Geweely, N. S., S. A. Ouf, M. A. Eldesoky, and A. A. Eladly,
"Stimulation of alkalothermophilic Aspergillus terreus xylanase by low-intensity laser radiation.",
Archives of microbiology, vol. 186, issue 1, pp. 1-9, 2006 Jul.
AbstractIn this study, Aspergillus terreus was irradiated by a 7.3 mW He-Ne laser in the presence of crystal violet, toluidine blue O and hematoporphyrin as photosensitizers. Xylanases recovered from non-irradiated and irradiated fungi were purified and characterized. The maximum production of xylanase (42.2 U/ml) was obtained after 5 min of laser irradiation in the absence of the photosensitizer. The irradiation of the sensitized fungus diminished the production of xylanase. On purification using G-100, the specific activity of xylanase recovered from the irradiated fungus was 292 U/mg protein representing a 37-fold purification over the crude extract compared with 95.6 U/mg protein representing the 12.8-fold for the enzyme recovered from the non-irradiated fungus. The enzyme recovered from the irradiated fungus had lower molecular weight as compared with that recovered from the non-irradiated one. Characterization of the purified enzymes revealed that the enzyme recovered from the irradiated fungus was more thermostable and had a wider range of optimum reaction temperature (60-70 degrees C) and pH (4.0-12.0), compared to the non-irradiated one.
Geweely, N. S., S. A. Ouf, M. A. Eldesoky, and A. A. Eladly,
"Stimulation of alkalothermophilic Aspergillus terreus xylanase by low-intensity laser radiation.",
Archives of microbiology, vol. 186, issue 1, pp. 1-9, 2006 Jul.
AbstractIn this study, Aspergillus terreus was irradiated by a 7.3 mW He-Ne laser in the presence of crystal violet, toluidine blue O and hematoporphyrin as photosensitizers. Xylanases recovered from non-irradiated and irradiated fungi were purified and characterized. The maximum production of xylanase (42.2 U/ml) was obtained after 5 min of laser irradiation in the absence of the photosensitizer. The irradiation of the sensitized fungus diminished the production of xylanase. On purification using G-100, the specific activity of xylanase recovered from the irradiated fungus was 292 U/mg protein representing a 37-fold purification over the crude extract compared with 95.6 U/mg protein representing the 12.8-fold for the enzyme recovered from the non-irradiated fungus. The enzyme recovered from the irradiated fungus had lower molecular weight as compared with that recovered from the non-irradiated one. Characterization of the purified enzymes revealed that the enzyme recovered from the irradiated fungus was more thermostable and had a wider range of optimum reaction temperature (60-70 degrees C) and pH (4.0-12.0), compared to the non-irradiated one.
Geweely, N. S., S. A. Ouf, M. A. Eldesoky, and A. A. Eladly,
"Stimulation of alkalothermophilic Aspergillus terreusxylanase by low-intensity laser radiation",
Archives of microbiology, vol. 186, no. 1: Springer, pp. 1–9, 2006.
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] 