Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Method for screening hypoglycemic peptide for inhibiting activity of alpha-amylase

An amylase and blood sugar-lowering technology, which is applied in the field of screening peptides that inhibit α-amylase activity and lower blood sugar, to achieve the effects of reducing interference, improving efficiency, and improving magnetic enzyme activity

Pending Publication Date: 2021-06-25
KUNMING UNIV OF SCI & TECH
View PDF4 Cites 3 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0005] The purpose of the present invention is to address the shortcomings of screening active ingredients from complex compounds, and propose a method for enriching and screening hypoglycemic peptides using magnetically immobilized amylase combined with high-performance liquid phase technology, which can increase the number of anti-α-amylase-activating hypoglycemic peptides screened and targeting, to achieve efficient and specific separation and detection of trace blood sugar-lowering active ingredients; using the prepared magnetically immobilized amylase, it can quickly and effectively screen hypoglycemic peptides that inhibit α-amylase activity, which is more effective for magnetic enzymes Provide technical support for the ground isolation of hypoglycemic active ingredients

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 screening hypoglycemic peptide for inhibiting activity of alpha-amylase
  • Method for screening hypoglycemic peptide for inhibiting activity of alpha-amylase
  • Method for screening hypoglycemic peptide for inhibiting activity of alpha-amylase

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0031] (1) Press Fe 3 o 4 The ratio of the mass volume ratio of nanoparticles to the mixed solution is 1:10, the Fe 3 o 4 Nanoparticles were suspended in a mixed solution of ethanol and ammonia water (the volume ratio of ethanol and ammonia water was 9:1), sonicated for 30 min, and 300 µL tetramethoxysilane (TMOS) was added to 10 mL of the suspension to shake for 8 h. Repeated washing with ion water 3 times, vacuum drying overnight at 60°C to obtain Fe 3 o 4 @SiO 2 ; 3 o 4 @SiO 2 The infrared spectrum of figure 2As shown in (b), new absorption peaks appear at 802cm−1 and 1096cm−1, which are the bending vibration peaks of Si—OH in the silicon layer and the opposition of Si—O—Si in the silicon layer, respectively. Called stretching peaks, these signals confirm that the silane polymer is bound to the Fe 3 o 4 on the surface of magnetic particles.

[0032] (2) 100 mg of Fe obtained in step (1) 3 o 4 @SiO 2 The particles were suspended in 50mL of isopropanol, and th...

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 screening a hypoglycemic peptide for inhibiting activity of alpha-amylase, and belongs to the field of preparation and purification of bioactive peptides. According to the method, the tea seed meal proteolysis alpha-amylase activity inhibiting hypoglycemic peptide is rapidly enriched, separated and purified by combining magnetic separation of the magnetic immobilized alpha-amylase with a high performance liquid chromatography technology. The magnetic immobilized alpha-amylase is adopted to enrich the hypoglycemic peptide for inhibiting the activity of the alpha-amylase, the invention has the advantages of good specificity, rapidness and high efficiency, the magnetic enzyme can be reused, and another technical support is provided for quantitative detection of the hypoglycemic peptide. The cost is low, the operation is simple, and the practicability is very high. The new source of the hypoglycemic active peptide is increased, the full utilization of byproducts is realized, and the method has great potential in the aspect of developing functional food with hypoglycemic activity.

Description

technical field [0001] The invention relates to a method for screening a hypoglycemic peptide that inhibits alpha-amylase activity, and belongs to the field of bioactive peptide preparation. Background technique [0002] α-amylase (1,4-α-D-glucan-glucanohydrolase) is a very important enzyme in the digestion process of carbohydrates in food. By inhibiting its activity, glucose and maltose The production and absorption of the drug are slowed down to achieve the purpose of lowering postprandial blood sugar, thereby reducing the damage to the body of diabetic patients in a high-sugar environment, and effectively preventing and improving complications. α-amylase inhibitors can strictly control the rise of postprandial blood sugar, and are an important means of treating type 2 diabetes; a large number of studies have shown that glycosidase inhibitors play an important role in the treatment and prevention of diabetes. [0003] Bioactive peptides have a variety of biological functi...

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): C12P21/06C07K1/36C07K1/34C07K1/16C07K17/02C12N11/14G01N30/02G01N30/06G01N30/14G01N30/88A23L33/18A61K38/01A61P3/10
CPCC12P21/06C07K1/36C07K1/34C07K1/16C07K17/02C12N11/14C12N9/2414G01N30/02G01N30/06G01N30/14G01N30/88A23L33/18A61K38/01A61P3/10C12Y302/01001G01N2030/027A23V2002/00A23V2200/328A23V2250/55
Inventor 李莉蓉刘欢杨振光韩兴
Owner KUNMING UNIV OF SCI & TECH
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products