In this study the enzymatic activity of adsorbed Thermomonospora fusca E₅ and Trichoderma reesei CBHI cellulases were investigated using fluorescence techniques. In particular, cellulases were allowed to contact hydrophobic polystyrene surfaces under conditions of different solution concentrations, and adsorption times. Each of these variables is known to have a potential...
Cellulolytic enzymes capable of efficiently degrading crystalline cellulose are a
complex mixture of endo- (endoglucanases) and exo-acting (cellobiohydrolases)
enzymes. One approach to separating these enzymes is affinity chromatography. A new
ligand, p-aminophenyl l-thio-β-D-cellobioside (APTC), is introduced for this purpose.
The property of APTC in affinity chromatography is demonstrated using Trichoderma...
The traditional filter paper assay for saccharifying cellulase
originally described by M. Mandels et al (1976) has been modified to
make possible low activity determinations of Trichoderma
cellulases. The enzymatic activity appears to decline during a
prolonged incubation period if no precautions have been taken. By
means of adding bovine...
A novel type of model substrates, i.e. immobilized p-aminophenyl-β-D-cellooligosaccharides,
was developed and used in the study of exocellulases. The
two major cellobiohydrolases from Trichoderma reesei, CBH I and CBH II were
used as representative enzymes. p-Aminophenyl derivatives of cellobiose (PAPG₂),
cellotriose (PAPG₃), and cellotetraose (PAPG₄) were synthesized from the reaction...
The efficiency of cellulose hydrolysis under straight saccharification and simultaneous saccharification and fermentation (SSF) conditions was evaluated using three lignocellulosic materials (switchgrass, cornstover, and poplar), which had been pretreated with dilute sulfuric acid under conditions which optimized xylose concentrations in the prehydrolysate liquid. Yields of glucose, cellobiose and ethanol obtained...