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 Mw and radii if gyration Rg 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 Mw and radii of gyration Rg 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.
Highlights
Cellulose is the most abundant and renewable resource of the biosphere
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
Hydrolysis kinetics curves of microcrystalline cellulose digested by solutions of non-illuminated and white linearly polarized light (WLPL) illuminated enzymes WT and TR are presented in Figures 1(a) and (b) respectively
Summary
Cellulose is the most abundant and renewable resource of the biosphere. Degradation of cellulose, that enzymatic, to soluble sugars for fuels and industrially essential chemicals has been expected to solve problems of the energy shortage and, at the same time, environment protection. The mechanisms of the enzyme activity enhancement with WLPL is unknown It has been demonstrated [11] that 1 hr illumination with WLPL of α-amylase solutions led to statistically significant changes in the protein conformation of illuminated enzyme, accompanied by acceleration of the potato starch hydrolysis catalyzed by the activated enzyme. Such results indicate that the enhancement of the activity of WLPL stimulated enzymes could be related to conformational changes of the protein molecules In this study this problem is approached by examination of the effect of illumination with WLPL of two commercially available cellulases, isolated from different microorganisms. This effect is checked involving kinetics of the hydrolysis of microcrystalline cellulose catalysed with so stimulated enzymes. Changes of molecular weight of cellulose chains in the course of enzymatic degradation were recorded, to check the enzyme source and/or WLPL stimulation have any impact upon the molecular structure of enzymatically degraded polysaccharide chains
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