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

Ewelina Nowak, Gohar Khachatryan, Agnieszka Polit, Lidia Krzeminska-Fiedorowicz, Marta Dziedzicka-Wasylewska, Maciej Fiedorowicz

Department of Chemistry and Physics, University of Agriculture, Krakow, Poland.
Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Krakow, Poland.

DOI: 10.4236/ojopm.2012.23007                

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 illuminated 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 dichroism (CD) spectra. Additionally, molecular weight M_w and radii of gyration R_g of polysaccharide chains of microcrystalline 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 Mw and radii of gyration Rg 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.

Keywords

Cellulases; Polarized Light; Microcrystalline Cellulose

Conflicts of Interest

The authors declare no conflicts of interest.

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