Isolated fungal cellulose terminal domains and a synthetic minimum analogue bind to cellulose

Abstract

The cellulose‐binding properties of the highly conserved terminal region which is common to several fungal cellulases were studied. Domains were prepared by proteolytic cleavage of Trichoderma reesei CBH1 and the corresponding enzyme from Sporotrichum pulverulentum , and a peptide corresponding to residues 462–497 (the C‐terminal part) of Trichoderma CBH1 was synthesized. The three peptides showed similar binding behavior, whereas reduced and S ‐carboxymethylated T. reesei fragment was inactive. This region thus appears to serve as an independent functional domain in which the C‐terminal part is responsible for the binding, which in turn requires an intact three‐dimensional structure.