Stimulation of Selected Cellulases from Trichoderma reesei with White Linearly Polarized Light

Abstract

The impact of the illumination with white linearly polarized light (WLPL) of two commercially available cellulases from Trichoderma reesei on their activity in hydrolysis of microcrystalline cellulose was studied. Enzymes were illu-minated with WLPL for 60 min and 120 min and for each native and illuminated enzyme sample specific activity and kinetics of enzyme catalyzed hydrolysis of microcrystalline cellulose were established. Molecular weight M w and radii if gyration R g of protein chains of native and illuminated enzymes were measured by means of high pressure size exclu-sion chromatography coupled with multiangle laser light scattering and refractometric detectors (HPSEC-MALLS-RI). Conformations of protein chains of native and illuminated enzymes were evaluated on the basis of their circular dichro-ism (CD) spectra. Additionally, molecular weight M w and radii of gyration R g of polysaccharide chains of microcrystal-line cellulose native and digested for 10 min, 480 min and 1440 min with original and WLPL stimulated enzymes WT and TR were taken. Illumination with WLPL of both cellulases studied did not change secondary structures of protein molecules of native enzyme. Molecular weight M w and radii of gyration R g of illuminated enzymes differed greatly from those found for native enzymes. Illumination of enzymes led to increase of specific activity and rate constants of reaction of hydrolysis microcrystalline cellulose catalyzed by illuminated enzymes as compared with native enzymes.