Method for separating and purifying ACE inhibition peptide from rice draff and active peptide obtained therefor

A technology of inhibiting activity and rice grains, applied in the field of bioengineering and protein chemistry, to achieve the effect of simple method, excellent product sensory and high protein content

Inactive Publication Date: 2007-08-01
ZHEJIANG UNIV
View PDF1 Cites 9 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0005] The above research results show that the ACE inhibitory activity has an important relationship with the properties of the C-terminal and N-term

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Method for separating and purifying ACE inhibition peptide from rice draff and active peptide obtained therefor
  • Method for separating and purifying ACE inhibition peptide from rice draff and active peptide obtained therefor

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0035] Example 1: Sephadex G-15 was used to separate and prepare the hydrolysate of rice grains to obtain the separated components:

[0036] In the separation process, the present invention uses a 160cm (length)×30mm chromatography column, the detection wavelength is 280nm, and the eluent is distilled water. The eluent flow rate is 0.5ml / min, and the sample volume is 25-30ml, according to the wavelength value OD in the nucleic acid protein detection instrument 280 Change the collection of samples. According to the above given operating conditions, short peptides with ACE inhibitory activity can be collected.

[0037]As can be seen from Figure 1, the proteolysate of rice grains is separated into six distinct polypeptide components after separation by Sephadex G-15, which are named FI, F-II, F-III, and F respectively. -IV, FV, F-VI. The peak areas of components FI, F-II, F-III, F-IV, FV, and F-VI separated by Sephadex G-15 are 36.08%, 45.93%, 7.98%, and 2.13%, respectively. , 3.03%,...

Embodiment 2

[0043] Example 2: Study and comparison of the half inhibitory concentration (IC50) of the ACE inhibitory activity of the separated components of Sephadex G-15 from rice grains proteolysis:

[0044] Raw materials: The method described in Example 1 was used to obtain the gel separation components of the rice grains proteolysate as the research raw materials.

[0045] In order to accurately describe the ACE inhibitory activity of components F-I, F-II, F-III, F-IV, F-V, F-VI, the half-inhibitory concentration (IC 50 ). The measurement results are shown in Figure 2. It can be seen from Figure 2 that the half-inhibitory concentration (IC) of the ACE inhibitory activity of the separated components F-I, F-II, F-III, F-IV, F-V, and F-VI 50 ) Are 0.502g / mL, 0.171mg / mL, 0.041mg / mL, 0.019mg / mL, 0.011mg / mL, 0.017mg / mL, respectively. These data indicate that F-III, F-IV, F-V, and F-VI have higher ACE inhibitory activity; among them, the component with the highest ACE inhibitory activity is F-V,...

Embodiment 3

[0049] Example 3: Chromatographic separation of F-V components separated by Sephadex G-15 from rice grains proteolysate and preparation of reversed-phase high performance liquid chromatography:

[0050] In order to further ascertain the component F-V with high angiotensin-converting enzyme (ACE) inhibitory activity, reversed-phase high performance liquid chromatography was used to separate and analyze F-V, as follows:

[0051] In this implementation, the Sephadex G-15 separation component F-V of the proteolytic product is vacuum freeze-dried to form a freeze-dried powder. The process conditions of freeze-drying are: temperature -45°C and vacuum degree 20Pa.

[0052] Then dissolve the above lyophilized powder in distilled water to make a solution with a concentration of 5mg lyophilized powder / mL, and use C 18 Reversed-phase high performance liquid chromatography was separated and analyzed. The chromatographic conditions are as follows:

[0053] Chromatographic column: C18P / N84176 (...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

PUM

No PUM Login to view more

Abstract

The invention discloses a method for separating and purifying ACE inhibiting active peptide from rice dregs, taking rice dregs protein substrate as raw material. It comprises following steps: (1) separating rice dregs protein substrate with dextran gel Sephadex G-15 and getting separted component; testing ACE inhibiting activity for each got component; (2) vacuum cooling and drying the component with highest test value for ACE inhibiting activity to prepare freeze powder, dissloving freeze powder into distilled water to prepare solution with concentration being 5 mg freeze powder/ ml, separating said solution though inverse high efficiency liquid chromatography, and getting purified ACE inhibiting active peptide with the chromatogram peak value being the largest. The molecular weight of produced product is 645.3, and the primary structure of its amino acid is Phe-Asn-Gly-Phe-Tyr. The invention is characterized by easy device, simple process, good repeatability and wide application.

Description

Technical field [0001] The invention belongs to the fields of bioengineering and protein chemistry, and relates to a method for separating and purifying ACE inhibitory active peptides from rice grains, and an ACE inhibitory active peptide prepared by the method. Background technique [0002] With the improvement of people's living standards and the enhancement of self-protection awareness and safety awareness, non-drug therapy can not only achieve the purpose of curing diseases, but also avoid the damage of synthetic drugs to the human body, so it has been accepted by more and more people. . Hypertension is a common and frequently-occurring disease. The number of people suffering from hypertension in the world has exceeded 500 million. At the same time, hypertension is the most important factor in coronary heart disease, heart and kidney failure. Therefore, treatment of hypertension has become a global medical issue. Hard task. At present, there are more than 16 kinds of angioten...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

Application Information

Patent Timeline
no application Login to view more
IPC IPC(8): C07K1/16C07K7/06A61K38/08A61P9/12
Inventor 何国庆陈启和玄国栋阮晖
Owner ZHEJIANG UNIV
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap