“…BSA probably has a great affinity for lignin and lignin containing substrates due to its highly hydrophobic nature, isoelectric point (pI), and formation of highly hydrophobic agglomerates at temperatures above about 508C (Echterhoff et al, 2001) and could coat exposed lignin to prevent unspecific, unproductive cellulase adsorption, thus making more enzyme available for hydrolysis (Willies, 2007;Yang and Wyman, 2006). Furthermore, BSA may enhance enzyme stability (Huang and Monk, 2004;Robert, 1983) and reduce the hydrophobicity of surfaces, facilitating cellulase adsorption and desorption (Niamsiri et al, 2007;Park et al, 2002;Tilton et al, 1991). However, the interaction of BSA with the substrate surface may be affected by temperature, pH, ionic strength, substrate hydrophobicity, and surface charge (Chandra et al, 2007;Echterhoff et al, 2001;Ha et al, 1993;Halder et al, 2005).…”