Preparation, Identification, and Enzyme Inhibition Kinetic Analysis of Phosvitin α-Amylase Inhibitory Peptides
To explore the inhibiting effect of phosvitin phosphopeptide (PPP) on α-amylase, enabling it to regulate blood glucose levels and alleviate type Ⅱ diabetes mellitus. This study employed enzymatic hydrolysis of phosvitin with the inhibition rate of α-amylase as an index, followed by enzyme inhibition...
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The editorial department of Science and Technology of Food Industry
2025-01-01
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| Series: | Shipin gongye ke-ji |
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| Online Access: | http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2024010363 |
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| author | Tianrui XUE Binfei LÜ Mingran ZHANG Can LI Xiaowei ZHANG |
| author_facet | Tianrui XUE Binfei LÜ Mingran ZHANG Can LI Xiaowei ZHANG |
| author_sort | Tianrui XUE |
| collection | DOAJ |
| description | To explore the inhibiting effect of phosvitin phosphopeptide (PPP) on α-amylase, enabling it to regulate blood glucose levels and alleviate type Ⅱ diabetes mellitus. This study employed enzymatic hydrolysis of phosvitin with the inhibition rate of α-amylase as an index, followed by enzyme inhibition kinetics experiments to analyze the inhibitory type of PPP on α-amylase. LC-MS identification was conducted, and molecular docking was performed to screen for highly active α-amylase inhibitory peptides, which were subsequently validated. The results showed that optimal enzymatic hydrolysis conditions involved initial hydrolysis with trypsin (7000 U/g), followed by pepsin (60000 U/g) for 6 h each. The prepared PPP exhibited the highest α-amylase inhibition rate 70.69%±1.71% at a concentration of 7.81×10−3 mg/mL. PPP acted as a mixed-type inhibitor. Two novel highly active α-amylase inhibitory peptides FGTEPDAK and IWGR were identified and screened, exhibiting IC50 values of (0.80±0.14)×10−3 mg/mL and (1.80±0.31)×10−3 mg/mL, respectively. Both extremely significantly lower than the positive control acarbose's IC50 value (3.17±0.47)×10−3 mg/mL (P<0.01). This study highlights the potential use of PPP as a new hypoglycemic substance in developing functional foods for alleviating type Ⅱ diabetes mellitus. |
| format | Article |
| id | doaj-art-c6311a03e35a4b6384eee09016768309 |
| institution | Kabale University |
| issn | 1002-0306 |
| language | zho |
| publishDate | 2025-01-01 |
| publisher | The editorial department of Science and Technology of Food Industry |
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| series | Shipin gongye ke-ji |
| spelling | doaj-art-c6311a03e35a4b6384eee090167683092025-01-10T06:49:17ZzhoThe editorial department of Science and Technology of Food IndustryShipin gongye ke-ji1002-03062025-01-0146115216210.13386/j.issn1002-0306.20240103632024010363-1Preparation, Identification, and Enzyme Inhibition Kinetic Analysis of Phosvitin α-Amylase Inhibitory PeptidesTianrui XUE0Binfei LÜ1Mingran ZHANG2Can LI3Xiaowei ZHANG4College of Food Science and Engineering, Tianjin University of Science & Technology, Tianjin 300457, ChinaCollege of Food Science and Engineering, Tianjin University of Science & Technology, Tianjin 300457, ChinaCollege of Food Science and Engineering, Tianjin University of Science & Technology, Tianjin 300457, ChinaCollege of Food Science and Engineering, Tianjin University of Science & Technology, Tianjin 300457, ChinaCollege of Food Science and Engineering, Tianjin University of Science & Technology, Tianjin 300457, ChinaTo explore the inhibiting effect of phosvitin phosphopeptide (PPP) on α-amylase, enabling it to regulate blood glucose levels and alleviate type Ⅱ diabetes mellitus. This study employed enzymatic hydrolysis of phosvitin with the inhibition rate of α-amylase as an index, followed by enzyme inhibition kinetics experiments to analyze the inhibitory type of PPP on α-amylase. LC-MS identification was conducted, and molecular docking was performed to screen for highly active α-amylase inhibitory peptides, which were subsequently validated. The results showed that optimal enzymatic hydrolysis conditions involved initial hydrolysis with trypsin (7000 U/g), followed by pepsin (60000 U/g) for 6 h each. The prepared PPP exhibited the highest α-amylase inhibition rate 70.69%±1.71% at a concentration of 7.81×10−3 mg/mL. PPP acted as a mixed-type inhibitor. Two novel highly active α-amylase inhibitory peptides FGTEPDAK and IWGR were identified and screened, exhibiting IC50 values of (0.80±0.14)×10−3 mg/mL and (1.80±0.31)×10−3 mg/mL, respectively. Both extremely significantly lower than the positive control acarbose's IC50 value (3.17±0.47)×10−3 mg/mL (P<0.01). This study highlights the potential use of PPP as a new hypoglycemic substance in developing functional foods for alleviating type Ⅱ diabetes mellitus.http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2024010363phosvitin phosphopeptidecomplex enzymatic hydrolysisα-amylase inhibitorsmolecular dockingenzyme inhibition kinetics |
| spellingShingle | Tianrui XUE Binfei LÜ Mingran ZHANG Can LI Xiaowei ZHANG Preparation, Identification, and Enzyme Inhibition Kinetic Analysis of Phosvitin α-Amylase Inhibitory Peptides Shipin gongye ke-ji phosvitin phosphopeptide complex enzymatic hydrolysis α-amylase inhibitors molecular docking enzyme inhibition kinetics |
| title | Preparation, Identification, and Enzyme Inhibition Kinetic Analysis of Phosvitin α-Amylase Inhibitory Peptides |
| title_full | Preparation, Identification, and Enzyme Inhibition Kinetic Analysis of Phosvitin α-Amylase Inhibitory Peptides |
| title_fullStr | Preparation, Identification, and Enzyme Inhibition Kinetic Analysis of Phosvitin α-Amylase Inhibitory Peptides |
| title_full_unstemmed | Preparation, Identification, and Enzyme Inhibition Kinetic Analysis of Phosvitin α-Amylase Inhibitory Peptides |
| title_short | Preparation, Identification, and Enzyme Inhibition Kinetic Analysis of Phosvitin α-Amylase Inhibitory Peptides |
| title_sort | preparation identification and enzyme inhibition kinetic analysis of phosvitin α amylase inhibitory peptides |
| topic | phosvitin phosphopeptide complex enzymatic hydrolysis α-amylase inhibitors molecular docking enzyme inhibition kinetics |
| url | http://www.spgykj.com/cn/article/doi/10.13386/j.issn1002-0306.2024010363 |
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