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Volumn 22, Issue 1, 1998, Pages 42-49

Purification and characterization of a thermostable xylanase from Bacillus amyloliquefaciens

Author keywords

Bacillus amyloliquefaciens xylanase; Cellulase free; Composition; Hydrophobic interaction chromatography; Stability; Xylan

Indexed keywords

ADSORPTION; AMINO ACIDS; BACTERIA; BIOSYNTHESIS; CELL CULTURE; PRECIPITATION (CHEMICAL); PURIFICATION;

EID: 0031973584     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(97)00102-6     Document Type: Article
Times cited : (111)

References (41)
  • 2
    • 84981976048 scopus 로고
    • β-1,4-D-xylan-degrading enzyme systems: Biochemistry, molecular biology, and applications
    • 2. Coughlan, M. P. and Hazlewood, G. P. β-1,4-D-xylan-degrading enzyme systems: Biochemistry, molecular biology, and applications. Biotechnol. Appl. Biochem. 1993, 17, 259-289
    • (1993) Biotechnol. Appl. Biochem. , vol.17 , pp. 259-289
    • Coughlan, M.P.1    Hazlewood, G.P.2
  • 4
    • 0000980068 scopus 로고
    • Chemical structure of xylans and their interaction in the plant cell walls
    • Visser, J., Beldman, G., Kusters-van Someren, M. A., and Voragen, A. G. J., Eds. Elsevier, Amsterdam
    • 4. Joseleau, J. P., Comtat, J., and Ruel, K. Chemical structure of xylans and their interaction in the plant cell walls. In: Progress in Biotechnology 7. Xylans and Xylanases (Visser, J., Beldman, G., Kusters-van Someren, M. A., and Voragen, A. G. J., Eds.). Elsevier, Amsterdam, 1992, 1-16
    • (1992) Progress in Biotechnology 7. Xylans and Xylanases , pp. 1-16
    • Joseleau, J.P.1    Comtat, J.2    Ruel, K.3
  • 5
    • 0022386956 scopus 로고
    • Microbial xylanolytic systems
    • 5. Biely, P. Microbial xylanolytic systems. Trends Biotechnol. 1985, 3, 286-290
    • (1985) Trends Biotechnol. , vol.3 , pp. 286-290
    • Biely, P.1
  • 6
    • 0001247281 scopus 로고
    • Xylanases for the pulp and paper industry
    • Visser, J., Beldman, G., Kusters-van Someren, M. A., and Voragen, A. G. J., Eds. Elsevier, Amsterdam
    • 6. Nissen, A. M., Anker, L., Munk, N., and Lange, N. K. Xylanases for the pulp and paper industry. In: Progress in Biotechnology 7. Xylans and Xylanases (Visser, J., Beldman, G., Kusters-van Someren, M. A., and Voragen, A. G. J., Eds.). Elsevier, Amsterdam, 1992, 325-337
    • (1992) Progress in Biotechnology 7. Xylans and Xylanases , pp. 325-337
    • Nissen, A.M.1    Anker, L.2    Munk, N.3    Lange, N.K.4
  • 7
    • 0024087074 scopus 로고
    • Multiplicity of β-1,4-xylanase in microorganisms: Functions and applications
    • 7. Wong, K. K. Y., Tan, L. U. L., and Saddler, J. N. Multiplicity of β-1,4-xylanase in microorganisms: Functions and applications. Microbiol. Rev. 1988, 52, 305-317
    • (1988) Microbiol. Rev. , vol.52 , pp. 305-317
    • Wong, K.K.Y.1    Tan, L.U.L.2    Saddler, J.N.3
  • 9
    • 0000497914 scopus 로고
    • Purification and properties of endoxylanase produced by Bacillus pumilus
    • 9. Panbangred, W., Shinmyo, A., Kinoshita, S., and Okada, H. Purification and properties of endoxylanase produced by Bacillus pumilus. Agric. Biol. Chem. 1983, 47, 957-963
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 957-963
    • Panbangred, W.1    Shinmyo, A.2    Kinoshita, S.3    Okada, H.4
  • 11
    • 84998498469 scopus 로고
    • Purification and characterization of xylanases from alkalophilic thermophilic Bacillus spp
    • 11. Okazaki, W., Akiba, T., Horikoshi, K., and Akahoshi, R. Purification and characterization of xylanases from alkalophilic thermophilic Bacillus spp. Agric. Biol. Chem. 1985, 49, 2033-2039
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 2033-2039
    • Okazaki, W.1    Akiba, T.2    Horikoshi, K.3    Akahoshi, R.4
  • 12
    • 0025608736 scopus 로고
    • Purification and properties of thermostable xylanase and β-xylosidase produced by a newly isolated Bacillus stearothermophilus strain
    • 12. Nanmori, T., Watanabe, T., Shinke, R., Kohno, A., and Kawamura, Y. Purification and properties of thermostable xylanase and β-xylosidase produced by a newly isolated Bacillus stearothermophilus strain. J. Bacteriol. 1990, 172, 6669-6672
    • (1990) J. Bacteriol. , vol.172 , pp. 6669-6672
    • Nanmori, T.1    Watanabe, T.2    Shinke, R.3    Kohno, A.4    Kawamura, Y.5
  • 13
    • 0026741170 scopus 로고
    • Purification and properties of extracellular endoxylanases from alkalophilic thermophilic Bacillus sp
    • 13. Dey, D., Hinge, J., Shendye, A., and Rao, M. Purification and properties of extracellular endoxylanases from alkalophilic thermophilic Bacillus sp. Can. J. Microbiol. 1992, 38, 436-442
    • (1992) Can. J. Microbiol. , vol.38 , pp. 436-442
    • Dey, D.1    Hinge, J.2    Shendye, A.3    Rao, M.4
  • 15
    • 0027246551 scopus 로고
    • Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6
    • 15. Khasin, A., Alchanati, I., and Shoham, Y. Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6. Appl. Environ. Microbiol. 1993, 59, 1725-1730
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1725-1730
    • Khasin, A.1    Alchanati, I.2    Shoham, Y.3
  • 18
    • 0029635955 scopus 로고
    • Purification and characterization of a thermophilic alkaline xylanase from thermoalkaliphilic Bacillus sp. strain TAR-1
    • 18. Nakamura, S., Ishiguro, Y., Nakai, R., Wakabayashi, K., Aono, R., and Horikoshi, K. Purification and characterization of a thermophilic alkaline xylanase from thermoalkaliphilic Bacillus sp. strain TAR-1. J. Mol. Catal. B: Enz. 1995, 1, 7-15
    • (1995) J. Mol. Catal. B: Enz. , vol.1 , pp. 7-15
    • Nakamura, S.1    Ishiguro, Y.2    Nakai, R.3    Wakabayashi, K.4    Aono, R.5    Horikoshi, K.6
  • 19
    • 0028790376 scopus 로고
    • Purification and properties of xylanase a from alkali-tolerant Bacillus sp. strain BP-23
    • 19. Blanco, A., Vidal, T., Colom, J. F., and Pastor, J. F. I. Purification and properties of xylanase A from alkali-tolerant Bacillus sp. strain BP-23. Appl. Environ. Microbiol. 1995, 61, 4468-4470
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 4468-4470
    • Blanco, A.1    Vidal, T.2    Colom, J.F.3    Pastor, J.F.I.4
  • 21
    • 0000738385 scopus 로고
    • Genus Bacillus Cohn 1872
    • Sneath, P. H. A., McNair, N. S., and Sharpe, M. E., Eds. Williams & Wilkins, Baltimore
    • th Ed. (Sneath, P. H. A., McNair, N. S., and Sharpe, M. E., Eds.). Williams & Wilkins, Baltimore, 1986, 1105-1140
    • (1986) th Ed. , vol.2 , pp. 1105-1140
    • Claus, D.1    Berkeley, R.C.W.2
  • 22
    • 0022259472 scopus 로고
    • Production of cloned human leukocyte interferon by Bacillus subtilis: Optimal production is connected with restrained growth
    • 22. Meyer, H. P. and Fiechter, A. Production of cloned human leukocyte interferon by Bacillus subtilis: Optimal production is connected with restrained growth. Appl. Environ. Microbiol. 1985, 50, 503-507
    • (1985) Appl. Environ. Microbiol. , vol.50 , pp. 503-507
    • Meyer, H.P.1    Fiechter, A.2
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 23. Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 1970, 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 36949089946 scopus 로고
    • Disk electrophoresis of basic proteins and peptides on polyacrylamide gels
    • 24. Reisfeld, R. A., Lewis, U. J., and Williams, D. E. Disk electrophoresis of basic proteins and peptides on polyacrylamide gels. Nature 1962, 195, 281-283
    • (1962) Nature , vol.195 , pp. 281-283
    • Reisfeld, R.A.1    Lewis, U.J.2    Williams, D.E.3
  • 25
    • 0000544299 scopus 로고
    • A simplified ultrasensitive stain for detecting proteins in polyacrylamide gels
    • 25. Oakley, B. R., Kirsch, D. R., and Morris, N. R. A simplified ultrasensitive stain for detecting proteins in polyacrylamide gels. Anal. Biochem. 1980, 105, 361-363
    • (1980) Anal. Biochem. , vol.105 , pp. 361-363
    • Oakley, B.R.1    Kirsch, D.R.2    Morris, N.R.3
  • 26
    • 0029169999 scopus 로고
    • Detection of endo-xylanase activities in electrophoretic gels with congo red staining
    • 26. Breccia, J. D., Castro, G. R., Baigorí, M. D., and Siñeriz, F. Detection of endo-xylanase activities in electrophoretic gels with congo red staining. Biotechnol. Tech. 1995, 9, 145-148
    • (1995) Biotechnol. Tech. , vol.9 , pp. 145-148
    • Breccia, J.D.1    Castro, G.R.2    Baigorí, M.D.3    Siñeriz, F.4
  • 27
    • 0010581394 scopus 로고
    • Automatic recording apparatus for use in chromatography of amino acids
    • 27. Spackman, D. H., Stein, W. H., and Moore, S. Automatic recording apparatus for use in chromatography of amino acids. Anal. Chem. 1958, 30, 1190-1206
    • (1958) Anal. Chem. , vol.30 , pp. 1190-1206
    • Spackman, D.H.1    Stein, W.H.2    Moore, S.3
  • 29
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugars
    • 29. Miller, G. L. Use of dinitrosalicylic acid reagent for determination of reducing sugars. Anal. Chem. 1959, 31, 426-428
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 30
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • 30. Smith, P. K., Krohn, R. I., and Hermanson, E. K. Measurement of protein using bicinchoninic acid. Anal. Biochem. 1985, 150, 76-85
    • (1985) Anal. Biochem. , vol.150 , pp. 76-85
    • Smith, P.K.1    Krohn, R.I.2    Hermanson, E.K.3
  • 31
    • 0028330705 scopus 로고
    • Regulation of xylanolytic enzymes in Bacillus subtilis
    • 31. Lindner, C., Stulke, J., and Hecker, M. Regulation of xylanolytic enzymes in Bacillus subtilis. Microbiology 1994, 140, 753-757
    • (1994) Microbiology , vol.140 , pp. 753-757
    • Lindner, C.1    Stulke, J.2    Hecker, M.3
  • 32
    • 0023111434 scopus 로고
    • Isolation and some properties of a β-D-xylosidase from Clostridium acetobutylicum ATCC 824
    • 32. Lee, S. F. and Forsberg, C. W. Isolation and some properties of a β-D-xylosidase from Clostridium acetobutylicum ATCC 824. Appl. Environ. Microbiol. 1987, 53, 651-657
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 651-657
    • Lee, S.F.1    Forsberg, C.W.2
  • 33
    • 0021863774 scopus 로고
    • Acetyl xylan esterases in fungal cellulolytic systems
    • 33. Biely, P., Puls, J., and Schneider, H. Acetyl xylan esterases in fungal cellulolytic systems. FEBS Lett. 1985, 186, 80-84
    • (1985) FEBS Lett. , vol.186 , pp. 80-84
    • Biely, P.1    Puls, J.2    Schneider, H.3
  • 34
    • 0017850731 scopus 로고
    • A colorimetric assay for glycoproteins based on the periodic acid/Schiff stain
    • 34. Mantle, M. and Allen, A. A colorimetric assay for glycoproteins based on the periodic acid/Schiff stain. Biochem. Soc. Trans. 1978, 6, 607-609
    • (1978) Biochem. Soc. Trans. , vol.6 , pp. 607-609
    • Mantle, M.1    Allen, A.2
  • 35
    • 0026603057 scopus 로고
    • Glycoprotein components of cellulase and xylanase enzymes of a Bacillus sp
    • 35. Paul, J. and Varma, A. K. Glycoprotein components of cellulase and xylanase enzymes of a Bacillus sp. Biotechnol. Lett. 1992, 14, 207-212
    • (1992) Biotechnol. Lett. , vol.14 , pp. 207-212
    • Paul, J.1    Varma, A.K.2
  • 36
    • 0001719868 scopus 로고
    • Xylan structure, microbial xylanases, and their mode of action
    • 36. Bastawde, K. B. Xylan structure, microbial xylanases, and their mode of action. World J. Microbiol. Biotechnol. 1992, 8, 353-368
    • (1992) World J. Microbiol. Biotechnol. , vol.8 , pp. 353-368
    • Bastawde, K.B.1
  • 37
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • 37. Sreerama, N. and Woody, R. W. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 1993, 209, 32-44
    • (1993) Anal. Biochem. , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 38
    • 0002746984 scopus 로고
    • Amino acid sequence of the low molecular weight xylanase from Trichoderma viride
    • Visser, J., Beldman, G., Kusters-van Someren, M. A., and Voragen, A. G. J., Eds. Elsevier, Amsterdam
    • 38. Yaguchi, M., Roy, C., Ujiie, M., Watson, D. C., and Wakarchuk, W. Amino acid sequence of the low molecular weight xylanase from Trichoderma viride. In: Progress in Biotechnology 7. Xylans and Xylanases (Visser, J., Beldman, G., Kusters-van Someren, M. A., and Voragen, A. G. J., Eds.). Elsevier, Amsterdam, 1992, 149-154
    • (1992) Progress in Biotechnology 7. Xylans and Xylanases , pp. 149-154
    • Yaguchi, M.1    Roy, C.2    Ujiie, M.3    Watson, D.C.4    Wakarchuk, W.5
  • 39
    • 0029777273 scopus 로고    scopus 로고
    • Purification and characterization of two thermostable endo-1,4-β-D-xylanases from Thermotoga thermarum
    • 39. Sunna, A., Puls, J., and Antranikian, G. Purification and characterization of two thermostable endo-1,4-β-D-xylanases from Thermotoga thermarum. Biotechnol. Appl. Biochem. 1996, 24, 177-185
    • (1996) Biotechnol. Appl. Biochem. , vol.24 , pp. 177-185
    • Sunna, A.1    Puls, J.2    Antranikian, G.3
  • 40
    • 0030249794 scopus 로고    scopus 로고
    • Purification and properties of the xylanase produced by Thermomyces lanuginoxus
    • 40. Cesar, T. and Mrsa, V. Purification and properties of the xylanase produced by Thermomyces lanuginoxus. Enzyme Microb. Technol. 1996, 19, 289-296
    • (1996) Enzyme Microb. Technol. , vol.19 , pp. 289-296
    • Cesar, T.1    Mrsa, V.2
  • 41
    • 0010656779 scopus 로고    scopus 로고
    • Specificity and mode of action of a thermostable xylanase from Bacillus amyloliquefaciens. On-line monitoring of hydrolysis products
    • 41. Breccia, J.D., Torto, N., Gorton, L., Siñeriz, F., and Hatti-Kaul, R. Specificity and mode of action of a thermostable xylanase from Bacillus amyloliquefaciens. On-line monitoring of hydrolysis products. Appl. Biochem. Biotechnol. 1997, 68, 167-175
    • (1997) Appl. Biochem. Biotechnol. , vol.68 , pp. 167-175
    • Breccia, J.D.1    Torto, N.2    Gorton, L.3    Siñeriz, F.4    Hatti-Kaul, R.5


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