Method for inhibiting aggregation of proteins in aqueous solution and modifying physical property of proteins, product obtained therethrough and application of product

A technology for inhibiting protein and aqueous solutions, applied in the fields of application, protein food processing, protein food ingredients, etc., can solve the problems of application limitations, achieve the effects of protein molecular configuration stability, surface activity retention, and foaming improvement

Inactive Publication Date: 2012-06-20
SOUTH CHINA UNIV OF TECH
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, natural plant protein has high hydrophobicity, and its application in some food systems is limited. Therefore, it is necessary to modify the physical properties of the protein to improve its functional properties and expand its application field.

Method used

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  • Method for inhibiting aggregation of proteins in aqueous solution and modifying physical property of proteins, product obtained therethrough and application of product
  • Method for inhibiting aggregation of proteins in aqueous solution and modifying physical property of proteins, product obtained therethrough and application of product

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0030] Accurately weigh 0.5g of soybean 7S globulin, dissolve it in 10mL of 0.01mol / L sodium phosphate buffer solution with pH 6.5, weigh 1.5g of dextran and 1.5g of polyethylene glycol (PEG3000) into the buffer and mix evenly. React in a constant temperature magnetic stirrer at 95°C for 6h. After the reaction, quickly cool to room temperature (25°C) in an ice bath to terminate the reaction. The product is centrifuged at 5000rpm for 20min and dialyzed at 4°C for 48h to remove the inert crowding reagent polyethylene glycol and other small particles. Molecular matter. The product is freeze-dried to obtain a product with modified protein properties.

Embodiment 2

[0038] Accurately weigh 0.1g of soybean 7S globulin, dissolve it in 10mL of 0.01mol / L sodium phosphate buffer solution with pH 6, weigh 0.5g of dextran and 1.5g of polyethylene glycol (PEG2000) into the buffer and mix well, React in a constant temperature magnetic stirrer at 80°C for 10 hours. After the reaction is completed, quickly cool to room temperature (25°C) in an ice bath to terminate the reaction. The product is centrifuged at 4000 rpm for 30 minutes and dialyzed at 4°C for 24 hours to remove the inert crowding reagent polyethylene glycol and other small particles. Molecular matter. The product is freeze-dried to obtain a product with modified protein properties.

Embodiment 3

[0045] Accurately weigh 0.6g soybean protein isolate, dissolve it in 20mL 0.01mol / L sodium phosphate buffer solution with pH 8, weigh 3g carrageenan and 5g polyethylene glycol (PEG3350) and add them to the buffer, mix well, and stir magnetically at constant temperature The reaction was carried out at 60°C for 30 hours. After the reaction was completed, the reaction was quickly cooled to room temperature (25°C) in an ice bath to terminate the reaction. The product was centrifuged at 4000 rpm for 30 minutes and dialyzed at 4°C for 30 hours to remove the inert crowding agent polyethylene glycol and other small molecules. The product is freeze-dried to obtain a product with modified protein properties. After purification, the product is used as a new type of emulsifier in meat products such as ham sausage, which can produce better emulsification and thermal stability than ordinary soybean protein isolate, making the flavor and taste of ham sausage better.

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PUM

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Abstract

The invention discloses a method for inhibiting the aggregation of proteins in an aqueous solution and modifying the physical property of the proteins, a product obtained therethrough and an application of the product. A preparation method of the product comprises the following steps: 1, dissolving 1-10 parts by mass of the proteins in a buffer which is a buffer salt solution with the pH value of 6.0-8.0 and the concentration of 0.01-0.2M; 2, adding a macromolecular crowding reagent to the solution obtained in step 1, uniformly mixing, stirring for 4-30h in a 60-95DEG C constant temperature magnetic stirrer, and rapidly cooling to room temperature through ice-bath; 3, centrifuging the obtained product to remove insoluble substances; and 4, dialyzing the product obtained in step 3 to obtain the less aggregation protein physical property modification product. The preparation method which is simple and is easy to operate, and the product which can inhibit the protein aggregation and allows functional properties of the water solubility, the emulsibility, the foaming property, the thermal stability and the like of the proteins to be greatly improved can be applied to the modified protein preparation, food additives or the medicine industry.

Description

technical field [0001] The invention belongs to the field of food and relates to the modification of protein properties, in particular to a novel method for inhibiting protein aggregation and the application of these modified proteins in the food field. Background technique [0002] Protein widely exists in animals and plants, and its nutritional and functional properties (emulsifying, foaming, water-holding, etc.) make it widely used in the food industry, medicine and health care, and feed industries. Physicochemical properties play an important role in manufacturing, processing or preservation, and can also effectively improve the nutritional value of the product. However, natural plant protein has high hydrophobicity, and its application in some food systems is limited. Therefore, it is necessary to modify the physical properties of protein to improve its functional properties and expand its application field. [0003] In the fields of food and medicine, protein aggregat...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): A23J3/00A23L2/66A23L1/314A23L13/40
Inventor 齐军茹张曦杨晓泉
Owner SOUTH CHINA UNIV OF TECH
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