Bibliographic Details
| Title: |
Preparation, Identification, and Enzyme Inhibition Kinetic Analysis of Phosvitin α-Amylase Inhibitory Peptides |
| Authors: |
Tianrui XUE, Binfei LÜ, Mingran ZHANG, Can LI, Xiaowei ZHANG |
| Source: |
Shipin gongye ke-ji, Vol 46, Iss 1, Pp 152-162 (2025) |
| Publisher Information: |
The editorial department of Science and Technology of Food Industry, 2025. |
| Publication Year: |
2025 |
| Collection: |
LCC:Food processing and manufacture |
| Subject Terms: |
phosvitin phosphopeptide, complex enzymatic hydrolysis, α-amylase inhibitors, molecular docking, enzyme inhibition kinetics, Food processing and manufacture, TP368-456 |
| More Details: |
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 |
| Document Type: |
article |
| File Description: |
electronic resource |
| Language: |
Chinese |
| ISSN: |
1002-0306 |
| Relation: |
https://doaj.org/toc/1002-0306 |
| DOI: |
10.13386/j.issn1002-0306.2024010363 |
| Access URL: |
https://doaj.org/article/c6311a03e35a4b6384eee09016768309 |
| Accession Number: |
edsdoj.6311a03e35a4b6384eee09016768309 |
| Database: |
Directory of Open Access Journals |
