메뉴 건너뛰기




Volumn 107, Issue 4, 2009, Pages 360-365

Gene cloning and characterization of a xylanase from a newly isolated Bacillus subtilis strain R5

Author keywords

16S rRNA; Bacillus subtilis R5; Cloning; Extracellular enzymes; Kinetic parameters; Xylanase

Indexed keywords

16S RRNA; 16S RRNA SEQUENCES; BACILLUS SUBTILIS R5; BACILLUS SUBTILIS STRAINS; BIO SURFACTANTS; BIOCHEMICAL CHARACTERISTICS; EXTRACELLULAR ENZYMES; GENE CLONINGS; GENE PRODUCTS; MESOPHILIC; METAL CATIONS; NACL CONCENTRATIONS; OPTIMAL GROWTHS; OPTIMUM PH; OSAKA , JAPANS; RECOMBINANT ENZYMES; RELATIVE MOLECULAR MASS; SUBTILIS; XYLANASE;

EID: 62949180128     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2008.12.005     Document Type: Article
Times cited : (34)

References (25)
  • 1
    • 0032984477 scopus 로고    scopus 로고
    • Molecular and biotechnological aspects of xylanases
    • Kulkarni N., Shendye A., and Rao M. Molecular and biotechnological aspects of xylanases. FEMS Microbiol. Rev. 23 (1999) 411-456
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 411-456
    • Kulkarni, N.1    Shendye, A.2    Rao, M.3
  • 2
    • 0036210191 scopus 로고    scopus 로고
    • Biotechnology of microbial xylanases: enzymology, molecular biology, and application
    • Subramaniyan S., and Prema P. Biotechnology of microbial xylanases: enzymology, molecular biology, and application. Crit. Rev. Biotechnol. 22 (2002) 33-64
    • (2002) Crit. Rev. Biotechnol. , vol.22 , pp. 33-64
    • Subramaniyan, S.1    Prema, P.2
  • 3
    • 12144282020 scopus 로고    scopus 로고
    • Xylanases, xylanase families and extremophilic xylanases
    • Collins T., Gerday C., and Feller G. Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol. Rev. 29 (2005) 3-23
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 3-23
    • Collins, T.1    Gerday, C.2    Feller, G.3
  • 4
    • 33144464649 scopus 로고    scopus 로고
    • Identification of an endo-beta-1,4-d-xylanase from Magnaporthe grisea by gene knockout analysis, purification, and heterologous expression
    • Wu S.C., Halley J.E., Luttig C., Fernekes L.M., Gutiérrez-Sanchez G., Darvill A.G., and Albersheim P. Identification of an endo-beta-1,4-d-xylanase from Magnaporthe grisea by gene knockout analysis, purification, and heterologous expression. Appl. Environ. Microbiol. 72 (2006) 986-993
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 986-993
    • Wu, S.C.1    Halley, J.E.2    Luttig, C.3    Fernekes, L.M.4    Gutiérrez-Sanchez, G.5    Darvill, A.G.6    Albersheim, P.7
  • 5
    • 46949085932 scopus 로고    scopus 로고
    • Bifunctional xylanases and their potential use in biotechnology
    • Khandeparker R., and Numan M.T. Bifunctional xylanases and their potential use in biotechnology. J. Ind. Microbiol. Biotechnol. 35 (2008) 635-644
    • (2008) J. Ind. Microbiol. Biotechnol. , vol.35 , pp. 635-644
    • Khandeparker, R.1    Numan, M.T.2
  • 6
    • 0242656502 scopus 로고    scopus 로고
    • Effect of xylanase and beta-glucanase supplementation of wheat- or wheat- and barley-based diets on the performance of male turkeys
    • Mathlouthi N., Juin H., and Larbier M. Effect of xylanase and beta-glucanase supplementation of wheat- or wheat- and barley-based diets on the performance of male turkeys. Br. Poult. Sci. 44 (2003) 291-298
    • (2003) Br. Poult. Sci. , vol.44 , pp. 291-298
    • Mathlouthi, N.1    Juin, H.2    Larbier, M.3
  • 7
    • 12344317255 scopus 로고    scopus 로고
    • Degradation of cell wall polysaccharides by combinations of carbohydrase enzymes and their effect on nutrient utilization and broiler chicken performance
    • Meng X., Slominski B.A., Nyachoti C.M., Campbell L.D., and Guenter W. Degradation of cell wall polysaccharides by combinations of carbohydrase enzymes and their effect on nutrient utilization and broiler chicken performance. Poult. Sci. 84 (2005) 37-47
    • (2005) Poult. Sci. , vol.84 , pp. 37-47
    • Meng, X.1    Slominski, B.A.2    Nyachoti, C.M.3    Campbell, L.D.4    Guenter, W.5
  • 8
    • 0037014323 scopus 로고    scopus 로고
    • Improvement of flour quality through carbohydrases treatment during wheat tempering
    • Haros M., Rosell C.M., and Benedito C. Improvement of flour quality through carbohydrases treatment during wheat tempering. J. Agric. Food Chem. 50 (2002) 4126-4130
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 4126-4130
    • Haros, M.1    Rosell, C.M.2    Benedito, C.3
  • 9
    • 0022580815 scopus 로고
    • A xylanase gene from Bacillus subtilis: nucleotide sequence and comparison with B. pumilus gene
    • Paice M.G., Bourbonnais R., Desrochers M., Jurasek L., and Yaguchi M. A xylanase gene from Bacillus subtilis: nucleotide sequence and comparison with B. pumilus gene. Arch. Microbiol. 144 (1986) 201-206
    • (1986) Arch. Microbiol. , vol.144 , pp. 201-206
    • Paice, M.G.1    Bourbonnais, R.2    Desrochers, M.3    Jurasek, L.4    Yaguchi, M.5
  • 11
    • 0031715687 scopus 로고    scopus 로고
    • Purification and properties of two thermostable alkaline xylanases from an alkaliphilic Bacillus sp
    • Gessesse A. Purification and properties of two thermostable alkaline xylanases from an alkaliphilic Bacillus sp. Appl. Environ. Microbiol. 64 (1998) 3533-3535
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3533-3535
    • Gessesse, A.1
  • 13
    • 50049119985 scopus 로고    scopus 로고
    • Efficient degradation of grease using microorganisms
    • Rashid N., and Imanaka T. Efficient degradation of grease using microorganisms. J. Chem. Soc. Pak. 30 (2008) 612-617
    • (2008) J. Chem. Soc. Pak. , vol.30 , pp. 612-617
    • Rashid, N.1    Imanaka, T.2
  • 16
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 17
    • 0002878518 scopus 로고
    • Ausubel F.A., Brent R., Kingston R.E., Moore D.D., Sediman J.G., Smith J.A., and Struhl K. (Eds), Greene Publishing and Wiley-Interscience, New York
    • Tabor S. In: Ausubel F.A., Brent R., Kingston R.E., Moore D.D., Sediman J.G., Smith J.A., and Struhl K. (Eds). Current protocols in molecular biology vol. 2 (1990), Greene Publishing and Wiley-Interscience, New York 16.2.1-16.2.11
    • (1990) Current protocols in molecular biology , vol.2
    • Tabor, S.1
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid as reagent for the determination of reducing sugars
    • Miller G.L. Use of dinitrosalicylic acid as reagent for the determination of reducing sugars. Anal. Chem. 31 (1959) 426-428
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 20
    • 0026537453 scopus 로고
    • Interlaboratory testing of methods for assay of xylanase activity
    • Bailey M., Biely P., and Poutanen K. Interlaboratory testing of methods for assay of xylanase activity. J. Biotechnol. 23 (1992) 257-270
    • (1992) J. Biotechnol. , vol.23 , pp. 257-270
    • Bailey, M.1    Biely, P.2    Poutanen, K.3
  • 21
    • 0342264573 scopus 로고    scopus 로고
    • Electroelution as a simple and fast protein purification method: isolation of an extracellular xylanase from Bacillus sp. CCMI 966
    • Sa -Pereira P., Duarte J., and Costa-Ferreira M. Electroelution as a simple and fast protein purification method: isolation of an extracellular xylanase from Bacillus sp. CCMI 966. Enzyme Microb. Technol. 27 (2000) 95-99
    • (2000) Enzyme Microb. Technol. , vol.27 , pp. 95-99
    • Sa -Pereira, P.1    Duarte, J.2    Costa-Ferreira, M.3
  • 22
    • 29944447809 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of the xylanase gene from a Bacillus subtilis strain B10 in Escherichia coli
    • Huang J., Wang G., and Xiao L. Cloning, sequencing and expression of the xylanase gene from a Bacillus subtilis strain B10 in Escherichia coli. Bioresource Technol. 97 (2006) 802-808
    • (2006) Bioresource Technol. , vol.97 , pp. 802-808
    • Huang, J.1    Wang, G.2    Xiao, L.3
  • 23
    • 1642271576 scopus 로고    scopus 로고
    • Cloning and characterization of xylanase A from the strain Bacillus sp. BP-7: comparison with alkaline pI low molecular weight xylanases of family 11
    • Gallardo O., Pilar D., and Pastor F.I.J. Cloning and characterization of xylanase A from the strain Bacillus sp. BP-7: comparison with alkaline pI low molecular weight xylanases of family 11. Appl. Microbial. Biotechnol. 48 (2004) 276-279
    • (2004) Appl. Microbial. Biotechnol. , vol.48 , pp. 276-279
    • Gallardo, O.1    Pilar, D.2    Pastor, F.I.J.3
  • 24
    • 0026951036 scopus 로고
    • Purification and general properties of xylanase from Aspergilus terreus
    • Ghareib M. Purification and general properties of xylanase from Aspergilus terreus. Zentralbl Mikrobiol. 147 (1992) 569-576
    • (1992) Zentralbl Mikrobiol. , vol.147 , pp. 569-576
    • Ghareib, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.