Extraction, identification, and molecular mechanisms of α-glucosidase inhibitory peptides from defatted Antarctic krill (Euphausia superba) powder hydrolysates
Copyright © 2024 Elsevier B.V. All rights reserved..
The objective of this study was to explore the potential of Antarctic krill-derived peptides as α-glucosidase inhibitors for the treatment of type 2 diabetes. The enzymolysis conditions of α-glucosidase inhibitory peptides were optimized by response surface methodology (RSM), a statistical method that efficiently determines optimal conditions with a limited number of experiments. Gel chromatography and LC-MS/MS techniques were utilized to determine the molecular weight (Mw) distribution and sequences of the hydrolysates. The identification and analysis of the mechanism behind α-glucosidase inhibitory peptides were conducted through conventional and computer-assisted techniques. The binding affinities between peptides and α-glucosidase were further validated using BLI (biolayer interferometry) assay. The results revealed that hydrolysates generated by neutrase exhibited the highest α-glucosidase inhibition rate. Optimal conditions for hydrolysis were determined to be an enzyme concentration of 6 × 103 U/g, hydrolysis time of 5.4 h, and hydrolysis temperature of 45 °C. Four peptides (LPFQR, PSFD, PSFDF, VPFPR) with strong binding affinities to the active site of α-glucosidase, primarily through hydrogen bonding and hydrophobic interactions. This study highlights the prospective utility of Antarctic krill-derived peptides in curtailing α-glucosidase activity, offering a theoretical foundation for the development of novel α-glucosidase inhibitors and related functional foods to enhance diabetes management.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:266 |
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| Enthalten in: |
International journal of biological macromolecules - 266(2024), Pt 2 vom: 23. März, Seite 131126 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Zheng, Kewei [VerfasserIn] |
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| Links: |
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| Themen: |
α-Glucosidase inhibitory rate |
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| Anmerkungen: |
Date Revised 04.04.2024 published: Print-Electronic Citation Status Publisher |
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| doi: |
10.1016/j.ijbiomac.2024.131126 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 520 | |a Copyright © 2024 Elsevier B.V. All rights reserved. | ||
| 520 | |a The objective of this study was to explore the potential of Antarctic krill-derived peptides as α-glucosidase inhibitors for the treatment of type 2 diabetes. The enzymolysis conditions of α-glucosidase inhibitory peptides were optimized by response surface methodology (RSM), a statistical method that efficiently determines optimal conditions with a limited number of experiments. Gel chromatography and LC-MS/MS techniques were utilized to determine the molecular weight (Mw) distribution and sequences of the hydrolysates. The identification and analysis of the mechanism behind α-glucosidase inhibitory peptides were conducted through conventional and computer-assisted techniques. The binding affinities between peptides and α-glucosidase were further validated using BLI (biolayer interferometry) assay. The results revealed that hydrolysates generated by neutrase exhibited the highest α-glucosidase inhibition rate. Optimal conditions for hydrolysis were determined to be an enzyme concentration of 6 × 103 U/g, hydrolysis time of 5.4 h, and hydrolysis temperature of 45 °C. Four peptides (LPFQR, PSFD, PSFDF, VPFPR) with strong binding affinities to the active site of α-glucosidase, primarily through hydrogen bonding and hydrophobic interactions. This study highlights the prospective utility of Antarctic krill-derived peptides in curtailing α-glucosidase activity, offering a theoretical foundation for the development of novel α-glucosidase inhibitors and related functional foods to enhance diabetes management | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Defatted Antarctic krill powder | |
| 650 | 4 | |a Molecular docking | |
| 650 | 4 | |a Peptides | |
| 650 | 4 | |a α-Glucosidase inhibitory rate | |
| 700 | 1 | |a Wu, Yuanyuan |e verfasserin |4 aut | |
| 700 | 1 | |a Dai, Qingfei |e verfasserin |4 aut | |
| 700 | 1 | |a Yan, Xiaojun |e verfasserin |4 aut | |
| 700 | 1 | |a Liu, Yu |e verfasserin |4 aut | |
| 700 | 1 | |a Sun, Di |e verfasserin |4 aut | |
| 700 | 1 | |a Yu, Zhongjie |e verfasserin |4 aut | |
| 700 | 1 | |a Jiang, Shuoqi |e verfasserin |4 aut | |
| 700 | 1 | |a Ma, Qingbao |e verfasserin |4 aut | |
| 700 | 1 | |a Jiang, Wei |e verfasserin |4 aut | |
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