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Enzymatic modification of egg-white protein and some of its functional properties

✍ Scribed by Behnke, U. ;Kiss, E. ;Nádudvari, V. ;Rutiloff, H.

Publisher
John Wiley and Sons
Year
1986
Tongue
English
Weight
334 KB
Volume
30
Category
Article
ISSN
0027-769X

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✦ Synopsis

Because of the presence of proteinase inhibitors the enzymatic modification of egg-white protein demands a heating process to inactivate the inhibitors before enzyme action. The herewith occuring strong coagulation of the protein complicates the course of enzymatic hydrolysis. A laboratory process is given to produce partial hydrolyzates of egg-white protein using thermitase (a proteinase of Thermoactinomyces vulgaris) and pancreatin. To characterize the egg-white protein hydrolyzate the degree of hydrolysis, sensoric properties (especially bitterness) and some functional properties such as solubility, water binding capacity, emulsifiability and foaming properties are determined. In the case of low or medium degrees of hydrolysis the enzymatic modification results in better functional properties as compared with those of the starting material.

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