JP-7855350-B2 - Celenium chelate pea oligopeptide and its preparation method and uses

Inventors

• サイ、 ムイ
• マ、 ヨンキン
• チェン、 リアン
• ル、 ル
• チャン、 ハイシン
• ウェイ、 イン
• リウ、 ヤン
• チャオ、 ケル
• ワン、 ジン
• リ、 グオミン
• チョウ、 ミン
• グ、 ルイゼン
• ワン、 ユチェン
• ワン、 ユキン
• リン、 コン
• ビ、 ユアン
• ツゥイ、 シンユエ
• ル、 ジュン
• リウ、 ウェニン
• キン、 シュウユアン
• パン、 シンチャン
• ドン、 ツェ
• マ、 ヨン
• シュ、 ヤグアン

Assignees

• チャイナ ナショナル リサーチ インスティテュート オブ フード アンド ファーメンテーション インダストリーズ カンパニー リミテッド

Dates

Publication Date

20260508

Application Date

20181218

Priority Date

20181012

Claims (5)

1. A selen chelate pea oligopeptide, wherein the selen chelate pea oligopeptide contains a peptide fragment PPKIYP in a mass content of 25 ng/mg or more , and the selen chelate pea oligopeptide is A method using pepsin and performing hydrolysis for 4 hours under conditions of a pH of 2 and a temperature of 37°C. A method using trypsin and hydrolysis performed for 6 hours under conditions of a pH of 7.5 and a temperature of 37°C. After at least one of three digestion methods—one in which the temperature is kept constant at 37°C, hydrolysis is performed for 4 hours using pepsin under conditions where the pH value is 2, and then hydrolysis is performed for another 6 hours using trypsin under conditions where the pH value is 6.8—the selenium content after digestion does not change by more than 3% compared to the selenium content before digestion. The aforementioned selenium chelate pea oligopeptide has an acid-soluble protein content higher than 23%, a total nitrogen content higher than 23%, and components with a molecular weight of less than 1000u account for 85% or more, and a selenium content of 0.08 g/100 g or more. The method for preparing the selen chelate pea oligopeptide includes reacting a mixed system of an aqueous solution of pea oligopeptide and sodium selenite at a temperature of 60 to 90°C for 20 minutes or more, and subjecting the resulting reaction product to alcohol precipitation and drying to obtain the selen chelate pea oligopeptide. The aforementioned mixed system has a mass ratio of pea oligopeptide to sodium selenite of 1 to 5:1. The method for preparing the pea oligopeptide is as follows: A selenium chelate pea oligopeptide is characterized by mixing pea protein powder with water in a material-to-liquid ratio of 1:8 to 12, adjusting the pH of the material liquid to 8 to 10, controlling the temperature to 40 to 60°C, adding alkaline protease and neutral protease for enzymatic decomposition, with the dosage of both enzymes being 1.0 to 3.0% of the mass of the pea protein powder, the enzymatic decomposition time being 3 to 6 hours, the pea oligopeptide containing more than 80% of components with a molecular weight less than 1000u, and the mass concentration of the pea oligopeptide in the aqueous solution of the pea oligopeptide being 1 to 5 g/100 mL .
2. The selenium chelate pea oligopeptide according to claim 1, characterized in that, after heat treatment at 100°C or below for 2 hours, the selenium content is 97% or more of the content before heat treatment.
3. The selenium chelate pea oligopeptide is characterized in that, after being subjected to acid-base treatment for 2 hours under conditions of pH 3 to 11 and temperature 37°C, the selenium content is 75% or more of that before the acid-base treatment, as described in claim 1 or 2.
4. A method for preparing selen chelate pea oligopeptide, comprising reacting an aqueous solution of pea oligopeptide with sodium selenite in a mixed system at 60 to 90°C for 20 minutes or more, and subjecting the resulting reaction product to alcohol precipitation and drying to obtain the selen chelate pea oligopeptide. The aforementioned mixed system has a mass ratio of pea oligopeptide to sodium selenite of 1 to 5:1. The aforementioned selen chelate pea oligopeptide contains the peptide fragment PPKIYP in a mass content of 25 ng/mg or more . The aforementioned selenium chelate pea oligopeptide has an acid-soluble protein content higher than 23%, a total nitrogen content higher than 23%, and components with a molecular weight of less than 1000u account for 85% or more, and a selenium content of 0.08 g/100 g or more. The method for preparing the pea oligopeptide is as follows: A method for preparing selenium chelate pea oligopeptide, characterized by mixing pea protein powder with water in a material-to-liquid ratio of 1:8 to 12, adjusting the pH of the material liquid to 8 to 10, controlling the temperature to 40 to 60°C, adding alkaline protease and neutral protease for enzymatic decomposition, administering the two enzymes in amounts of 1.0 to 3.0% of the mass of the pea protein powder, having an enzymatic decomposition time of 3 to 6 hours, the pea oligopeptide containing more than 80% of components with a molecular weight less than 1000u, and having an aqueous solution of the pea oligopeptide with a mass concentration of 1 to 5 g/100 mL .
5. A method for using the selenium chelate pea oligopeptide described in any one of claims 1 to 3 in a healthcare food.

Description

This invention relates to selenium chelate pea oligopeptides , methods for preparing them, and their uses, and more particularly to selenium chelate pea oligopeptides that are highly stable, effectively absorbed by humans, and have excellent antioxidant properties, as well as their manufacturing techniques and uses. According to traditional metabolic models, proteins are hydrolyzed into amino acids before being absorbed and utilized by organisms. However, recent research suggests that animals' protein needs also depend on a certain amount of small molecule active peptides. Furthermore, it has been demonstrated that oligopeptides have dedicated carriers and absorption pathways in the human gut, allowing them to enter the small intestine and be absorbed in their complete form. Pea oligopeptides are small peptide molecules obtained after enzymatic degradation or hydrolysis of pea proteins. It has already been reported that pea oligopeptides are physiologically active peptides with a wide range of applications, possessing antibacterial, antioxidant, and ACE inhibitory activities. Selenium is one of the trace elements that humans must obtain from the outside world, and it plays a crucial role in maintaining human life activities. Research has shown that selenium deficiency can weaken the human immune system and potentially cause diseases such as Keshan disease. Currently, in addition to normal food intake, a common method of selenium supplementation is the oral administration of inorganic selenium, such as sodium selenite. However, research has shown that organic selenium is less toxic and has a higher absorption rate than inorganic selenium. As a result, there has been a surge in research reports on related oligopeptide selenium-based organic selenium products such as soy peptide selenium chelate, reishi mushroom peptide selenium chelate, and fish head protein peptide selenium chelate. However, there are few reports on pea oligopeptides or selenium chelation. While introducing selenium into oligopeptide molecules and using the resulting oligopeptide selenium (usually called chelated selenium) directly as a product to ensure effective selenium supplementation, or using oligopeptide selenium as an intermediate raw material for further processing to guarantee the expected effects of subsequent processing, both are noteworthy issues in this type of product research. However, selenium-chelated pea oligopeptides that are effectively absorbed by humans and stably combined are even rarer. This is a diagram of the selenium standard curve drawn to measure the selenium content of the present invention.This is a gel chromatogram showing the molecular weight distribution of the selen chelate pea oligopeptide in Example 1 of the present invention.This is a full-wavelength ultraviolet scan diagram of pea oligopeptide and selenium chelate pea oligopeptide in Example 1 of the present invention.This is a scanning electron microscope image (×1000) of the pea oligopeptide and the selenium chelate pea oligopeptide in Example 1 of the present invention.This is an infrared spectral diagram of pea oligopeptide and selen chelate pea oligopeptide in Example 1 of the present invention.This figure shows the selenium content of selenium chelate pea oligopeptide treated under different temperature conditions in Example 1 of the present invention.This figure shows the selenium content of selenium chelate pea oligopeptide treated under different acid-base conditions in Example 1 of the present invention.This is the selenium content of the selenium chelate pea oligopeptide treated with different digestion methods in Example 1 of the present invention.This is a comparative diagram of DPPH free radical removal using selen chelate pea oligopeptide and its synthesis raw materials in Example 1 of the present invention.This is a comparison chart of DPPH free radical removal by VC.This is a comparative diagram of OH free radical removal using selen chelate pea oligopeptide and its synthesis raw materials in Example 1 of the present invention.This is a comparison diagram of OH free radical removal by VC.This is a comparative diagram of the reducing ability of selen chelate pea oligopeptide and its synthesis raw materials in Example 1 of the present invention.This is a comparison chart of VC reduction capabilities.This is the primary mass spectrum diagram of the peptide fragment TGRGAP.This is a secondary mass spectral diagram of the peptide fragment TGRGAP.This is the primary mass spectral diagram of the peptide fragment PPKIYP.This is a secondary mass spectral diagram of the peptide fragment PPKIYP.This is the primary mass spectrum diagram of the peptide fragment HQMPKP.This is a secondary mass spectral diagram of the peptide fragment HQMPKP.This is the primary mass spectral diagram of the peptide fragment TSSLP.This is a secondary mass spectral diagram of the peptide fragment TSSLP.This is a mass spectral diagram of the synthetic peptide fragment TG