Structure characterization and mechanism of angiotensin I-converting enzyme (ACE) inhibitory peptides modified by plastein reaction derived from tiger nut (Cyperus esculentus)
The development of peptides derived from plants, which have potential anti-angiotensin converting enzyme (ACE) activity and other bioactivities, are of scientific interest. ACE inhibitory peptide (CLPP, the ACE inhibitory rate is 76.52 ± 1.07%) was obtained by hydrolysis of tiger nut (Cyperus escule...
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Frontiers Media S.A.
2025-01-01
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| Series: | Frontiers in Sustainable Food Systems |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fsufs.2024.1476134/full |
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| author | Junhua Shi Zhuo Yang Ming Xu Guogang Zhao Yawen Gao Hongyan Zheng Ji Feng |
| author_facet | Junhua Shi Zhuo Yang Ming Xu Guogang Zhao Yawen Gao Hongyan Zheng Ji Feng |
| author_sort | Junhua Shi |
| collection | DOAJ |
| description | The development of peptides derived from plants, which have potential anti-angiotensin converting enzyme (ACE) activity and other bioactivities, are of scientific interest. ACE inhibitory peptide (CLPP, the ACE inhibitory rate is 76.52 ± 1.07%) was obtained by hydrolysis of tiger nut (Cyperus esculentus) protein with alkaline protease. The plastein product (PCLPP, the ACE inhibitory rate is 85 ± 2.33%) was prepared by modifying CLPP with a plastein reaction. The results of SEM, IR, and XRD show that the structure of PCLPP is different from that of CLPP. The results of differential scanning calorimetry, fluorescence, and free amino analysis showed that the reaction was carried out by aggregation and condensation. These results suggest that the plastein reaction may be an effective method to increase the variety of bioactive peptides. |
| format | Article |
| id | doaj-art-2fc4ee1a4889440882b6afb827a219a2 |
| institution | DOAJ |
| issn | 2571-581X |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Sustainable Food Systems |
| spelling | doaj-art-2fc4ee1a4889440882b6afb827a219a22025-08-20T03:01:35ZengFrontiers Media S.A.Frontiers in Sustainable Food Systems2571-581X2025-01-01810.3389/fsufs.2024.14761341476134Structure characterization and mechanism of angiotensin I-converting enzyme (ACE) inhibitory peptides modified by plastein reaction derived from tiger nut (Cyperus esculentus)Junhua Shi0Zhuo Yang1Ming Xu2Guogang Zhao3Yawen Gao4Hongyan Zheng5Ji Feng6College of Food Science and Engineering, Jilin Agricultural University, Changchun, ChinaCollege of Food Science and Engineering, Jilin Agricultural University, Changchun, ChinaCollege of Food Science and Engineering, Jilin Agricultural University, Changchun, ChinaCybersecurity Academy, Changchun University, Changchun, ChinaCollege of Food Science and Engineering, Jilin Agricultural University, Changchun, ChinaCollege of Food Science and Engineering, Jilin Agricultural University, Changchun, ChinaJilin Province Product Quality Supervision and Inspection Institute, Changchun, ChinaThe development of peptides derived from plants, which have potential anti-angiotensin converting enzyme (ACE) activity and other bioactivities, are of scientific interest. ACE inhibitory peptide (CLPP, the ACE inhibitory rate is 76.52 ± 1.07%) was obtained by hydrolysis of tiger nut (Cyperus esculentus) protein with alkaline protease. The plastein product (PCLPP, the ACE inhibitory rate is 85 ± 2.33%) was prepared by modifying CLPP with a plastein reaction. The results of SEM, IR, and XRD show that the structure of PCLPP is different from that of CLPP. The results of differential scanning calorimetry, fluorescence, and free amino analysis showed that the reaction was carried out by aggregation and condensation. These results suggest that the plastein reaction may be an effective method to increase the variety of bioactive peptides.https://www.frontiersin.org/articles/10.3389/fsufs.2024.1476134/fullplastein reactiontrypsinpeptidesangiotensin converting enzymetiger nut |
| spellingShingle | Junhua Shi Zhuo Yang Ming Xu Guogang Zhao Yawen Gao Hongyan Zheng Ji Feng Structure characterization and mechanism of angiotensin I-converting enzyme (ACE) inhibitory peptides modified by plastein reaction derived from tiger nut (Cyperus esculentus) Frontiers in Sustainable Food Systems plastein reaction trypsin peptides angiotensin converting enzyme tiger nut |
| title | Structure characterization and mechanism of angiotensin I-converting enzyme (ACE) inhibitory peptides modified by plastein reaction derived from tiger nut (Cyperus esculentus) |
| title_full | Structure characterization and mechanism of angiotensin I-converting enzyme (ACE) inhibitory peptides modified by plastein reaction derived from tiger nut (Cyperus esculentus) |
| title_fullStr | Structure characterization and mechanism of angiotensin I-converting enzyme (ACE) inhibitory peptides modified by plastein reaction derived from tiger nut (Cyperus esculentus) |
| title_full_unstemmed | Structure characterization and mechanism of angiotensin I-converting enzyme (ACE) inhibitory peptides modified by plastein reaction derived from tiger nut (Cyperus esculentus) |
| title_short | Structure characterization and mechanism of angiotensin I-converting enzyme (ACE) inhibitory peptides modified by plastein reaction derived from tiger nut (Cyperus esculentus) |
| title_sort | structure characterization and mechanism of angiotensin i converting enzyme ace inhibitory peptides modified by plastein reaction derived from tiger nut cyperus esculentus |
| topic | plastein reaction trypsin peptides angiotensin converting enzyme tiger nut |
| url | https://www.frontiersin.org/articles/10.3389/fsufs.2024.1476134/full |
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