Cellulases have nonlinear kinetics on polymeric sub-
strates, which appear to be due to substrate heterogeneity
but they show Michaelis–Menten kinetics on small
soluble substrates [14]. Most cellulases are endocellul-
lases, which have an open active site so they can bind and
cleave a cellulose molecule at any accessible point along
the chain [15]. Endocellulases bind randomly along a
cellulose molecule, make a few cleavages and then dis-
sociate from the chain, thus they rapidly decrease the
viscosity of CMC. All exocellulases have their active site
inside a tunnel and they bind only at one end of a
cellulose chain. They cleave off cellobiose processively
from the chain end [16]. Thus exocellulases have low
activity on CMC and do not decrease its viscosity. They
remain bound to a cellulose chain, processively cleaving
cellobiose residues from the chain end until they dis-
sociate. There are two types of exocellulases, one class
attacks the reducing end of cellulose molecules while the
other attacks the nonreducing end [17]. Finally there is a
third class of cellulases, processive endoglucanases that so
far are found only in bacteria. Most processive endoglu-
canases have a unique domain structure in which the C-
terminus of a family 9 cd is rigidly attached to a family 3c
CBM domain [18,19]. These enzymes carry out an initial
endocellulytic attack on a cellulose chain but then they
processively attack the nonreducing end of the initially
cleaved chain, releasing cellotetraose. Some family 5
processive endocellulases also have been identified in
Saccharophagus degradans.