | Identifying Endogenous Proteins of Perennial Ryegrass (<i>Lolium perenne</i>) with <i>Ex Vivo</i> Antioxidant Activity |
| title_fullStr | Identifying Endogenous Proteins of Perennial Ryegrass (<i>Lolium perenne</i>) with <i>Ex Vivo</i> Antioxidant Activity |
| title_full_unstemmed | Identifying Endogenous Proteins of Perennial Ryegrass (<i>Lolium perenne</i>) with <i>Ex Vivo</i> Antioxidant Activity |
| title_short | Identifying Endogenous Proteins of Perennial Ryegrass (<i>Lolium perenne</i>) with <i>Ex Vivo</i> Antioxidant Activity |
| title_sort | identifying endogenous proteins of perennial ryegrass i lolium perenne i with i ex vivo i antioxidant activity |
| topic | perennial ryegrass green biorefining wet fractionation antioxidant activity size fractionation bottom-up proteomics |
| url | https://www.mdpi.com/2227-7382/13/1/8 |
| work_keys_str_mv | AT kathrinedanneraakjærpedersen identifyingendogenousproteinsofperennialryegrassiloliumperenneiwithiexvivoiantioxidantactivity AT linethopholmandersen identifyingendogenousproteinsofperennialryegrassiloliumperenneiwithiexvivoiantioxidantactivity AT madsheiselberg identifyingendogenousproteinsofperennialryegrassiloliumperenneiwithiexvivoiantioxidantactivity AT camillaagerskovbrigsted identifyingendogenousproteinsofperennialryegrassiloliumperenneiwithiexvivoiantioxidantactivity AT frejalyngsstøvring identifyingendogenousproteinsofperennialryegrassiloliumperenneiwithiexvivoiantioxidantactivity AT louisemailundmikkelsen identifyingendogenousproteinsofperennialryegrassiloliumperenneiwithiexvivoiantioxidantactivity AT sofiealbrekthansen identifyingendogenousproteinsofperennialryegrassiloliumperenneiwithiexvivoiantioxidantactivity AT christianenricorusbjergweberskov identifyingendogenousproteinsofperennialryegrassiloliumperenneiwithiexvivoiantioxidantactivity AT mettelubeck identifyingendogenousproteinsofperennialryegrassiloliumperenneiwithiexvivoiantioxidantactivity AT simongregersenechers identifyingendogenousproteinsofperennialryegrassiloliumperenneiwithiexvivoiantioxidantactivity |