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Method for preparing antioxidant tripeptide from rice polypeptide and application

A technology of rice peptides and peptides, applied in the field of peptides, can solve problems such as destructive activity, adverse effects on product safety, and structural damage, and achieve the effects of simple preparation methods, good antioxidant activity, and product safety

Inactive Publication Date: 2019-04-05
INFINITUS (CHINA) CO LTD
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0005] At present, there are invention patents for enzymatically hydrolyzing rice protein to prepare rice polypeptide technology, but they all show certain deficiencies in different aspects: for example, they cannot maintain stability in the gastrointestinal tract, and the structure is destroyed before absorption and loses activity; during the preparation process Especially in the drying process, the destroyed activity is affected; the extraction reagent in the extraction process has adverse effects on product safety

Method used

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  • Method for preparing antioxidant tripeptide from rice polypeptide and application
  • Method for preparing antioxidant tripeptide from rice polypeptide and application
  • Method for preparing antioxidant tripeptide from rice polypeptide and application

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0049] The enzymolysis of embodiment 1 rice protein

[0050] 1. Enzyme hydrolysis:

[0051] 1. Enzymatic hydrolysis of flavored protein: rice protein was prepared into a solution with a concentration of 100mg / mL with distilled water as a solvent, added flavored protease to 0.75wt%, temperature 50°C, pH 6.0, after enzymolysis for 4 hours, use a boiling water bath to inactivate the enzyme, and centrifuge at 8000rpm After 20 minutes, the supernatant was concentrated and freeze-dried to obtain polypeptide A.

[0052] 2. Simulated gastric digestion: Polypeptide A was prepared into a solution with a concentration of 100 mg / mL by using distilled water as a solvent, adding pepsin to 1.7% wt%, temperature 37°C, pH 1.5, enzymatic hydrolysis for 1.5 hours, and using a boiling water bath to inactivate the enzyme. Centrifuge at 8000rpm for 20min, and the supernatant is concentrated and freeze-dried to obtain polypeptide B.

[0053] 3. Simulated gastrointestinal digestion: After enzymatic...

Embodiment 2

[0064] Embodiment 2 cellulose glass column purification

[0065] A DEAE-52 cellulose glass column (1.6×30 cm) was pre-equilibrated with distilled water. The rice polypeptide prepared in Example 1 was prepared into a solution with a concentration of 50 mg / mL in distilled water, and loaded on the DEAE-52 column.

[0066] Take 200 mL of distilled water and 200 mL of NaCl solutions with concentrations of 0.05 mol / L, 0.1 mol / L, 0.2 mol / L and 0.4 mol / L for gradient elution at a flow rate of 0.5 mL / min. Collect each fraction eluted and monitor at 214nm, collect the purified product as Figure 2a shown.

[0067] The six fractions obtained (F1, F2, F3, F4, F5 and F6) were collected, each fraction was freeze-dried, and their ORAC antioxidant activity was measured. The ORAC test results of each component are as follows Figure 2b As shown, the ORAC value of component F1 was 4.412±0.161, which was significantly higher than other components, so F1 was further purified.

Embodiment 3

[0068] Embodiment 3 Sephadex column purification

[0069] A Sephadex G-15 column (1.6 x 60 cm) was pre-equilibrated with distilled water. The polypeptide F1 prepared in Example 3 was prepared into a solution with a concentration of 30 mg / mL with distilled water, and loaded onto a well-balanced Sephadex G-15 column for further purification. Fractions were eluted with distilled water at a flow rate of 0.5 mL / min, and each eluted fraction was collected and then detected at 214 nm.

[0070] The results of the secondary purification are as follows Figure 2c As shown, F1 obtained three fractions (F1-a, F1-b, F1-c) through secondary purification, and this purification method can effectively separate the components of rice polypeptide; the ORAC detection results of each component are as follows: Figure 2d As shown, the ORAC value of wherein component F1-a is 6.815 ± 0.298, is significantly higher than other other components, and the rice polypeptide oxygen free radical absorption ...

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Abstract

The invention relates to the technical field of polypeptide, in particular to a method for preparing antioxidant tripeptide from rice polypeptide and application. The antioxidant peptide provided by the invention and prepared from the rice polypeptide contains three kinds of tripeptides including Ser-Ile-Arg, Ser-Leu-Arg and Val-Pro-Arg. During the preparation of the antioxidant tripeptide, enzymolysis, cellulose glass column purification and dextran gel column purification are sequentially performed; the antioxidant tripeptide can resist the gastro-intestinal digestion; the ORAC (Oxygen Radical Absorption Capacity) is high; the result shows that the antioxidant tripeptide has high anti-oxidization activity. The preparation method of the polypeptide is simple; a harmful reagent is not needed; the obtained product is safer.

Description

technical field [0001] The invention relates to the technical field of polypeptides, in particular to a method and application for preparing antioxidant tripeptides from rice polypeptides. Background technique [0002] Rice is the largest grain variety in my country, with an annual output of about 200 million tons, accounting for about 30% of the total grain planting area in the world. Rice protein is considered as a high-quality protein because of its high bioavailability, reasonable amino acid composition, and unique hypoallergenicity. Compared with milk and bean protein, it is more suitable for feed, infants, the elderly, and special groups . But for a long time, my country's rice processing has only been in the primary processing state to meet people's ration needs. The rice processing product structure is single, the deep processing rate is only 20%, and there are few high value-added products. [0003] Peptides are the most active, most absorbable, and highly functio...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C07K5/083C07K1/16C12P21/06A61K38/07A61P39/06A23L33/18
CPCA23L33/18A23V2002/00A61K38/00A61P39/06C07K5/0808C07K5/081C12P21/06A23V2200/30
Inventor 梁明尹西拳任娇艳
Owner INFINITUS (CHINA) CO LTD
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