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

Method for preparing antioxidant peptides from oats by utilizing enzymatic membrane reactor

An enzyme membrane reactor, anti-oxidation peptide technology, applied in the preparation method of peptides, chemical instruments and methods, peptides, etc., can solve the problems of incompleteness and achieve good application prospects

Inactive Publication Date: 2011-10-12
BEIJING TECHNOLOGY AND BUSINESS UNIVERSITY
View PDF1 Cites 15 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, because the current understanding of the characteristics of the enzyme membrane reactor is not comprehensive enough, there are many problems that need to be further studied and solved.

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 preparing antioxidant peptides from oats by utilizing enzymatic membrane reactor
  • Method for preparing antioxidant peptides from oats by utilizing enzymatic membrane reactor
  • Method for preparing antioxidant peptides from oats by utilizing enzymatic membrane reactor

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0069] Embodiment 1, investigate the protease used for enzymatic hydrolysis oat gluten protein and enzymatic hydrolysis mode

[0070] (1) Determination of enzymatic hydrolysis index

[0071] First, a certain amount of oat gluten protein was weighed and placed in a constant temperature reactor, and the oat gluten protein was hydrolyzed according to the three protease hydrolysis conditions of Alcalase, Pepsin and Trypsin in Table 2. During the enzymolysis process, 1mol / L NaOH or Keep the pH value of the HCl solution constant, and record the consumption of NaOH or HCl solution. At the same time, take samples at 0min, 60min, 120min, 180min, and 240min, and place them in a boiling water bath for 15min to inactivate the enzyme and cool to room temperature. , adjust the pH value of the solution to the isoelectric point of oat gluten protein (pI=4.0), let it stand for 30min, centrifuge (10000r / min, 4°C, 10min), take the supernatant and adjust the pH value to 7.0; then, the The supern...

Embodiment 2

[0084] Embodiment 2, investigate the speed of Alcalase enzymolysis oat gluten protein

[0085] Studying the characteristics of Alcalase enzymatic hydrolysis of oat bran protein is a prerequisite for further optimizing the process of using Alcalase to prepare oat antioxidant peptides, and the enzymatic hydrolysis speed is the key to the study of Alcalase enzymatic hydrolysis characteristics of oat bran protein, because the speed of enzymatic hydrolysis It directly determines the feasibility of preparing antioxidant peptides by enzymatic membrane reactor. If the enzymatic hydrolysis of oat bran protein by Alcalase is too slow, oat bran protein will quickly form a gel layer on the membrane surface, and the membrane will be seriously polluted, resulting in enzymatic membrane reaction. The device stops working. Therefore, the rate of enzymatic hydrolysis was characterized by the consumption rate of NaOH, the effects of the size of the enzymatic hydrolysis system, the concentration ...

Embodiment 3

[0093] Embodiment 3, investigate the impact of enzyme membrane reactor system on enzyme activity

[0094] First, add 2500ml buffer solution (0.02mol / L pH value = 8.0 phosphate buffer) to the reaction tank, and add 12.5ml Alcalase, stir for 15min, take 5ml enzyme solution to measure its enzyme activity and absorbance at 280nm; then, turn off the ultra- Open the peristaltic pump at the permeate outlet of the filter membrane. The flow rate of the feed liquid is 25L / h. After 3 minutes of normal temperature and normal pressure circulation, open the outlet of the ultrafiltration membrane permeate and adjust the pressure to 0.01MPa. Add phosphate buffer solution to the system, record the amount added, open the pressure control valve, turn off the peristaltic pump, close the permeate outlet after each cycle for 60 minutes, measure the volume of the ultrafiltration membrane permeate, and measure its enzyme activity and 280nm Absorbance; Then, add the amount of buffer and permeate to 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 preparing antioxidant peptides from oats. Alcalase is determined to serve as the enzyme for preparation through investigating the antioxidant activities and yields of the products obtained by carrying out enzymolysis on the oat bran proteins with different proteases. Reduction of the enzymolysis speed of the Alcalase toward the oat bran proteins is determined to be mainly caused by substrate consumption and enzyme activity loss through investigating the enzymolysis speed of the Alcalase toward the oat bran proteins. Meanwhile, an enzymatic membrane reactorsystem is determined to have good retention effect on the Alcalase through studying the impact of the enzymatic membrane reactor system on the enzyme activity. The activity loss of the Alcalase is mainly caused by the damage to the enzyme in the operation process of a peristaltic pump and the adsorption of an ultrafiltration membrane toward the enzyme. By utilizing Design Expert 6.0.5 to design the response surface analysis experiment with four factors and three levels, the optimum process conditions under which the antioxidant peptides from oats can be prepared by utilizing the enzymatic membrane reactor are as follows: the substrate concentration is 3%; the enzyme addition is 3.2%; the feed flow rate is 45L / h; the operation pressure is 0.07MPa; the temperature is 55 DEG C; and the pH value is 7.3. Through verification, the DPPH scavenging rate of the products under the conditions can reach 57.39%.

Description

technical field [0001] The invention relates to a method for preparing oat antioxidant peptide by using an enzyme membrane reactor. Background technique [0002] Bioactive peptide is a general term for different peptides composed of 20 natural amino acids in different compositions and arrangements, ranging from dipeptides to complex linear and circular structures. It is the most complex multifunctional compound derived from proteins. It has human metabolism and Physiological adjustment function, high food safety, is the most popular research topic in the international food industry [1] . With the development of biological science and technology and the strengthening of people's awareness of health care, bioactive peptides have become the main development trend of the current pharmaceutical and health care products industry. In recent years, antioxidants have been vigorously developed at home and abroad, and their uses are becoming more and more extensive. They are not only...

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): C12P21/06C07K1/34
Inventor 任清张晓平郭项雨
Owner BEIJING TECHNOLOGY AND BUSINESS UNIVERSITY
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

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

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com