文摘
The influence of pH within the range 6.9–10.0 on the kinetic parameters of Micrococcus lysodeicticus cell lysis catalyzed by hen egg lysozyme has been studied at 25°C and 37°C. The effective pK b values have been calculated for the group determining lysozyme catalytic activity. The ΔH ion value indicates that this group is a carboxyl, although its pK (9.15 at 25°C) is far beyond the range characteristic of carboxylic groups. The cause of this abnormal pK b value is supposed to be the strong negative charge of the bacterial cell wall. As a result, the enzyme, which catalyzes the hydrolysis of N-acetylglucosamine-N-acetylmuramic acid copolymer, operates in a highly acidic microenvironment.