FIBRIL FORMATION FROM CELLULOSE BY A NOVEL PROTEIN FROM TRICHODERMA-REESEI - A NON-HYDROLYTIC CELLULOLYTIC COMPONENT

A low molecular weight protein, named fibril-forming protein (FFP), wa s isolated from the culture supernatant of Avicel-grown Trichoderma re esei. The protein was purified to homogeneity and it exhibited a molec ular weight of 11,400 Da. Low amounts of this protein caused apparentl y non-hydrolytic disruption of filter paper, releasing fibrils without any detectable release of reducing sugars. It displayed no hydrolytic activity on carboxymethylcellulose (CMC), p-nitrophenyl-beta-D-glucos ide (pNPG) or 4-methylumbelliferyl cellobioside. The pH optimum of the protein was between 4 and 5. The temperature optimum was 40 degrees C and the computed activation energy (E-a) for the filter paper disrupt ion process was 4.18 kcal/mol, suggesting disruption of non-covalent b onds. It had no immunological cross reactivity with reported cellulase components of T. reesei.