An ultrasensitive, continuous assay for xylanase using the fluorogenic substrate 6,8-difluoro-4-methylumbelliferyl β-d-xylobioside
作者： Yue Ge , Evan G. Antoulinakis , Kyle R. Gee , Iain Johnson
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摘要: We describe a fluorescence-based assay for the analysis of xylanase activity using novel fluorogenic substrate, 6,8-difluoro-4-methylumbelliferyl beta-D-xylobioside (DiFMUX(2)). Generation fluorescent 6,8-difluoro-4-methylumbelliferone (DiFMU) from substrate corresponded directly to activity. High-performance liquid chromatography digestion products showed that hydrolyzed DiFMUX(2) DiFMU and xylobiose. The provides speed, sensitivity, convenience required measuring or screening inhibitors in high-throughput format is suitable kinetic xylanases variety sources.
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sci-hub.se 参考文章(15)
William R. Kenealy, Thomas W. Jeffries, Rapid 2,2'-bicinchoninic-based xylanase assay compatible with high throughput screening. Biotechnology Letters. ,vol. 25, pp. 1619- 1623 ,(2003) , 10.1023/A:1025668031928
Herman van Tilbeurgh, Marc Claeyssens, Clement K. de Bruyne, The use of 4-methylumbelliferyl and other chromophoric glycosides in the study of cellulolytic enzymes FEBS Letters. ,vol. 149, pp. 152- 156 ,(1982) , 10.1016/0014-5793(82)81092-2
Ji-Hu Zhang, Thomas D. Y. Chung, Kevin R. Oldenburg, A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays. Journal of Biomolecular Screening. ,vol. 4, pp. 67- 73 ,(1999) , 10.1177/108705719900400206
Kyle R. Gee, Wei-Chuan Sun, Mahesh K. Bhalgat, Rosalyn H. Upson, Dieter H. Klaubert, Katherine A. Latham, Richard P. Haugland, Fluorogenic Substrates Based on Fluorinated Umbelliferones for Continuous Assays of Phosphatases and β-Galactosidases Analytical Biochemistry. ,vol. 273, pp. 41- 48 ,(1999) , 10.1006/ABIO.1999.4202
Tariq A. Tahir, Jean-Guy Berrin, Ruth Flatman, Alain Roussel, Peter Roepstorff, Gary Williamson, Nathalie Juge, Specific characterization of substrate and inhibitor binding sites of a glycosyl hydrolase family 11 xylanase from Aspergillus niger. Journal of Biological Chemistry. ,vol. 277, pp. 44035- 44043 ,(2002) , 10.1074/JBC.M205657200
Q. K. Beg, M. Kapoor, L. Mahajan, G. S. Hoondal, Microbial xylanases and their industrial applications: a review. Applied Microbiology and Biotechnology. ,vol. 56, pp. 326- 338 ,(2001) , 10.1007/S002530100704
Peter Biely, Danica Mislovičová, Rudolf Toman, Soluble chromogenic substrates for the assay of endo-1,4-β-xylanases and endo-1,4-β-glucanases Analytical Biochemistry. ,vol. 144, pp. 142- 146 ,(1985) , 10.1016/0003-2697(85)90095-8
Hisataka Taguchi, Tohru Hamasaki, Takashi Akamatsu, Hirosuke Okada, A Simple Assay for Xylanase Using o-Nitrophenyl-β-D-xylobioside Bioscience, Biotechnology, and Biochemistry. ,vol. 60, pp. 983- 985 ,(1996) , 10.1271/BBB.60.983
Thomas W Jeffries, Biochemistry and genetics of microbial xylanases Current Opinion in Biotechnology. ,vol. 7, pp. 337- 342 ,(1996) , 10.1016/S0958-1669(96)80041-3
P. Biely, M. Vršanská, M. Tenkanen, D. Kluepfel, Endo-β-1,4-xylanase families: differences in catalytic properties Journal of Biotechnology. ,vol. 57, pp. 151- 166 ,(1997) , 10.1016/S0168-1656(97)00096-5