Exploring the Release of Elastin Peptides Generated from Enzymatic Hydrolysis of Bovine Elastin via Peptide Mapping
To enhance the understanding of enzymatic hydrolysis and to accelerate the discovery of key bioactive peptides within enzymatic products, this research focused on elastin as the substrate and investigated the variations in peptide profiles and the production of key bioactive peptides (those exceedin...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-11-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/28/22/7534 |
| _version_ | 1797458247735574528 |
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| author | Jianan Zhang Yang Liu Liwen Jiang Tiantian Zhao Guowan Su Mouming Zhao |
| author_facet | Jianan Zhang Yang Liu Liwen Jiang Tiantian Zhao Guowan Su Mouming Zhao |
| author_sort | Jianan Zhang |
| collection | DOAJ |
| description | To enhance the understanding of enzymatic hydrolysis and to accelerate the discovery of key bioactive peptides within enzymatic products, this research focused on elastin as the substrate and investigated the variations in peptide profiles and the production of key bioactive peptides (those exceeding 5% of the total) and their impacts on the biological activity of the hydrolysates. Through the application of advanced analytical techniques, such as stop-flow two-dimensional liquid chromatography and ultra-high-performance liquid chromatography-tandem mass spectrometry, the research tracks the release and profiles of peptides within elastin hydrolysates (EHs). Despite uniform peptide compositions, significant disparities in peptide concentrations were detected across the hydrolysates, hinting at varying levels of bioactive efficacy. A comprehensive identification process pinpointed 403 peptides within the EHs, with 18 peptides surpassing 5% in theoretical maximum content, signaling their crucial role in the hydrolysate’s bioactivity. Of particular interest, certain peptides containing sequences of alanine, valine, and glycine were released in higher quantities, suggesting Alcalase<sup>®</sup> 2.4L’s preference for these residues. The analysis not only confirms the peptides’ dose-responsive elastase inhibitory potential but also underscores the nuanced interplay between peptide content, biological function, and their collective synergy. The study sets the stage for future research aimed at refining enzymatic treatments to fully exploit the bioactive properties of elastin. |
| first_indexed | 2024-03-09T16:34:21Z |
| format | Article |
| id | doaj.art-7ba4de6473a349eeb4a8371b0f39c9de |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-09T16:34:21Z |
| publishDate | 2023-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-7ba4de6473a349eeb4a8371b0f39c9de2023-11-24T14:58:08ZengMDPI AGMolecules1420-30492023-11-012822753410.3390/molecules28227534Exploring the Release of Elastin Peptides Generated from Enzymatic Hydrolysis of Bovine Elastin via Peptide MappingJianan Zhang0Yang Liu1Liwen Jiang2Tiantian Zhao3Guowan Su4Mouming Zhao5School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, ChinaCollege of Food Science and Technology, Hunan Agricultural University, Changsha 410125, ChinaCollege of Food Science and Technology, Hunan Agricultural University, Changsha 410125, ChinaSericulture & Agri-Food Research Institute, Guangdong Academy of Agricultural Sciences, Key Laboratory of Functional Foods, Ministry of Agriculture and Rural Affairs, Guangdong Key Laboratory of Agricultural Products Processing, Guangzhou 510610, ChinaSchool of Food Science and Engineering, South China University of Technology, Guangzhou 510640, ChinaSchool of Food Science and Engineering, South China University of Technology, Guangzhou 510640, ChinaTo enhance the understanding of enzymatic hydrolysis and to accelerate the discovery of key bioactive peptides within enzymatic products, this research focused on elastin as the substrate and investigated the variations in peptide profiles and the production of key bioactive peptides (those exceeding 5% of the total) and their impacts on the biological activity of the hydrolysates. Through the application of advanced analytical techniques, such as stop-flow two-dimensional liquid chromatography and ultra-high-performance liquid chromatography-tandem mass spectrometry, the research tracks the release and profiles of peptides within elastin hydrolysates (EHs). Despite uniform peptide compositions, significant disparities in peptide concentrations were detected across the hydrolysates, hinting at varying levels of bioactive efficacy. A comprehensive identification process pinpointed 403 peptides within the EHs, with 18 peptides surpassing 5% in theoretical maximum content, signaling their crucial role in the hydrolysate’s bioactivity. Of particular interest, certain peptides containing sequences of alanine, valine, and glycine were released in higher quantities, suggesting Alcalase<sup>®</sup> 2.4L’s preference for these residues. The analysis not only confirms the peptides’ dose-responsive elastase inhibitory potential but also underscores the nuanced interplay between peptide content, biological function, and their collective synergy. The study sets the stage for future research aimed at refining enzymatic treatments to fully exploit the bioactive properties of elastin.https://www.mdpi.com/1420-3049/28/22/7534elastin peptides2D LC-MSpeptide fingerprintingenzymatic cleavage patternselastase inhibitory activity |
| spellingShingle | Jianan Zhang Yang Liu Liwen Jiang Tiantian Zhao Guowan Su Mouming Zhao Exploring the Release of Elastin Peptides Generated from Enzymatic Hydrolysis of Bovine Elastin via Peptide Mapping Molecules elastin peptides 2D LC-MS peptide fingerprinting enzymatic cleavage patterns elastase inhibitory activity |
| title | Exploring the Release of Elastin Peptides Generated from Enzymatic Hydrolysis of Bovine Elastin via Peptide Mapping |
| title_full | Exploring the Release of Elastin Peptides Generated from Enzymatic Hydrolysis of Bovine Elastin via Peptide Mapping |
| title_fullStr | Exploring the Release of Elastin Peptides Generated from Enzymatic Hydrolysis of Bovine Elastin via Peptide Mapping |
| title_full_unstemmed | Exploring the Release of Elastin Peptides Generated from Enzymatic Hydrolysis of Bovine Elastin via Peptide Mapping |
| title_short | Exploring the Release of Elastin Peptides Generated from Enzymatic Hydrolysis of Bovine Elastin via Peptide Mapping |
| title_sort | exploring the release of elastin peptides generated from enzymatic hydrolysis of bovine elastin via peptide mapping |
| topic | elastin peptides 2D LC-MS peptide fingerprinting enzymatic cleavage patterns elastase inhibitory activity |
| url | https://www.mdpi.com/1420-3049/28/22/7534 |
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