Study on Fermentation Preparation, Stability, and Angiotensin-Converting Enzyme Inhibitory Activity of Tomato Pomace Peptide
The substantial quantity of discarded tomato pomace (TP) results in the waste of valuable resources. This study utilizes these tomato by-products by mixing them with water in a specific proportion and fermenting the mixture in two stages: first with yeast, and then with lactic acid bacteria. The mos...
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MDPI AG
2025-01-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/14/2/145 |
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| author | Ying Mu Ruxianguli Maimaitiyiming Jingyang Hong Yu Wang Yao Zhao Ruoqing Liu Liang Wang Keping Chen Aihemaitijiang Aihaiti |
| author_facet | Ying Mu Ruxianguli Maimaitiyiming Jingyang Hong Yu Wang Yao Zhao Ruoqing Liu Liang Wang Keping Chen Aihemaitijiang Aihaiti |
| author_sort | Ying Mu |
| collection | DOAJ |
| description | The substantial quantity of discarded tomato pomace (TP) results in the waste of valuable resources. This study utilizes these tomato by-products by mixing them with water in a specific proportion and fermenting the mixture in two stages: first with yeast, and then with lactic acid bacteria. The most suitable microbial strains for TP fermentation were identified by evaluating parameters such as peptide content, degree of hydrolysis, and gel electrophoresis analysis. Subsequently, tomato pomace peptides (TPPs) were separated into peptides of different molecular weights using ultrafiltration. The IC<sub>50</sub> values, ACE inhibitory activities, and in vitro stability of these peptides were compared, and their secondary structures and microstructures were characterized. The results indicated that the soluble protein concentration increased from 26.25 mg/g to 39.03 mg/g after 32 h of fermentation with strain <i>RV171</i>. After an additional 32 h of fermentation with <i>Bifidobacterium thermophilum</i>, the peptide content reached 49.18 ± 0.43%. SDS-PAGE gel electrophoresis showed that the TPP molecular weights were predominantly below 10 kDa. The IC<sub>50</sub> results demonstrated that fractions with smaller molecular weights exhibited greater ACE inhibitory activities. Structural analysis confirmed that the TP hydrolysate was indeed a peptide. |
| format | Article |
| id | doaj-art-38f78def75dd4be4a043f3092f965b29 |
| institution | Kabale University |
| issn | 2304-8158 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj-art-38f78def75dd4be4a043f3092f965b292025-01-24T13:32:38ZengMDPI AGFoods2304-81582025-01-0114214510.3390/foods14020145Study on Fermentation Preparation, Stability, and Angiotensin-Converting Enzyme Inhibitory Activity of Tomato Pomace PeptideYing Mu0Ruxianguli Maimaitiyiming1Jingyang Hong2Yu Wang3Yao Zhao4Ruoqing Liu5Liang Wang6Keping Chen7Aihemaitijiang Aihaiti8College of Life Science and Technology, Xinjiang University, Urumqi 830000, ChinaCollege of Life Science and Technology, Xinjiang University, Urumqi 830000, ChinaCollege of Life Science and Technology, Xinjiang University, Urumqi 830000, ChinaCollege of Life Science and Technology, Xinjiang University, Urumqi 830000, ChinaCollege of Life Science and Technology, Xinjiang University, Urumqi 830000, ChinaCollege of Life Science and Technology, Xinjiang University, Urumqi 830000, ChinaCollege of Life Science and Technology, Xinjiang University, Urumqi 830000, ChinaXinjiang Huize Food Limited Liability Company, Urumqi 830000, ChinaCollege of Life Science and Technology, Xinjiang University, Urumqi 830000, ChinaThe substantial quantity of discarded tomato pomace (TP) results in the waste of valuable resources. This study utilizes these tomato by-products by mixing them with water in a specific proportion and fermenting the mixture in two stages: first with yeast, and then with lactic acid bacteria. The most suitable microbial strains for TP fermentation were identified by evaluating parameters such as peptide content, degree of hydrolysis, and gel electrophoresis analysis. Subsequently, tomato pomace peptides (TPPs) were separated into peptides of different molecular weights using ultrafiltration. The IC<sub>50</sub> values, ACE inhibitory activities, and in vitro stability of these peptides were compared, and their secondary structures and microstructures were characterized. The results indicated that the soluble protein concentration increased from 26.25 mg/g to 39.03 mg/g after 32 h of fermentation with strain <i>RV171</i>. After an additional 32 h of fermentation with <i>Bifidobacterium thermophilum</i>, the peptide content reached 49.18 ± 0.43%. SDS-PAGE gel electrophoresis showed that the TPP molecular weights were predominantly below 10 kDa. The IC<sub>50</sub> results demonstrated that fractions with smaller molecular weights exhibited greater ACE inhibitory activities. Structural analysis confirmed that the TP hydrolysate was indeed a peptide.https://www.mdpi.com/2304-8158/14/2/145tomato pomacetwo-stage fermentationpeptidestabilitystructure characterizationACE inhibitory activity |
| spellingShingle | Ying Mu Ruxianguli Maimaitiyiming Jingyang Hong Yu Wang Yao Zhao Ruoqing Liu Liang Wang Keping Chen Aihemaitijiang Aihaiti Study on Fermentation Preparation, Stability, and Angiotensin-Converting Enzyme Inhibitory Activity of Tomato Pomace Peptide Foods tomato pomace two-stage fermentation peptide stability structure characterization ACE inhibitory activity |
| title | Study on Fermentation Preparation, Stability, and Angiotensin-Converting Enzyme Inhibitory Activity of Tomato Pomace Peptide |
| title_full | Study on Fermentation Preparation, Stability, and Angiotensin-Converting Enzyme Inhibitory Activity of Tomato Pomace Peptide |
| title_fullStr | Study on Fermentation Preparation, Stability, and Angiotensin-Converting Enzyme Inhibitory Activity of Tomato Pomace Peptide |
| title_full_unstemmed | Study on Fermentation Preparation, Stability, and Angiotensin-Converting Enzyme Inhibitory Activity of Tomato Pomace Peptide |
| title_short | Study on Fermentation Preparation, Stability, and Angiotensin-Converting Enzyme Inhibitory Activity of Tomato Pomace Peptide |
| title_sort | study on fermentation preparation stability and angiotensin converting enzyme inhibitory activity of tomato pomace peptide |
| topic | tomato pomace two-stage fermentation peptide stability structure characterization ACE inhibitory activity |
| url | https://www.mdpi.com/2304-8158/14/2/145 |
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