Abstract:
: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.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Ogawa R,Miura Y,Tokura S,Koriyama Tdoi
10.1016/s0141-8130(05)80076-5keywords:
subject
Has Abstractpub_date
1992-12-01 00:00:00pages
343-7issue
6eissn
0141-8130issn
1879-0003pii
S0141-8130(05)80076-5journal_volume
14pub_type
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