Method for improving foaming property and emulsifying property of ovalbumin

Abstract

The invention relates to a method for improving foaming property and emulsifying property of ovalbumin. According to the method, ovalbumin is taken as an object, and mild limited oxidation is performed on the ovalbumin by using an oxidant solution so as to have foaming property and emulsifying property of the ovalbumin improve, wherein the oxidant solution comprises FeCl3 of which the concentration is 0.1 mmol / L, ascorbic acid of which the concentration is 0.1 mmol / L and H2O2 of which the concentration is 8.0-12.0 mmol / L; the ovalbumin undergoes low-temperature oxidation; the oxidation productis washed by using phosphate buffer of which the pH value is 6.0; centrifugal separation is carried out; and freeze-drying is performed on the separated precipitate. The ovalbumin after the mild limited oxidation performed by adopting the method disclosed by the invention has foaming capacity up to 159.85-175.67%, foam stability up to 73.62-82.53%, emulsifying activity up to 11.08-13.45 m<2 > / g and emulsion stability up to 97.14-109.51%.

Description

technical field [0001] The present invention relates to a method for improving the foamability and emulsification of ovalbumin. Background technique [0002] The most important protein in egg white is ovalbumin, which accounts for 54% of egg white protein. Ovalbumin is a monomeric globular phosphoglycoprotein, consisting of 385 amino acid residues, with a relative molecular mass of 43.0kDa, an isoelectric point of 4.5, and an internal glycosyl content of about 3%. There are 4 free sulfhydryl groups in its hydrophobic center, 1 a disulfide bond. In the natural state of ovalbumin, the α-helical structure is stretched out and becomes the center of each reaction. At the same time, there are 5 β-fold structures parallel to the axis on the horizontal axis of the protein molecule, and the ovalbumin molecule contains 1 N- Glycosylation sites, 2 phosphorylation sites, 1 disulfide bond buried inside the hydrophobic center, and 4 free sulfhydryl groups. In the natural egg liquid sys...

AI Technical Summary

Problems solved by technology

However, the pure product of ovalbumin separated from the egg white protein system loses the synergistic effect of ovomucoid, ovomucin, ovotransferrin and lysozyme, and the foaming and emulsifying properties are significantly reduced, which hinders the functional properties of ovalbumin in Application in the food industry, especially in food processing such as cakes, so it is of great significance to improve its foaming and emulsifying properties by physical or biochemical methods