Susceptibilities of bacterial cellulose containing N-acetylglucosamine residues for cellulolytic and chitinolytic enzymes.
Detailed characterization of enzyme susceptibility of bacterial cellulose containing N-acetylglucosamine (GlcNAc) residues (N-AcGBC) which possess high susceptibility for cellulase and lysozyme and slight susceptibility for chitinase was studied. Turbidimetric lysozyme assay of N-AcGBC showed that (i) the susceptibilities of various N-AcGBCs for lysozyme were proportional to GlcNAc content, and (ii) N-AcGBC homogenates were divided into two groups based on the rate of turbidity reduction (not dependent on GlcNAc content). High reactivity of N-AcGBC for lysozyme would arise from fine microfibrils characteristic of bacterial cellulose (BC) and random distribution of GlcNAc residues in N-AcGBC because water soluble oligomers of N-AcGBC produced by lysozymic hydrolysis did not inhibit lysozyme activity; however, the random distribution of GlcNAc seemed to result in the slight susceptibility of N-AcGBC for chitinase. The rate of cellulolytic turbidity reduction of N-AcGBC was slower than that of BC, which arose from the inhibition for binding of cellulase by GlcNAc residues.
Ogawa
R
R
Department of Polymer Science, Faculty of Science, Hokkaido University, Sapporo, Japan.
Miura
Y
Y
Tokura
S
S
Koriyama
T
T
D000091:Acetobacter / Q000378:metabolism; D000117:Acetylglucosamine / Q000737:chemistry / Q000378:metabolism*; D002480:Cellulase / Q000378:metabolism; D002482:Cellulose / Q000737:chemistry / Q000378:metabolism*; D002686:Chitin / Q000378:metabolism; D002688:Chitinases / Q000378:metabolism; D006868:Hydrolysis; D007700:Kinetics; D009113:Muramidase / Q000378:metabolism; D013379:Substrate Specificity
D002686:Chitin; D002482:Cellulose; D002688:Chitinases; D009113:Muramidase; D002480:Cellulase; D000117:Acetylglucosamine