The mechanism of the activity of lysozyme on bacteria
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The object of this problem was to demonstrate and discuss the kinetics of the bacteriolytic action of egg white lysozyme. This was done to elucidate further the enzymic nature and the mechanism of lysozyme action. The activity of the enzyme was measured by a turbidimetric method. Crystalline lysozyme was diluted to various concentrations with phosphate buffer (pH 6.2) and incubated at various temperatures with bacterial substrates such as Micrococcus lysodeikticus and Sarcina luten. The decrease in optical density was followed on a Colemen spectrophotometer, using a wave length of 540. The data indicates that the reaction follows the mono-molecular equation as others have earlier cited in the literature. The average Q10 value was 1.75 +/- 0.14. The energy of activation (u) was found to be 10,200 +/- 1600 cal for experiments conducted with lysozyme at three different concentrations and on both substrates. The similarity of "u" values indicates that the lyzing action of lysozyme is characteristic of the enzyme on both substrates. It appears that the lysozyme is splitting the same type of linkage in the mucopolysaccharide component of the bacterial cell membrane. Thus this enzymatic reaction is quite specific. It was also shown that the velocity of the lytic action by lysozyme is determined by the amount of lysozyme absorbed, i.e. - absorption is the rate-determining step.
Thesis (M.A)--Boston University
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