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Glucose oxidase (GOD) was illuminated with white linearly polarized light (WLPL). The enzyme was illuminated at room temperature in separate vessels then admixed to a reactor filled with D-glucose. The illumination of the enzyme for 60 min at 25-30 degrees C and pH 6.5-7.0 provided its superior stimulation as proven in the oxidation of beta-D-glucose. Lyophilization of the illuminated enzyme reduced its activity by, approximately, 30%.

After illumination with white, linearly polarized light (WLPL), cyclodextrin glycosyltransferase produced mixture of alpha-, beta-, and gamma-cyclodextrins (CD) with higher overall yield than did that enzyme when nonilluminated. The illumination also influenced the ratio of those CD and that effect depended on concentration of enzyme and illumination time. At a high enzyme concentration (0.64 U/cm(3)), regardless the illumination time, formation of beta-CD predominated. The highest yield of beta-CD was afforded after 1 h illumination and 2 h illumination led to a significant increase in the yield of gamma-CD. Three-month storage of enzyme illuminated with WLPL did not reduce its enhanced activity.

Illumination with white linearly polarized light (WLPL) stimulated chitinase and chitosanase in their degradation of chitin and chitosan, respectively. Enzymes were illuminated at room temperature in separate vessels, then admixed in reactors containing polysaccharides. Hydrolysis of chitosan to glucosamine followed first order kinetics whereas hydrolysis of chitin to N-acetylglucosamine deviated from the first order kinetics. In both cases, an increase in the rate of hydrolysis depended on the illumination time. Efficient degradation required up to 60 min exposure of the enzyme to WLPL.

The alpha-amylolysis of potato, corn, waxy corn, and amaranthus starches with porcine pancreatic alpha-amylase upon illumination with visible polarized and nonpolarized light was studied. Samples were illuminated for 1 h either directly after blending the enzyme with starch or the enzyme solutions were illuminated for 1 h prior to the admixture of starch. Independently of the mode of illumination, no significant change in the hydrolysis kinetics was noted for corn, waxy corn, and amaranthus starches. The illumination of potato starch in the presence of alpha-amylase with polarized and nonpolarized light significantly accelerated the hydrolysis. In the first 5-h step the hydrolysis rate increased from 12.0 to 60.0 g x kg(-)(1) h(-)(1). Preillumination of enzyme in solution resulted in an increase in the rate of hydrolysis to 151.6 and 131.4 g x kg(-)(1) h(-)(1) after illumination with polarized and nonpolarized light, respectively. Circular dichroism spectra of alpha-amylase solutions stored in the dark and illuminated with visible polarized and nonpolarized light provided evaluation of the protein conformation, whereas exposure of enzyme solutions to the nonpolarized did not change the secondary structure of the protein. The illumination of the alpha-amylase solutions with polarized light significantly changed the amounts of alpha-helix and beta-form vs unilluminated samples: 42.3% and 25.5% vs 36.6% and 30.2%, respectively.