메뉴 건너뛰기




Volumn 5, Issue 3, 2006, Pages 351-356

Purification and characterization of an endoxylanase from solid-state culture of alkalitolerant Aspergillus fumigatus MKU1

Author keywords

Aspergillus fumigatus; Biochemical characterization; Purification; Solid state culture; Xylanase

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); ALKALI; CARBOXYMETHYLCELLULOSE; COPPER ION; CYSTEINE; DITHIOTHREITOL; FERRIC ION; MERCURY; XYLAN; XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 33748452250     PISSN: 09725849     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper
Times cited : (2)

References (33)
  • 1
    • 0028245641 scopus 로고
    • The xylan-degrading enzyme system
    • Filho E X F, The xylan-degrading enzyme system, Braz J Med Biol Res, 27 (1994) 1093-1109.
    • (1994) Braz J Med Biol Res , vol.27 , pp. 1093-1109
    • Filho, E.X.F.1
  • 2
    • 0030971501 scopus 로고    scopus 로고
    • Microbial xylanolytic enzyme system: Properties and applications
    • Bajpai P, Microbial xylanolytic enzyme system: Properties and applications, Adv Appl Microbiol, 43 (1997) 141-194.
    • (1997) Adv Appl Microbiol , vol.43 , pp. 141-194
    • Bajpai, P.1
  • 3
    • 0003035453 scopus 로고
    • Mechanisms of enzymic hydrolysis of hemicelluloses (xylans) and procedures for determination of the enzyme activity involved
    • edited by M P Coughlan (Elsevier Applied Science, London)
    • Puls J & Poutanen K, Mechanisms of enzymic hydrolysis of hemicelluloses (xylans) and procedures for determination of the enzyme activity involved, in Enzyme systems for lignocellulose degradation, edited by M P Coughlan (Elsevier Applied Science, London) 1989, 151-2165.
    • (1989) Enzyme Systems for Lignocellulose Degradation , pp. 151-2165
    • Puls, J.1    Poutanen, K.2
  • 5
    • 0024087074 scopus 로고
    • Multiplicity of β-1,4-xylanase in microorganisms: Functions and applications
    • Wong K K Y, Tan L U L & Saddler J N, Multiplicity of β-1,4-xylanase in microorganisms: Functions and applications, Microbiol Rev, 52 (1988) 305-317.
    • (1988) Microbiol Rev , vol.52 , pp. 305-317
    • Wong, K.K.Y.1    Tan, L.U.L.2    Saddler, J.N.3
  • 6
    • 0141782482 scopus 로고    scopus 로고
    • Purification and characterization of a new low molecular weight endoxylanase from Penicillium capsulatum
    • Ryan S E, Nolan K, Thompson R, Gubitz G M, Savage A V et al, Purification and characterization of a new low molecular weight endoxylanase from Penicillium capsulatum, Enzyme Microb Technol, 33 (2003) 775-785.
    • (2003) Enzyme Microb Technol , vol.33 , pp. 775-785
    • Ryan, S.E.1    Nolan, K.2    Thompson, R.3    Gubitz, G.M.4    Savage, A.V.5
  • 7
    • 0034857415 scopus 로고    scopus 로고
    • Xylanase from a newly isolated Fusarium verticillioides capable of utilizing corn fiber xylan
    • Saha B C, Xylanase from a newly isolated Fusarium verticillioides capable of utilizing corn fiber xylan, Appl Microbiol Biotechnol, 56 (2001), 762-766.
    • (2001) Appl Microbiol Biotechnol , vol.56 , pp. 762-766
    • Saha, B.C.1
  • 8
    • 0038095190 scopus 로고    scopus 로고
    • Purification and characterization of a novel cellulase-free xylanase from Acrophialophora nainiana
    • Cardoso O A V & Filho E X F, Purification and characterization of a novel cellulase-free xylanase from Acrophialophora nainiana, FEMS Microbiol Lett, 223 (2003) 309-314.
    • (2003) FEMS Microbiol Lett , vol.223 , pp. 309-314
    • Cardoso, O.A.V.1    Filho, E.X.F.2
  • 9
    • 0031104640 scopus 로고    scopus 로고
    • Purification and characterization of an acidic endo-β-1,4-xylanase from the tomato vascular pathogen Fusarium oxysporum f. sp. lycopersici
    • Ruiz M C, Di Pietroa A & Roncero M I G, Purification and characterization of an acidic endo-β-1,4-xylanase from the tomato vascular pathogen Fusarium oxysporum f. sp. lycopersici, FEMS Microbiol Lett, 148 (1997) 75-82.
    • (1997) FEMS Microbiol Lett , vol.148 , pp. 75-82
    • Ruiz, M.C.1    Di Pietroa, A.2    Roncero, M.I.G.3
  • 10
    • 0033230280 scopus 로고    scopus 로고
    • Characterization of neutral xylanases from Chaetomium cellulolyticum and their biobleaching effect on eucalyptus pulp
    • Baraznenok V A, Becker E G, Ankudimova N V & Okunev N N, Characterization of neutral xylanases from Chaetomium cellulolyticum and their biobleaching effect on eucalyptus pulp, Enzyme Microb Technol, 25 (1999) 651-659.
    • (1999) Enzyme Microb Technol , vol.25 , pp. 651-659
    • Baraznenok, V.A.1    Becker, E.G.2    Ankudimova, N.V.3    Okunev, N.N.4
  • 11
    • 0026537453 scopus 로고
    • Interlaboratory testing of methods for asssay of xylanase activity
    • Bailey M J, Biely P & Poutanen K, Interlaboratory testing of methods for asssay of xylanase activity, J Biotechnol, 23 (1992) 257-270.
    • (1992) J Biotechnol , vol.23 , pp. 257-270
    • Bailey, M.J.1    Biely, P.2    Poutanen, K.3
  • 12
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for the determination of reducing sugar
    • Miller G L, Use of dinitrosalicylic acid reagent for the determination of reducing sugar, Anal Chem, 31 (1959) 426-428.
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 14
    • 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 & 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
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U K, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature (Lond), 227 (1970) 680-685.
    • (1970) Nature (Lond) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 33751330608 scopus 로고
    • The determination of the enzyme dissociation
    • Lineweaver H & Burk D, The determination of the enzyme dissociation, J Am Chem Soc, 56 (1934) 658-66.
    • (1934) J Am Chem Soc , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 17
    • 0032984477 scopus 로고    scopus 로고
    • Molecular and biotechnological aspects of xylanases
    • Kulkarni N, Shendye A & Rao M, Molecular and biotechnological aspects of xylanases, FEMS Microbiol Rev, 23 (1998) 411-456.
    • (1998) FEMS Microbiol Rev , vol.23 , pp. 411-456
    • Kulkarni, N.1    Shendye, A.2    Rao, M.3
  • 18
    • 0033573878 scopus 로고    scopus 로고
    • Extractive cultivation of recombinant Escherichia coli using aqueous two phase systems for production and separation of extracellular xylanase
    • Kulkarni N, Vaidya A & Rao M, Extractive cultivation of recombinant Escherichia coli using aqueous two phase systems for production and separation of extracellular xylanase, Biochem Biophys Res Commun, 255 (1999) 274-278.
    • (1999) Biochem Biophys Res Commun , vol.255 , pp. 274-278
    • Kulkarni, N.1    Vaidya, A.2    Rao, M.3
  • 19
    • 16544378227 scopus 로고    scopus 로고
    • Purification and characterization of a low molecular weight endoxylanase from solid state cultures of alkali-tolerant Aspergillus fischeri
    • Senthilkumar S R, Ashokumar B, Chandra Raj K & Gunasekaran P, Purification and characterization of a low molecular weight endoxylanase from solid state cultures of alkali-tolerant Aspergillus fischeri, Biotechnol Lett, 26 (2004) 1283-1287.
    • (2004) Biotechnol Lett , vol.26 , pp. 1283-1287
    • Senthilkumar, S.R.1    Ashokumar, B.2    Chandra Raj, K.3    Gunasekaran, P.4
  • 21
    • 0027246551 scopus 로고
    • Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6
    • Khasin A, Alchanati I & Sholam Y, Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6, Appl Environ Microbiol, 59 (1993) 1725-1730.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 1725-1730
    • Khasin, A.1    Alchanati, I.2    Sholam, Y.3
  • 22
    • 0027595156 scopus 로고
    • Biochemical characteristics of two endo-β-1,4-xylanases produced by Penicillium capsulatum
    • Filho E X F, Puls J & Coughlan M P, Biochemical characteristics of two endo-β-1,4-xylanases produced by Penicillium capsulatum, J Ind Microbiol, 11 (1993) 171-180.
    • (1993) J Ind Microbiol , vol.11 , pp. 171-180
    • Filho, E.X.F.1    Puls, J.2    Coughlan, M.P.3
  • 25
    • 0035370202 scopus 로고    scopus 로고
    • A combination of weakly stabilizing mutations with a disulfide bridge in the α-helix region of Trichoderma reesei endo-1,4-β-xylanase II increases the thermal stability through synergism
    • Turunen O, Etuaho K, Fenel F, Vhmaanperä J, Wu X et al, A combination of weakly stabilizing mutations with a disulfide bridge in the α-helix region of Trichoderma reesei endo-1,4-β-xylanase II increases the thermal stability through synergism, J Biotechnol, 88 (2001) 37-46.
    • (2001) J Biotechnol , vol.88 , pp. 37-46
    • Turunen, O.1    Etuaho, K.2    Fenel, F.3    Vhmaanperä, J.4    Wu, X.5
  • 26
    • 0028271827 scopus 로고
    • Increase in catalytic activity and thermostability of the xylanase a of Streptomyces lividans 1326 by site-specific mutagenesis
    • Moreau A, Shareck F, Kluepfel D & Morosoli R, Increase in catalytic activity and thermostability of the xylanase A of Streptomyces lividans 1326 by site-specific mutagenesis, Enzyme Microb Technol, 16 (1994) 420-424.
    • (1994) Enzyme Microb Technol , vol.16 , pp. 420-424
    • Moreau, A.1    Shareck, F.2    Kluepfel, D.3    Morosoli, R.4
  • 27
    • 0032816375 scopus 로고    scopus 로고
    • Purification and biochemical characteristics of β-D-xylanase from a thermophilic fungus Thermomyces lanuginosus-SSBP
    • Lin J, Ndlovu L M, Singh S & Pillay B, Purification and biochemical characteristics of β-D-xylanase from a thermophilic fungus Thermomyces lanuginosus-SSBP, Biotechnol Appl Biochem, 30 (1999) 73-79.
    • (1999) Biotechnol Appl Biochem , vol.30 , pp. 73-79
    • Lin, J.1    Ndlovu, L.M.2    Singh, S.3    Pillay, B.4
  • 28
    • 0022045528 scopus 로고
    • Purification and characterization of endoxylanases from Aspergillus niger. Part III. An enzyme of pI 3.65
    • Fournier A R, Frederick M M, Frederick J R & Reilly P J, Purification and characterization of endoxylanases from Aspergillus niger. Part III. An enzyme of pI 3.65, Biotechnol Bioeng, 27 (1985) 539-545.
    • (1985) Biotechnol Bioeng , vol.27 , pp. 539-545
    • Fournier, A.R.1    Frederick, M.M.2    Frederick, J.R.3    Reilly, P.J.4
  • 29
    • 0022042987 scopus 로고
    • Purification and characterization of endoxylanases from Aspergillus niger. Part II. An enzyme of pI 4.5
    • Shei J C, Fratzke A R, Frederick M M, Frederick J R & Reilly P J, Purification and characterization of endoxylanases from Aspergillus niger. Part II. An enzyme of pI 4.5, Biotechnol Bioeng, 27 (1985) 533-538.
    • (1985) Biotechnol Bioeng , vol.27 , pp. 533-538
    • Shei, J.C.1    Fratzke, A.R.2    Frederick, M.M.3    Frederick, J.R.4    Reilly, P.J.5
  • 30
    • 0034714124 scopus 로고    scopus 로고
    • Purification and characterization of a new xylanase from Acrophialophora nainiana
    • Salles B C, Cunha R B, Fontes W, Sousa M V & Filho E X F, Purification and characterization of a new xylanase from Acrophialophora nainiana, J Biotechnol, 81 (2000) 199-204.
    • (2000) J Biotechnol , vol.81 , pp. 199-204
    • Salles, B.C.1    Cunha, R.B.2    Fontes, W.3    Sousa, M.V.4    Filho, E.X.F.5
  • 31
    • 0025107503 scopus 로고
    • Chemical modification of xylanases: Evidence for essential tryptophan and cyesteine residues at the active site
    • Deshpande V, Hinge J & Ray M, Chemical modification of xylanases: Evidence for essential tryptophan and cyesteine residues at the active site, Biochim Biophys Acta. 1031 (1990) 172-177.
    • (1990) Biochim Biophys Acta. , vol.1031 , pp. 172-177
    • Deshpande, V.1    Hinge, J.2    Ray, M.3
  • 32
    • 0028200558 scopus 로고
    • Purification, characterization and substrate specificities of multiple xylanases from Streptomyces sp. Strain B-12-2
    • Egir G, Szakacs G & Jeffries T W, Purification, characterization and substrate specificities of multiple xylanases from Streptomyces sp. Strain B-12-2, Appl Environ Microbiol, 60 (1994) 2609-2615.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 2609-2615
    • Egir, G.1    Szakacs, G.2    Jeffries, T.W.3
  • 33
    • 0035064322 scopus 로고    scopus 로고
    • Purification and characterisation of xylanolytic enzymes of a cellulase-free thermophilic strain of Clostridium absonum CFR-702
    • Rani D S & Nand K, Purification and characterisation of xylanolytic enzymes of a cellulase-free thermophilic strain of Clostridium absonum CFR-702, Anaerobe, 7 (2001) 45-53.
    • (2001) Anaerobe , vol.7 , pp. 45-53
    • Rani, D.S.1    Nand, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.