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Volumn 71, Issue 9, 2005, Pages 5318-5323

Enzyme-coupled assay for β-xylosidase hydrolysis of natural substrates

Author keywords

[No Author keywords available]

Indexed keywords

CHROMOPHORES; ENZYME INHIBITION; ENZYME KINETICS; HYDROGEN PEROXIDE; HYDROLYSIS; POSITIVE IONS;

EID: 25144473735     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.71.9.5318-5323.2005     Document Type: Article
Times cited : (24)

References (22)
  • 1
    • 4143116834 scopus 로고    scopus 로고
    • Enzyme-coupled assay of acetylxylan esterases on monoacetylated 4-nitrophenyl β-D-xylopyranosides
    • Biely, P., M. Mastihubová, D. C. la Grange, W. H. van Zyl, and B. A. Prior. 2004. Enzyme-coupled assay of acetylxylan esterases on monoacetylated 4-nitrophenyl β-D-xylopyranosides. Anal. Biochem. 332:109-115.
    • (2004) Anal. Biochem. , vol.332 , pp. 109-115
    • Biely, P.1    Mastihubová, M.2    La Grange, D.C.3    Van Zyl, W.H.4    Prior, B.A.5
  • 2
    • 0041816478 scopus 로고    scopus 로고
    • Detailed kinetic analysis of a family 52 glycoside hydrolase: A β-xylosidase from Geobacillus stearothermophilus
    • Bravman, T., G. Zolotnitsky, V. Belakhov, G. Shoham, B. Henrissat, T. Baasov, and Y. Shoham. 2003. Detailed kinetic analysis of a family 52 glycoside hydrolase: a β-xylosidase from Geobacillus stearothermophilus. Biochemistry 42:10528-10536.
    • (2003) Biochemistry , vol.42 , pp. 10528-10536
    • Bravman, T.1    Zolotnitsky, G.2    Belakhov, V.3    Shoham, G.4    Henrissat, B.5    Baasov, T.6    Shoham, Y.7
  • 3
    • 0037310428 scopus 로고    scopus 로고
    • Microbial conversion of corn stalks to riches
    • Doi, R. H. 2003. Microbial conversion of corn stalks to riches. J. Bacteriol. 185:701-702.
    • (2003) J. Bacteriol. , vol.185 , pp. 701-702
    • Doi, R.H.1
  • 4
    • 0017656783 scopus 로고
    • Quantitative determination of D-xylose by a coupled reaction of D-xylose isomerase with D-glucitol dehydrogenase
    • Kersters-Hilderson, H., E. V. Doorslaer, C. K. De Bruyne, and K. Yamanaka. 1977. Quantitative determination of D-xylose by a coupled reaction of D-xylose isomerase with D-glucitol dehydrogenase. Anal. Biochem. 80:41-50.
    • (1977) Anal. Biochem. , vol.80 , pp. 41-50
    • Kersters-Hilderson, H.1    Doorslaer, E.V.2    De Bruyne, C.K.3    Yamanaka, K.4
  • 5
    • 84979146389 scopus 로고
    • Stereochemistry and mechanism of enzyme reactions
    • Koshland, D. E. 1953. Stereochemistry and mechanism of enzyme reactions. Biol. Rev. 28:416-436.
    • (1953) Biol. Rev. , vol.28 , pp. 416-436
    • Koshland, D.E.1
  • 6
    • 25144469343 scopus 로고    scopus 로고
    • Erithacus Software Ltd., Surrey, United Kingdom
    • Leatherbarrow, R. J. 2004. GraFit 5. Erithacus Software Ltd., Surrey, United Kingdom.
    • (2004) GraFit 5
    • Leatherbarrow, R.J.1
  • 7
    • 0035910126 scopus 로고    scopus 로고
    • Cloning and characterization of two cellulase genes from Lentinula edodes
    • Lee, C. C., D. W. S. Wong, and G. H. Robertson. 2001. Cloning and characterization of two cellulase genes from Lentinula edodes. FEMS Microbiol. Lett. 205:355-360.
    • (2001) FEMS Microbiol. Lett. , vol.205 , pp. 355-360
    • Lee, C.C.1    Wong, D.W.S.2    Robertson, G.H.3
  • 8
    • 0027234633 scopus 로고
    • Genetic organization, sequence and biochemical characterization of recombinant β-xylosidse from Thermoanaerobacterium saccharolyticum strain B6A-RI
    • Lee, Y.-E., and G. Zeikus. 1993. Genetic organization, sequence and biochemical characterization of recombinant β-xylosidse from Thermoanaerobacterium saccharolyticum strain B6A-RI. J. Gen. Microbiol. 139:1235-1243.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 1235-1243
    • Lee, Y.-E.1    Zeikus, G.2
  • 9
    • 0030886131 scopus 로고    scopus 로고
    • Isolation, analysis and expression of two genes from Thermoanaerobacterium sp. strain JW/SL YS485: A β-xylosidase and a novel acetyl xylan esterase with cephalosporin C deacetylase activity
    • Lorenz, W. W., and J. Wiegel. 1997. Isolation, analysis and expression of two genes from Thermoanaerobacterium sp. strain JW/SL YS485: a β-xylosidase and a novel acetyl xylan esterase with cephalosporin C deacetylase activity. J. Bacteriol. 179:5436-5441.
    • (1997) J. Bacteriol. , vol.179 , pp. 5436-5441
    • Lorenz, W.W.1    Wiegel, J.2
  • 10
    • 3543106035 scopus 로고    scopus 로고
    • Novel methods for directed evolution of enzymes: Quality, not quantity
    • Lutz, S., and W. M. Patrick. 2004. Novel methods for directed evolution of enzymes: quality, not quantity. Curr. Opin. Biotechnol. 15:291-297.
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 291-297
    • Lutz, S.1    Patrick, W.M.2
  • 11
    • 0030694040 scopus 로고    scopus 로고
    • Mechanism of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolase: Kinetics and pH studies with 4-methylumbelliferyl β-D-glucan oligosaccharides
    • Malet, C., and A. Planas. 1997. Mechanism of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolase: kinetics and pH studies with 4-methylumbelliferyl β-D-glucan oligosaccharides. Biochemistry 36:13838-13848.
    • (1997) Biochemistry , vol.36 , pp. 13838-13848
    • Malet, C.1    Planas, A.2
  • 14
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • Stemmer, W. P. 1994. DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution. Proc. Natl. Acad. Sci. USA 91:10747-10751.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10747-10751
    • Stemmer, W.P.1
  • 16
    • 0037031275 scopus 로고    scopus 로고
    • Mechanism of Thermoanaerobacterium saccharolyticum β-xylosidase: Kinetic studies
    • Vocadlo, D. J., J. Wicki, K. Rupitz, and S. G. Withers. 2002. Mechanism of Thermoanaerobacterium saccharolyticum β-xylosidase: kinetic studies. Biochemistry 41:9727-9735.
    • (2002) Biochemistry , vol.41 , pp. 9727-9735
    • Vocadlo, D.J.1    Wicki, J.2    Rupitz, K.3    Withers, S.G.4
  • 17
    • 25144487178 scopus 로고    scopus 로고
    • Recent advances in enzyme development
    • J. R. Whitaker, A. G. J. Voragen, and D. W. S. Wong (ed.). Marcel Dekker, New York, N.Y.
    • Wong, D. W. S. 2003. Recent advances in enzyme development, p. 379-387. In J. R. Whitaker, A. G. J. Voragen, and D. W. S. Wong (ed.), Handbook of food enzymology. Marcel Dekker, New York, N.Y.
    • (2003) Handbook of Food Enzymology , pp. 379-387
    • Wong, D.W.S.1
  • 18
    • 0141568787 scopus 로고    scopus 로고
    • Direct screening of libraries of yeast clones for α-amylase activity on raw starch hydrolysis
    • Wong, D. W. S., S. B. Batt, C. C. Lee, and G. H. Robertson. 2003. Direct screening of libraries of yeast clones for α-amylase activity on raw starch hydrolysis. Protein Pept. Lett. 10:459-468.
    • (2003) Protein Pept. Lett. , vol.10 , pp. 459-468
    • Wong, D.W.S.1    Batt, S.B.2    Lee, C.C.3    Robertson, G.H.4
  • 19
    • 16244362031 scopus 로고    scopus 로고
    • High-activity barley α-amylase by directed evolution
    • Wong, D. W. S., S. B. Batt, C. C. Lee, and G. H. Robertson. 2004. High-activity barley α-amylase by directed evolution. Protein J. 23:453-460.
    • (2004) Protein J. , vol.23 , pp. 453-460
    • Wong, D.W.S.1    Batt, S.B.2    Lee, C.C.3    Robertson, G.H.4
  • 20
    • 52849113752 scopus 로고    scopus 로고
    • Isolation of a raw starch-binding fragment from barley α-amylase
    • Wong, D. W. S., S. B. Batt, B. K. Tibbot, and G. H. Robertson. 2000. Isolation of a raw starch-binding fragment from barley α-amylase. J. Protein Chem. 19:373-377.
    • (2000) J. Protein Chem. , vol.19 , pp. 373-377
    • Wong, D.W.S.1    Batt, S.B.2    Tibbot, B.K.3    Robertson, G.H.4
  • 21
    • 0033963529 scopus 로고    scopus 로고
    • Glycosidase mechanisms: Anatomy of a finely tuned catalyst
    • Zechel, D. L., and S. G. Withers. 2000. Glycosidase mechanisms: anatomy of a finely tuned catalyst. Acc. Chem. Res. 33:11-18.
    • (2000) Acc. Chem. Res. , vol.33 , pp. 11-18
    • Zechel, D.L.1    Withers, S.G.2
  • 22
    • 0031573401 scopus 로고    scopus 로고
    • A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: Applications in detecting the activity of phagocyte NADPH oxidase and other oxidases
    • Zhou, M., Z. Diwu, N. Panchuk-Voloshina, and R. P. Haugland. 1997. A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases. Anal. Biochem. 253:162-168.
    • (1997) Anal. Biochem. , vol.253 , pp. 162-168
    • Zhou, M.1    Diwu, Z.2    Panchuk-Voloshina, N.3    Haugland, R.P.4


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