메뉴 건너뛰기




Volumn 55, Issue 5, 2009, Pages 329-334

Characterization and application of recombinant β-glucosidase (BglH) from Bacillus licheniformis KCTC 1918

Author keywords

Cellulose; Cellulose degradation; Glucosidase

Indexed keywords

BACTERIOLOGY; CLONING; ELECTROPHORESIS; ENCODING (SYMBOLS); ENZYME ACTIVITY; GENE ENCODING; HYDROLYSIS; SIGNAL ENCODING; SODIUM DODECYL SULFATE; SULFUR COMPOUNDS; UREA; WOOD;

EID: 70350602566     PISSN: 14350211     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10086-009-1044-2     Document Type: Article
Times cited : (15)

References (33)
  • 1
    • 33747823854 scopus 로고    scopus 로고
    • A specific short dextrin-hydrolyzing extracellular glucosidase from the thermophilic fungus Thermoascus aurantiacus 179-5
    • Caralho AFAC, Goncalves AZ, da Silva R, Gomes E (2006) A specific short dextrin-hydrolyzing extracellular glucosidase from the thermophilic fungus Thermoascus aurantiacus 179-5. J Microbiol 44:276-283.
    • (2006) J Microbiol , vol.44 , pp. 276-283
    • Caralho, A.F.A.C.1    Goncalves, A.Z.2    da Silva, R.3    Gomes, E.4
  • 2
    • 0035965060 scopus 로고    scopus 로고
    • Characterization of a thermostable β-glucosidase (BglB) from Thermotoga maritima showing transglycosylation activity
    • Goyal K, Selvakumar P, Hayashi K (2001) Characterization of a thermostable β-glucosidase (BglB) from Thermotoga maritima showing transglycosylation activity. J Mol Catal B 15:45-53.
    • (2001) J Mol Catal B , vol.15 , pp. 45-53
    • Goyal, K.1    Selvakumar, P.2    Hayashi, K.3
  • 4
    • 0034811848 scopus 로고    scopus 로고
    • Cloning of a Paenibacillus sp. endo-β-1,4-glucanase gene and its coexpression with the Endomyces fibuliger β-glucosidase gene in Saccharomyces cerevisiae
    • Park JN, Kim HO, Shin DJ, Kim HJ, Lee HB, Chun SB, Bai S (2001) Cloning of a Paenibacillus sp. endo-β-1,4-glucanase gene and its coexpression with the Endomyces fibuliger β-glucosidase gene in Saccharomyces cerevisiae. J Microbiol Biotechnol 11: 685-692.
    • (2001) J Microbiol Biotechnol , vol.11 , pp. 685-692
    • Park, J.N.1    Kim, H.O.2    Shin, D.J.3    Kim, H.J.4    Lee, H.B.5    Chun, S.B.6    Bai, S.7
  • 5
    • 2442638138 scopus 로고    scopus 로고
    • Differential transcription of β-glucosidase and cellobiose dehydrogenase genes in cellulose degradation by the basidiomycete Phanerochaete chrysosporium
    • Yoshida M, Igarashi K, Kawai R, Aida K, Samejima M (2004) Differential transcription of β-glucosidase and cellobiose dehydrogenase genes in cellulose degradation by the basidiomycete Phanerochaete chrysosporium. FEMS Microbiol Lett 235:177-182.
    • (2004) FEMS Microbiol Lett , vol.235 , pp. 177-182
    • Yoshida, M.1    Igarashi, K.2    Kawai, R.3    Aida, K.4    Samejima, M.5
  • 7
    • 0031295876 scopus 로고    scopus 로고
    • Cellulose degradation enzymes and their potential industrial applications
    • Bhat MK, Bhat S (1997) Cellulose degradation enzymes and their potential industrial applications. Biotechnol Adv 15:583-620.
    • (1997) Biotechnol Adv , vol.15 , pp. 583-620
    • Bhat, M.K.1    Bhat, S.2
  • 9
    • 0027469655 scopus 로고
    • Purification, characterization, gene cloning, and sequencing of a new β-glucosidase from Bacillus circulans subsp. alkalophilus
    • Paavilainen S, Hellman J, Korpela T (1993) Purification, characterization, gene cloning, and sequencing of a new β-glucosidase from Bacillus circulans subsp. alkalophilus. Appl Environ Microb 59:927-932.
    • (1993) Appl Environ Microb , vol.59 , pp. 927-932
    • Paavilainen, S.1    Hellman, J.2    Korpela, T.3
  • 10
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B (1991) A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 280:309-316.
    • (1991) Biochem J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 11
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence based classification of glycoside hydrolases
    • Henrissat B, Davies G (1997) Structural and sequence based classification of glycoside hydrolases. Curr Opin Struct Biol 7:637-644.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 12
    • 0028268204 scopus 로고
    • Structural similarity of plant chitinase and lysozymes from animals and phage
    • Holm L, Sander C (1994) Structural similarity of plant chitinase and lysozymes from animals and phage. FEBS Lett 340:129-132.
    • (1994) FEBS Lett , vol.340 , pp. 129-132
    • Holm, L.1    Sander, C.2
  • 13
    • 0028982269 scopus 로고
    • Construction of chimeric β-glucosidases with improved enzymatic properties
    • Singh A, Hayashi K (1995) Construction of chimeric β-glucosidases with improved enzymatic properties. J Biol Chem 270:21928-21933.
    • (1995) J Biol Chem , vol.270 , pp. 21928-21933
    • Singh, A.1    Hayashi, K.2
  • 14
    • 0026770535 scopus 로고
    • Purification and characterization of a Bacillus polymyxa β-glucosidase expressed in Escherichia coli
    • Painbeni E, Valles S, Polaina J, Flors A (1992) Purification and characterization of a Bacillus polymyxa β-glucosidase expressed in Escherichia coli. J Bacteriol 174:3087-3091.
    • (1992) J Bacteriol , vol.174 , pp. 3087-3091
    • Painbeni, E.1    Valles, S.2    Polaina, J.3    Flors, A.4
  • 15
    • 38549170356 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of two β-glucosidases from isoflavone glycosidase-hydrolyzing Bacillus subtilis natto
    • Kuo LC, Lee KT (2008) Cloning, expression, and characterization of two β-glucosidases from isoflavone glycosidase-hydrolyzing Bacillus subtilis natto. J Agr Food Chem 56:119-125.
    • (2008) J Agr Food Chem , vol.56 , pp. 119-125
    • Kuo, L.C.1    Lee, K.T.2
  • 16
    • 0031032671 scopus 로고    scopus 로고
    • Identification and characterization of a new β-glucoside utilization system in Bacillus subtilis
    • Tobisch S, Glaser P, Kruger S, Hecker M (1997) Identification and characterization of a new β-glucoside utilization system in Bacillus subtilis. J Bacteriol 179:496-506.
    • (1997) J Bacteriol , vol.179 , pp. 496-506
    • Tobisch, S.1    Glaser, P.2    Kruger, S.3    Hecker, M.4
  • 17
    • 0025811139 scopus 로고
    • A simple method for the isolation of chromosomal DNA from gram positive or acid-fast bacteria
    • Bollet C, Gevaudan MJ, Lamballerie X, Zandotti C, Micco P (1991) A simple method for the isolation of chromosomal DNA from gram positive or acid-fast bacteria. Nucleic Acids Res 19: 1955.
    • (1991) Nucleic Acids Res , vol.19 , pp. 1955
    • Bollet, C.1    Gevaudan, M.J.2    Lamballerie, X.3    Zandotti, C.4    Micco, P.5
  • 18
    • 0026941151 scopus 로고
    • Purification and characterization of two extracellular β-glucosidases from Aspergillus nidulans
    • Kwon KS, Kang HG, Hah YC (1992) Purification and characterization of two extracellular β-glucosidases from Aspergillus nidulans. FEMS Microbiol Lett 97:149-154.
    • (1992) FEMS Microbiol Lett , vol.97 , pp. 149-154
    • Kwon, K.S.1    Kang, H.G.2    Hah, Y.C.3
  • 19
    • 0142195885 scopus 로고    scopus 로고
    • A comparative study between an endoglucanase IV and its fused protein complex Cel5-CBM6
    • Bae HJ, Turcotte G, Chamberland H, Karita S, Vezina LP (2003) A comparative study between an endoglucanase IV and its fused protein complex Cel5-CBM6, FEMS Microbiol Lett 227:175-181.
    • (2003) FEMS Microbiol Lett , vol.227 , pp. 175-181
    • Bae, H.J.1    Turcotte, G.2    Chamberland, H.3    Karita, S.4    Vezina, L.P.5
  • 20
    • 0037300835 scopus 로고    scopus 로고
    • Purification and characterization of a cellulase-free xylanase of a moderate thermophile Bacillus licheniformis A99
    • Archana A, Satyanarayana T (2003) Purification and characterization of a cellulase-free xylanase of a moderate thermophile Bacillus licheniformis A99. World J Microb Biotechnol 19:53-57.
    • (2003) World J Microb Biotechnol , vol.19 , pp. 53-57
    • Archana, A.1    Satyanarayana, T.2
  • 21
    • 0037569631 scopus 로고    scopus 로고
    • Presteady-state kinetics of Bacillus licheniformis 1,3-1,4-β-glucanase: Evidence for a regulatory binding state
    • Abel M, Iversen K, Planas A, Christensen U (2003) Presteady-state kinetics of Bacillus licheniformis 1,3-1,4-β-glucanase: evidence for a regulatory binding state. Biochem J 371:997-1003.
    • (2003) Biochem J , vol.371 , pp. 997-1003
    • Abel, M.1    Iversen, K.2    Planas, A.3    Christensen, U.4
  • 22
    • 0038344488 scopus 로고    scopus 로고
    • Family 3 β-glucosidase from cellulose-degrading culture of the white-rot fungus Phanerochaete chrysosporium is a glucan 1,3-β-glucosidase
    • Igarashi K, Tani T, Kawaki R, Samegima M (2003) Family 3 β-glucosidase from cellulose-degrading culture of the white-rot fungus Phanerochaete chrysosporium is a glucan 1,3-β-glucosidase. J Biosci Bioeng 95:572-576.
    • (2003) J Biosci Bioeng , vol.95 , pp. 572-576
    • Igarashi, K.1    Tani, T.2    Kawaki, R.3    Samegima, M.4
  • 23
    • 34247098005 scopus 로고    scopus 로고
    • Purification and biochemical characterization of an extracellular β-glucosidase from the wood-decaying fungus Daldinia eschscholzii (Ehrenb.:Fr.) Rehm
    • Karnchanatat A, Petsom A, Sanvanich P, Piaphukiew J, Whalley AJ, Reynolds CD, Sihanonth P (2007) Purification and biochemical characterization of an extracellular β-glucosidase from the wood-decaying fungus Daldinia eschscholzii (Ehrenb.:Fr.) Rehm. FEMS Microbiol Lett 270:162-170.
    • (2007) FEMS Microbiol Lett , vol.270 , pp. 162-170
    • Karnchanatat, A.1    Petsom, A.2    Sanvanich, P.3    Piaphukiew, J.4    Whalley, A.J.5    Reynolds, C.D.6    Sihanonth, P.7
  • 24
    • 0025182502 scopus 로고
    • Three-dimensional structure of cellobiohydrolase II from Tricoderma reesei
    • Rouvinen J, Bergfors T, Teeri T, Knowles J, Jone T (1990) Three-dimensional structure of cellobiohydrolase II from Tricoderma reesei. Science 249:380-386.
    • (1990) Science , vol.249 , pp. 380-386
    • Rouvinen, J.1    Bergfors, T.2    Teeri, T.3    Knowles, J.4    Jone, T.5
  • 25
    • 0029310610 scopus 로고
    • Purification and properties of a wall-bound endo-1,4-β-glucanase from suspension-cultured poplar cells
    • Ohmiya Y, Takeda T, Nakamura S, Sakai F, Hayashi T (1995) Purification and properties of a wall-bound endo-1,4-β-glucanase from suspension-cultured poplar cells. Plant Cell Physiol 36: 607-614.
    • (1995) Plant Cell Physiol , vol.36 , pp. 607-614
    • Ohmiya, Y.1    Takeda, T.2    Nakamura, S.3    Sakai, F.4    Hayashi, T.5
  • 26
    • 0028786543 scopus 로고
    • Purification and characterization of an intracellular β-glucosidase from Botrytis cinerea
    • Gueguen Y, Chemardin P, Arnaud A, Galzy P (1995) Purification and characterization of an intracellular β-glucosidase from Botrytis cinerea. Enzyme Microb Tech 17:900-906.
    • (1995) Enzyme Microb Tech , vol.17 , pp. 900-906
    • Gueguen, Y.1    Chemardin, P.2    Arnaud, A.3    Galzy, P.4
  • 27
    • 0031685554 scopus 로고    scopus 로고
    • Purification, characterization, and substrate specificity of a novel highly glucose tolerant β-glucosidase from Asperillus oryzae
    • Riou C, Salmon J, Vallier M, Gunata Z, Barre P (1998) Purification, characterization, and substrate specificity of a novel highly glucose tolerant β-glucosidase from Asperillus oryzae. Appl Environ Microb 64:3607-3614.
    • (1998) Appl Environ Microb , vol.64 , pp. 3607-3614
    • Riou, C.1    Salmon, J.2    Vallier, M.3    Gunata, Z.4    Barre, P.5
  • 28
    • 0026770535 scopus 로고
    • Purification and characterization of a Bacillus polymyxa β-glucosidase expressed in Escherichia coli
    • Eric P, Salvador V, Julio P, Agusti F (1992) Purification and characterization of a Bacillus polymyxa β-glucosidase expressed in Escherichia coli. J Bacteriol 174:3087-3091.
    • (1992) J Bacteriol , vol.174 , pp. 3087-3091
    • Eric, P.1    Salvador, V.2    Julio, P.3    Agusti, F.4
  • 29
    • 0034644552 scopus 로고    scopus 로고
    • Purification and characterization of cellulase produced by two Bacillus strains
    • Mawadza C, Kaul R, Zvauya R, Mattiasson B (2000) Purification and characterization of cellulase produced by two Bacillus strains. J Biotechnol 83:177-187.
    • (2000) J Biotechnol , vol.83 , pp. 177-187
    • Mawadza, C.1    Kaul, R.2    Zvauya, R.3    Mattiasson, B.4
  • 30
    • 0037298812 scopus 로고    scopus 로고
    • Purification and characterization of two intracellular β-glucosidases from the Neurospora crassa mutant cell-1
    • Yazdi MT, Khosravi AA, Nemati M, Motlagh DV (2003) Purification and characterization of two intracellular β-glucosidases from the Neurospora crassa mutant cell-1. World J Microb Biotechnol 19:79-84.
    • (2003) World J Microb Biotechnol , vol.19 , pp. 79-84
    • Yazdi, M.T.1    Khosravi, A.A.2    Nemati, M.3    Motlagh, D.V.4
  • 32
    • 34249809704 scopus 로고    scopus 로고
    • Optimization of enzyme complexes for lignocelluloses hydrolysis
    • Berlin A, Maximenko A, Gilkes N, Saddler J (2007) Optimization of enzyme complexes for lignocelluloses hydrolysis. Biotechnol Bioeng 97:287-296.
    • (2007) Biotechnol Bioeng , vol.97 , pp. 287-296
    • Berlin, A.1    Maximenko, A.2    Gilkes, N.3    Saddler, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.