Abstract
In order to study the substrate specificities of egg-white lysozyme, p-nitrophenyl 2-acetamido-4- O-(2-acetamido-2-deoxy-β- D-glucopyranosyl)-2-deoxy-β- D-glucopyranoside (V) and p-nitrophenyl 2-acetamido-6- O-(2-acetamido-2-deoxy-β- D-glucopyranosyl)-2-deoxy-β- D-glucopyranoside (XI) were synthesized. Compound V was hydrolyzed by lysozyme, even though its hydrolysis was slow and required relatively massive proportions of the enzyme. On the other hand, both XI and p-nitrophenyl 2-acetamido-2-deoxy-β- D-glucopyranoside (VI) were found to be unaffected by the enzyme. These observations are discussed in relation to the structure of a disaccharide isolated from the cell wall of Micrococcus lysodeikticus by the action of lysozyme, and to the mechanism of resistance of certain bacteria to egg-white lysozyme.
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