Angiotensin-converting enzyme inhibitory peptide and its preparation method and application

An angiotensin and inhibitory peptide technology, applied in the field of biomedicine, achieves the effects of reasonable process design, good application prospects, and strong operability

Active Publication Date: 2014-10-08
NANJING UNIVERSITY OF TRADITIONAL CHINESE MEDICINE
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, there is no report on the ACE inhibitory peptides derived from the four-cornered clam.

Method used

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  • Angiotensin-converting enzyme inhibitory peptide and its preparation method and application

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0023] A method for preparing an angiotensin-converting enzyme inhibitory peptide, comprising the following steps:

[0024] (1) Preparation of four-cornered clam hydrolyzate:

[0025] Wash the soft clam with four corners and add 3 times the amount of water to decoct twice, 45 minutes each time, separate the decoction liquid and meat dregs, and drain; take the meat dregs, add 3 times the amount of water to homogenize, and then add enzyme activity 30000U / g trypsin hydrolysis, the weight of trypsin added is 1.0% of the weight of meat dregs, the temperature of enzymolysis is 48 ℃, the pH of enzymolysis is 8.50, and the reaction time of enzymolysis is 2 h; Inactivate in a boiling water bath for 15 min, then centrifuge at 10,000 rpm, 4°C for 20 min, and take the supernatant;

[0026] (2) Purification by ultrafiltration:

[0027] Take the supernatant obtained from enzymatic hydrolysis in step (1), filter it with a 0.45 μm microporous filter membrane, and carry out ultrafiltration t...

Embodiment 2

[0030] Example 2 Sequence analysis of angiotensin-converting enzyme inhibitory peptide

[0031] Take the angiotensin-converting enzyme inhibitory peptide prepared in Example 1, and use ESI-Q TOF MS / MS to analyze the amino acid sequence of the polypeptide. The mass spectrometry conditions are: ESI source, scanning mode: positive ion mode, mass scanning range: 50-1000 m / z; The molecular weight of the active polypeptide obtained by analysis is 619.42 Da, and the mass spectrometry detection picture is as follows figure 1 As shown, the determined amino acid sequence is: Leu-Ala-Ser-Pro-Thr-Met.

Embodiment 3

[0032] Example 3 Synthesis of angiotensin-converting enzyme inhibitory peptide

[0033] According to the amino acid sequence obtained in Example 2, the angiotensin-converting enzyme inhibitory peptide Leu-Ala-Ser-Pro-Thr-Met was synthesized by solid-phase synthesis. The purity of the synthesized polypeptide was analyzed by HPLC to be 98%, and the mass spectrometry determined The molecular weight is 619.46 Da, which is consistent with the molecular weight of the purified polypeptide, and the fragments of the secondary mass spectrum are consistent with the fragments of the purified polypeptide.

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Abstract

The invention discloses an angiotensin-converting enzyme inhibitory peptide and its preparation method and application. The amino acid sequence of the inhibitory peptide is: Leu-Ala-Ser-Pro-Thr-Met. The present invention adopts modern biochemical technology means to track, screen and evaluate the active ingredients in clams that inhibit angiotensin-converting enzymes, and prepare them through enzymatic hydrolysis, ultrafiltration, reversed-phase high-performance liquid chromatography and other purification methods. The experimental results It shows that the inhibitory peptide has a good effect of inhibiting angiotensin-converting enzyme, has a good antihypertensive effect, and has good safety performance, and has a good application prospect.

Description

technical field [0001] The invention relates to an active polypeptide, in particular to a polypeptide with ACE-inhibiting activity isolated from an enzymatic hydrolyzate of clam molluscs, and belongs to the technical field of biomedicine. Background technique [0002] Angiotensin Converting Enzyme (ACE) is a zinc ion-dependent dipeptide carboxypeptidase that is widely present in mammalian tissues and can convert angiotensin Ⅰ (Angiotensin Ⅰ) into angiotensin Ⅱ ( Angiotensin Ⅱ), the latter is a strong vasoconstrictor, which promotes the increase of blood pressure; on the other hand, ACE can convert bradykinin, which has vasodilation effect, into an inactive fragment, inhibiting the antihypertensive system-activation Peptide release enzyme - kinin system (Kallikrein-Kinin System, KKS), also lead to increased blood pressure. Therefore, inhibiting the activity of ACE can relieve the increase of blood pressure and has the effect of treating hypertension. [0003] Modern researc...

Claims

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Application Information

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Patent Type & Authority Patents(China)
IPC IPC(8): C07K7/06C07K1/20C12P21/06A61K38/08A61P9/12
Inventor 刘睿吴皓朱蕴菡程建明卞慧敏王令充王欣之
Owner NANJING UNIVERSITY OF TRADITIONAL CHINESE MEDICINE
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