Interaction of lysozyme with isomeric p-nitrophenyl O-(2-acetamido-2-deoxy-β- D-glucopyranosyl)- O-(2-acetamido-2-deoxy-β- D-glucopyranosyl)-2-acetamido-2-deoxy-β- D-glucopyranosides

• Published in: Carbohydrate research 1972, Vol.21 (2), p.269-273
• Main Authors: Khorlin, A.Ya, Shashkova, E.A., Zurabyan, S.E.
• Format: Article
• Language: English
• ISSN: 0008-6215; 1873-426X
• DOI: 10.1016/S0008-6215(00)82153-9

The action of hen egg-white lysozyme on three isomeric trisaccharides, p-nitrophenyl tri- N-acetylchitotrioside ( 1), p-nitrophenyl O-(2-acetamido-2-deoxy-β- D-glucopyranosyl)-(1→4)- O-(2-acetamido-2-deoxy-β- D-glucopyranosyl)-(1→6)-2-acetamido-2-deoxy-β- D-glucopyranoside ( 2), and p-nitrophenyl O-(2-acetamido-2-deoxy-β- D-glucopyranosyl)-(1→3)- O-(2-acetamido-2-deoxy-β- D-glucopyranosyl)-(1→6)-2-acetamido-2-deoxy-β- D-glucopyranoside ( 3), was investigated. These three compounds exhibited the same inhibitory effect on the lysozyme-catalyzed hydrolysis of Micrococcus lysodeikticus cell walls. In addition, 2 and 3 were slowly hydrolysed by the enzyme with a marked lag period. This suggests that the lysozyme specificity, closely associated with the conformation of the enzyme active site, can vary extensively.