메뉴 건너뛰기




Volumn 22, Issue 10, 2012, Pages 1388-1394

Characterization of a recombinant thermostable xylanase from hot spring thermophilic Geobacillus sp. TC-W7

Author keywords

Characterization; Geobacillus sp. TC W7; Recombinant expression; Stable pH; Thermostable xylanase

Indexed keywords

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CHROMATOGRAPHY, AFFINITY; CLONING, MOLECULAR; EDETIC ACID; ENDO-1,4-BETA XYLANASES; ENZYME ACTIVATION; ENZYME ASSAYS; ENZYME INHIBITORS; ENZYME STABILITY; FERRIC COMPOUNDS; GENES, BACTERIAL; GENES, RRNA; GEOBACILLUS; HOT SPRINGS; HOT TEMPERATURE; HYDROGEN-ION CONCENTRATION; METALS, ALKALI; METALS, HEAVY; MOLECULAR SEQUENCE DATA; OCTOXYNOL; RECOMBINANT PROTEINS; RNA, RIBOSOMAL, 16S; XYLANS;

EID: 84930480208     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.1203.03045     Document Type: Article
Times cited : (28)

References (21)
  • 1
    • 35448990189 scopus 로고    scopus 로고
    • Production and partial characterization of cellulase free xylanase by Bacillus subtilis C01 using agriresidues and its application in biobleaching of nonwoody plant pulps
    • Ayyachamy, M. and T. M. Vatsala. 2007. Production and partial characterization of cellulase free xylanase by Bacillus subtilis C01 using agriresidues and its application in biobleaching of nonwoody plant pulps. Lett. Appl. Microbiol. 45: 467-472.
    • (2007) Lett. Appl. Microbiol. , vol.45 , pp. 467-472
    • Ayyachamy, M.1    Vatsala, T.M.2
  • 2
    • 0026537453 scopus 로고
    • Interlaboratory testing of methods for assay of xylanase activity
    • Bailey, M. J., P. Biely, and K. Poutanen. 1992. Interlaboratory testing of methods for assay of xylanase activity. J. Biotechnol. 23: 257-270.
    • (1992) J. Biotechnol. , vol.23 , pp. 257-270
    • Bailey, M.J.1    Biely, P.2    Poutanen, K.3
  • 3
    • 0032965966 scopus 로고    scopus 로고
    • Application of enzymes in the pulp and paper industry
    • Bajpai, P. 1999. Application of enzymes in the pulp and paper industry. Biotechnol. Prog. 15: 147-157.
    • (1999) Biotechnol. Prog. , vol.15 , pp. 147-157
    • Bajpai, P.1
  • 5
    • 0032851952 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of two xylanase-encoding genes from Cellulomonas pachnodae
    • Cazemier, A. E., J. C. Verdoes, A. J. van Ooyen, and H. J. Camp. 1999. Molecular and biochemical characterization of two xylanase-encoding genes from Cellulomonas pachnodae. Appl. Environ. Microbiol. 65: 4099-4107.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 4099-4107
    • Cazemier, A.E.1    Verdoes, J.C.2    van Ooyen, A.J.3    Camp, H.J.4
  • 6
    • 12144282020 scopus 로고    scopus 로고
    • Xylanases, xylanase families and extremophilic xylanases
    • Collins, T., C. Gerday, and G. Feller. 2005. Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol. Rev. 29: 3-23.
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 3-23
    • Collins, T.1    Gerday, C.2    Feller, G.3
  • 7
    • 33846427726 scopus 로고    scopus 로고
    • A novel cellulase free alkaliphilic xylanase from alkali tolerant Penicillium citrinum: Production, purification and characterization
    • Dutta, T., R. Sengupta, R. Sahoo, S. R. Sinha, A. Bhattacharjee, and S. Ghosh. 2007. A novel cellulase free alkaliphilic xylanase from alkali tolerant Penicillium citrinum: Production, purification and characterization. Lett. Appl. Microbiol. 44: 206-211.
    • (2007) Lett. Appl. Microbiol. , vol.44 , pp. 206-211
    • Dutta, T.1    Sengupta, R.2    Sahoo, R.3    Sinha, S.R.4    Bhattacharjee, A.5    Ghosh, S.6
  • 8
    • 29944447809 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of the xylanase gene from a Bacillus subtilis strain B10 in Escherichia coli
    • Huang, J., G. Wang, and L. Xiao. 2006. Cloning, sequencing and expression of the xylanase gene from a Bacillus subtilis strain B10 in Escherichia coli. Bioresour. Technol. 97: 802-808.
    • (2006) Bioresour. Technol. , vol.97 , pp. 802-808
    • Huang, J.1    Wang, G.2    Xiao, L.3
  • 9
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 10
    • 0002448290 scopus 로고
    • New developments in the application of enzymes for biomass processing
    • In M. P. Coughlan (ed.), Elsevier Applied Science, London
    • Linko, M., K. Poutanen, and L. Viikari. 1989. New developments in the application of enzymes for biomass processing, pp. 331-346. In M. P. Coughlan (ed.). Enzyme Systems for Lignocellulose Degradation. Elsevier Applied Science, London.
    • (1989) Enzyme Systems for Lignocellulose Degradation , pp. 331-346
    • Linko, M.1    Poutanen, K.2    Viikari, L.3
  • 11
    • 33745186246 scopus 로고    scopus 로고
    • Characterization of a recombinant maltogenic amylase from deep sea thermophilic Bacillus sp. WPD616
    • Liu, B., Y. Wang, and X. Zhang. 2006. Characterization of a recombinant maltogenic amylase from deep sea thermophilic Bacillus sp. WPD616. Enzyme Microb. Technol. 39: 805-810.
    • (2006) Enzyme Microb. Technol. , vol.39 , pp. 805-810
    • Liu, B.1    Wang, Y.2    Zhang, X.3
  • 12
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller, G. L. 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31: 426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 13
    • 34347351985 scopus 로고    scopus 로고
    • Application of Aspergillus fumigatus xylanase for quality improvement of waste paper pulp
    • Savitha, S., S. Sadhasivam, and K. Swaminathan. 2007. Application of Aspergillus fumigatus xylanase for quality improvement of waste paper pulp. Bull. Environ. Contam. Toxicol. 78: 217-221.
    • (2007) Bull. Environ. Contam. Toxicol. , vol.78 , pp. 217-221
    • Savitha, S.1    Sadhasivam, S.2    Swaminathan, K.3
  • 14
    • 13844272454 scopus 로고    scopus 로고
    • Xylanase production by a newly isolated Aspergillus foetidus strain and its characterization
    • Shah, A. R. and D. Madamwar. 2005. Xylanase production by a newly isolated Aspergillus foetidus strain and its characterization. Process Biochem. 40: 1763-1771.
    • (2005) Process Biochem , vol.40 , pp. 1763-1771
    • Shah, A.R.1    Madamwar, D.2
  • 15
    • 0035543091 scopus 로고    scopus 로고
    • Cloning, characterization, and expression of xylanase gene from Bacillus lyticus in Escherichia coli and Bacillus subtilis
    • Srivastava, P. and K. J. Mukherjee. 2001. Cloning, characterization, and expression of xylanase gene from Bacillus lyticus in Escherichia coli and Bacillus subtilis. Prep. Biochem. Biotechnol. 31: 389-400.
    • (2001) Prep. Biochem. Biotechnol. , vol.31 , pp. 389-400
    • Srivastava, P.1    Mukherjee, K.J.2
  • 16
    • 0036210191 scopus 로고    scopus 로고
    • Biotechnology of microbial xylanases: Enzymology, molecular biology, and application
    • Subramaniyan, S. and P. Prema. 2002. Biotechnology of microbial xylanases: Enzymology, molecular biology, and application. Crit. Rev. Biotechnol. 22: 33-46.
    • (2002) Crit. Rev. Biotechnol. , vol.22 , pp. 33-46
    • Subramaniyan, S.1    Prema, P.2
  • 17
    • 0029994845 scopus 로고    scopus 로고
    • Growth and production of xylanolytic enzymes by the extreme thermophilic anaerobic bacterium Thermotoga thermarum
    • Sunna, A. and G. Antranikian. 1996. Growth and production of xylanolytic enzymes by the extreme thermophilic anaerobic bacterium Thermotoga thermarum. Appl. Microbiol. Biotechnol. 45: 671-676.
    • (1996) Appl. Microbiol. Biotechnol. , vol.45 , pp. 671-676
    • Sunna, A.1    Antranikian, G.2
  • 18
    • 0000871895 scopus 로고
    • Hemicelluloses
    • In W. Pigman and D. Horton (eds.), Academic Press, New York
    • Whistler, R. L. and E. L. Richards. 1970. Hemicelluloses, pp. 447-469. In W. Pigman and D. Horton (eds.). The Carbohydrates. Academic Press, New York.
    • (1970) The Carbohydrates , pp. 447-469
    • Whistler, R.L.1    Richards, E.L.2
  • 19
    • 0002499398 scopus 로고
    • Use of complex formation between Congo red and polysaccharide in detection and assay of polysaccharide hydrolases
    • Wood, P., J. D. Erfle, and R. M. Teather. 1989. Use of complex formation between Congo red and polysaccharide in detection and assay of polysaccharide hydrolases. Methods Enzymol. 160: 59-74.
    • (1989) Methods Enzymol , vol.160 , pp. 59-74
    • Wood, P.1    Erfle, J.D.2    Teather, R.M.3
  • 20
    • 33749835413 scopus 로고    scopus 로고
    • Characterization of a recombinant thermostable xylanase from deep-sea thermophilic Geobacillus sp. MT-1 in East Pacific
    • Wu, S., B. Liu, and X. Zhang. 2006. Characterization of a recombinant thermostable xylanase from deep-sea thermophilic Geobacillus sp. MT-1 in East Pacific. Appl. Microbiol. Biotechnol. 72: 1210-1216.
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , pp. 1210-1216
    • Wu, S.1    Liu, B.2    Zhang, X.3
  • 21
    • 33645859900 scopus 로고    scopus 로고
    • High-level expression of an alpha-L-arabinofuranosidase from Thermotoga maritima in Escherichia coli for the production of xylobiose from xylan
    • Xue, Y., A. Wu, H. Zeng, and W. Shao. 2006. High-level expression of an alpha-L-arabinofuranosidase from Thermotoga maritima in Escherichia coli for the production of xylobiose from xylan. Biotechnol. Lett. 28: 351-356.
    • (2006) Biotechnol. Lett. , vol.28 , pp. 351-356
    • Xue, Y.1    Wu, A.2    Zeng, H.3    Shao, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.