Record Detail

To identify the interactions between the
carbohydrate-binding module (CBM) of fungal cellulases
and the surface of cellulose crystalline regions,
the interactions between four fungal cellulases from
different origins and cellulose nanocrystal substrates
with polymorphs of cellulose I, II, and the hybrid I/II,
were measured by a quartz crystal microbalance with
dissipation technique and compared in this investigation.
The experiments of cellulase adsorption/desorption
on substrates were conducted at 15 C and the
results showed that the preference of four tested fungal
cellulases to the substrates with different polymorphs
followed the order of cellulose I, I/II to II. However,
when the experiments conducted at 45 C, the exhibited
hydrolytic activity of substrates followed an
inverse order. As such, it can be concluded that in the
whole process of enzymatic hydrolysis, treatments
involving polymorphic conversion from cellulose I to
II reduces the speed of CBM recognition but facilitates
the hydrolysis reaction, and therefore the overall
performance of polymorphic conversion is beneficial
to enzymatic hydrolysis.