Clostridium thermocellum recombinant beta-(1,3-1,4)-glucanase LicB was
expressed in Escherichia coli K-12 and purified to electrophoretic ho
mogeneity. Specific activity of the final preparation was 12,000 U/mg.
Antibodies against recombinant LicB protein reacted with a specific b
and of purified C. thermocellum F7 cellulosomes, suggesting localizati
on in the extracellular multienzyme complex. This indicates that the c
ellulosome takes part in the hydrolysis of other polysaccharides besid
es cellulose.