China National Research Institute of Food and Fermentation Industries

China National Research Institute of Food and Fermentation Industries Co., Ltd.

Yongqing Ma

Liang Chen

Yong Ma

Lu Lu

Jun Lu

Zhe Dong

Muyi Cai

Ruizeng Gu

Xingchang Pan

Yaguang Xu

Jing Wang

Yang Wang

Ying Wei

Wenying Liu

Haixin Zhang

Kelu Cao

Ming Zhou

Guoming Li

Zhentao Jin

Tao Ma

Yuchen Wang

Feng Lin

Yuan Bi

Kong Ling

Yuqing Wang

Xiuyuan Qin

Xinyue Cui

Simeng Jiang

Weixue Yi

A selenium-chelating pea oligopeptide, a preparation method thereof and use thereof. After the selenium-chelating pea oligopeptide is subjected to digestion treatment in at least one of following three ways, a change rate of selenium content not more than 3% with respect to the selenium content before the digestion treatment: hydrolyzing for 4 hours by a pepsin at a pH value of 2 and a temperature of 37° C.; hydrolyzing for 6 hours by a trypsin at a pH value of 7.5 and a temperature of 37° C.; maintaining the temperature constant at 37° C., firstly hydrolyzing for 4 hours by the pepsin at a pH value of 2, and then continuing to hydrolyze for 6 hours by a trypsin at a pH value of 6.8. The preparation method thereof includes mixing and reacting an aqueous solution of pea oligopeptide and sodium selenite, and then being subjected to alcohol precipitation and drying.

Selenium-chelating pea oligopeptide, and preparation method and use thereof

Aand uses thereof. Thehas a deposit number of CGMCC No. 14813. Thecan be used for increasing the amount of an organic acid in a raw material. Thecan be used for fermenting the raw material, where the raw material can be selected from at least one of fruits, which can increase the content of the organic acid in a fermented product.

Lactobacillus paracasei and uses thereof

Disclosed are a fish protein oligopeptide with low allergenicity and slight fishiness, and industrial preparation method and application thereof. The method comprises the following steps: 1) washing fresh fish flesh and/or fish wastes, crushing, and adding water to obtain a mixture; 2) performing thermal denaturation on the mixture to obtain a denaturized protein solution; 3) centrifuging the denaturized protein solution to obtain a precipitate, and adding water into the precipitate and grinding, to obtain a slurry; 4) adjusting the slurry to pH 6-9, and sequentially adding a neutral protease, a papain and an alkaline protease to conduct enzymolysis, and after enzyme inactivation, to obtain an enzymatic hydrolysate; 5) centrifuging the enzymatic hydrolysate, and performing membrane filtration on centrifuged supernatant, to obtain the fish protein oligopeptide with low allergenicity and slight fishiness. The method completely eliminates the allergenicity and fishiness of fish proteins, and prevents release of bitter components.

Fish protein oligopeptide with low allergenicity and slight fishiness and industrial preparation method and application thereof

The present invention discloses a method for producing wheat glutamine peptide using wheat gluten powder as raw material, belonging to the fields of food and biotechnology. The method includes the steps of: performing enzymolysis in two steps using Alcalase and papain with the wheat gluten powder as raw material, to obtain the wheat glutamine peptide with components with molecular weight of less than 1000 Da being more than 90%, characteristic glutamine peptide segment glutamine-arginine-glutamine (Gln-Arg-Gln, QRQ) content being more than 2.0% and glutamine content being up to 23.54% by treating the enzymatic hydrolysate by centrifugation, ultrafiltration, concentration, spray drying, etc. The produced glutamine peptide can be used as functional nutrition composition ingredient in the development and production of ordinary foods, health foods and medicines.

Method for producing wheat glutamine peptide

The present invention discloses a method for producing antihypertensive active peptides with corn germ protein as the material. The method comprises an alkali-heat treatment and continuous enzymolysis of the corn germ protein. The components with molecular weight less than 1000 Da in the active peptides obtained according to the present method account for more than 92%, and alanine-tyrosine (Ala-Tyr, AY) as the characteristic peptide fragments in the antihypertensive peptides accounts for more than 0.6%, so that the active peptides have a good ACE inhibitory activity in vitro as well as stability against temperature, pH and major gastrointestinal digestive enzymes, and have a significant effect of lowering blood pressure on spontaneous hypertension rats in vivo. The active peptides can be applied as a new functional nutrient to development and production of food, health food and pharmaceutical.

Method for preparing active peptides from corn germ proteins

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Beijing, China

Yongqing Ma