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Thesis (M.S.)—University of Nebraska—Lincoln, 1971. Department of Food Science and Technology.


Copyright 1971, the author. Used by permission.


In order to elucidate the role of certain amino acid residues in the function of the milk lysozyme, the present study was undertaken to specifically modify certain amino acid residues of BML and HML and of EWL, as a control, and to determine the effect of these modifications on the activity and immunology of the lysozymes. The study was undertaken with the following objectives: (1) To chemically modify the lysine, arginine, histidine, tyrosine, cysteine, and methionine residues of BML and HML, and to compare the results of those of EWL. (2) To determine the effect of modifications on lytic activity. (3) To determine the number of free SH groups in the native and reduced lysozymes. (4) To determine the effect of modification on chitinase activity. (5) To determine the effect of modifications on the immnodiffusion patterns of the lysozymes.

The human milk used in this study was purchased from the Wilmington Mothers’ Milk Bank in Wilmington, Delaware.The samples of human milk were maintained at -20 C until enzyme isolation was begun. Bovine milk was obtained from the Food Science and Technology Department or from local dairies and was used immediately after separation to obtain the skim milk.

Advisor: Khem M. Shahani