Most cellulolytic enzymes consist of distinct catalytic and cellulose-
binding domains (CBDs). Similar domain structures are also found in en
zymes degrading other insoluble carbohydrates such as raw starch and c
hitin. Such binding domains improve the binding and facilitate the act
ivity of the catalytic domain on the insoluble but not on soluble subs
trates, Based on their amino acid sequence similarities, the CBDs have
been divided into several different families. Structure determination
and subsequent mutagenesis studies have revealed that CBDs rely on se
veral aromatic amino acids for binding to the cellulose surfaces. The
CBDs binding to crystalline cellulose have different topologies but sh
are similar rigid backbone structures for correct positioning of the s
ide chains required for the substrate recognition and binding. CBDs re
present ideal affinity tags for specific immobilisation of various oth
er proteins to cellulose. Furthermore, improved understanding and cont
rol of their action will be important for the improvement of the biote
chnological value of cellulolytic enzymes. (C) 1997 Elsevier Science B
.V.