Evaluation of the binding affinity and antioxidant activity of phlorizin to pepsin and trypsin
Phlorizin (PHL) is a natural compound with strong antioxidant properties mainly found in apples. In this paper, the interaction mechanism of PHL with pepsin and trypsin was comparatively evaluated by computer simulation, fluorescence spectra, circular dichroism (CD), and fourier transform infrared (...
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| Format: | Article |
| Language: | English |
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Tsinghua University Press
2024-01-01
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| Series: | Food Science and Human Wellness |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213453023001192 |
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| author | Jing Zhang Di Wu Lan Tang Xia Hu Zhen Zeng Wen Wu Fang Geng Hui Li |
| author_facet | Jing Zhang Di Wu Lan Tang Xia Hu Zhen Zeng Wen Wu Fang Geng Hui Li |
| author_sort | Jing Zhang |
| collection | DOAJ |
| description | Phlorizin (PHL) is a natural compound with strong antioxidant properties mainly found in apples. In this paper, the interaction mechanism of PHL with pepsin and trypsin was comparatively evaluated by computer simulation, fluorescence spectra, circular dichroism (CD), and fourier transform infrared (FT-IR) spectra at a molecular level. Fluorescence spectra showed that PHL quenches the pepsin/trypsin by static quenching. Thermodynamic parameters indicated that PHL binds to pepsin mainly through hydrogen bonds and van der Waals forces, and that of trypsin was electrostatic forces. The ground state complexes PHL and protease have a moderate affinity of 105 L/mol PHL binds more strongly to trypsin than to pepsin. CD and FT-IR spectra results showed that pepsin/trypsin decreased the β-sheet content and slightly changed its secondary structure upon PHL. These experimental results are mutually verified with the predicted computer-aid simulation results. Upon PHL and trypsin binding, the antioxidant capacity of PHL was elevated. Nevertheless, the antioxidant capacity of PHL was decreased after binding to pepsin. This work elucidates the binding of PHL binding mechanisms to pepsin/trypsin and provides useful information for the digestion of PHL to improve the application of PHL in food processing. |
| format | Article |
| id | doaj-art-9b4e7ade497a4da5b058bcc87948ef96 |
| institution | Kabale University |
| issn | 2213-4530 |
| language | English |
| publishDate | 2024-01-01 |
| publisher | Tsinghua University Press |
| record_format | Article |
| series | Food Science and Human Wellness |
| spelling | doaj-art-9b4e7ade497a4da5b058bcc87948ef962025-02-03T05:54:06ZengTsinghua University PressFood Science and Human Wellness2213-45302024-01-01131392400Evaluation of the binding affinity and antioxidant activity of phlorizin to pepsin and trypsinJing Zhang0Di Wu1Lan Tang2Xia Hu3Zhen Zeng4Wen Wu5Fang Geng6Hui Li7Meat Processing Key Laboratory of Sichuan Province, School of Food and Biological Engineering, Chengdu University, Chengdu 610106, ChinaMeat Processing Key Laboratory of Sichuan Province, School of Food and Biological Engineering, Chengdu University, Chengdu 610106, China; Corresponding author at: Meat Processing Key Laboratory of Sichuan Province, School of Food and Biological Engineering, Chengdu University, Chengdu, Sichuan, China.Meat Processing Key Laboratory of Sichuan Province, School of Food and Biological Engineering, Chengdu University, Chengdu 610106, ChinaMeat Processing Key Laboratory of Sichuan Province, School of Food and Biological Engineering, Chengdu University, Chengdu 610106, ChinaMeat Processing Key Laboratory of Sichuan Province, School of Food and Biological Engineering, Chengdu University, Chengdu 610106, ChinaMeat Processing Key Laboratory of Sichuan Province, School of Food and Biological Engineering, Chengdu University, Chengdu 610106, ChinaMeat Processing Key Laboratory of Sichuan Province, School of Food and Biological Engineering, Chengdu University, Chengdu 610106, ChinaSchool of Chemical Engineering, Sichuan University, Chengdu 610065, ChinaPhlorizin (PHL) is a natural compound with strong antioxidant properties mainly found in apples. In this paper, the interaction mechanism of PHL with pepsin and trypsin was comparatively evaluated by computer simulation, fluorescence spectra, circular dichroism (CD), and fourier transform infrared (FT-IR) spectra at a molecular level. Fluorescence spectra showed that PHL quenches the pepsin/trypsin by static quenching. Thermodynamic parameters indicated that PHL binds to pepsin mainly through hydrogen bonds and van der Waals forces, and that of trypsin was electrostatic forces. The ground state complexes PHL and protease have a moderate affinity of 105 L/mol PHL binds more strongly to trypsin than to pepsin. CD and FT-IR spectra results showed that pepsin/trypsin decreased the β-sheet content and slightly changed its secondary structure upon PHL. These experimental results are mutually verified with the predicted computer-aid simulation results. Upon PHL and trypsin binding, the antioxidant capacity of PHL was elevated. Nevertheless, the antioxidant capacity of PHL was decreased after binding to pepsin. This work elucidates the binding of PHL binding mechanisms to pepsin/trypsin and provides useful information for the digestion of PHL to improve the application of PHL in food processing.http://www.sciencedirect.com/science/article/pii/S2213453023001192InteractionPhlorizinPepsinTrypsinAntioxidation |
| spellingShingle | Jing Zhang Di Wu Lan Tang Xia Hu Zhen Zeng Wen Wu Fang Geng Hui Li Evaluation of the binding affinity and antioxidant activity of phlorizin to pepsin and trypsin Food Science and Human Wellness Interaction Phlorizin Pepsin Trypsin Antioxidation |
| title | Evaluation of the binding affinity and antioxidant activity of phlorizin to pepsin and trypsin |
| title_full | Evaluation of the binding affinity and antioxidant activity of phlorizin to pepsin and trypsin |
| title_fullStr | Evaluation of the binding affinity and antioxidant activity of phlorizin to pepsin and trypsin |
| title_full_unstemmed | Evaluation of the binding affinity and antioxidant activity of phlorizin to pepsin and trypsin |
| title_short | Evaluation of the binding affinity and antioxidant activity of phlorizin to pepsin and trypsin |
| title_sort | evaluation of the binding affinity and antioxidant activity of phlorizin to pepsin and trypsin |
| topic | Interaction Phlorizin Pepsin Trypsin Antioxidation |
| url | http://www.sciencedirect.com/science/article/pii/S2213453023001192 |
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