Premium
THE β‐N‐ACETYLGLUCOSAMINIDASE ACTIVITY OF EGG WHITE. 2. Heat Inactivation of the Enzyme in Egg White and Whole Egg
Author(s) -
DONOVAN J. W.,
HANSEN L. U.
Publication year - 1971
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1971.tb02064.x
Subject(s) - egg white , pasteurization , chemistry , kinetics , enzyme , denaturation (fissile materials) , food science , reaction rate constant , biochemistry , nuclear chemistry , physics , quantum mechanics
SUMMARY– The kinetics of the heat inactivation of β‐N‐acetylglucosaminidase in egg white and whole egg at neutral pH is first order in the temperature range 58–62°C. Rate constants for enzyme inactivation by heat are reported for both egg white and whole egg. The activation energy for heat denaturation is 91 kcal/mole in egg white and 73 kcal/mole in whole egg. Reduction of enzymatic activity upon heating can be used as an indication of whether egg white or whole egg has been maintained at the time‐temperature combinations approved for pasteurization by the U.S. Department of Agriculture. This test should be useful as a process control tool.