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Volumn 7, Issue 21, 2008, Pages 3939-3948

Production, purification and characterization of celullase-free xylanase from Aspergillus terreus UL 4209

Author keywords

Aspergillus terreus; Cellulase free xylanase; MALDI TOF; Purification

Indexed keywords

CELLULASE; XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 56249112001     PISSN: None     EISSN: 16845315     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (28)

References (48)
  • 2
    • 0030971501 scopus 로고    scopus 로고
    • Micrbial xylanolytic enzyme system: Properties and applications
    • Bajpai P (1997). Micrbial xylanolytic enzyme system: properties and applications. Adv. Appl. Microbiol. 43: 141-194.
    • (1997) Adv. Appl. Microbiol , vol.43 , pp. 141-194
    • Bajpai, P.1
  • 5
    • 0034084579 scopus 로고    scopus 로고
    • High-level production of recombinant fungal endo-β-1,4- xylanase in the methylotrophic yeast Pichia pastoris
    • Berrin JG, Williamson G, Puigserver A, Chaix JC, McLauchlan WR, Juge N (2000) High-level production of recombinant fungal endo-β-1,4- xylanase in the methylotrophic yeast Pichia pastoris. Protein Exp. Purif. 19: 179-187.
    • (2000) Protein Exp. Purif , vol.19 , pp. 179-187
    • Berrin, J.G.1    Williamson, G.2    Puigserver, A.3    Chaix, J.C.4    McLauchlan, W.R.5    Juge, N.6
  • 6
    • 0022386956 scopus 로고
    • Microbial xylanolytic systems
    • Biely P (1985). Microbial xylanolytic systems. Trends Biotechnol. 3: 286-290.
    • (1985) Trends Biotechnol , vol.3 , pp. 286-290
    • Biely, P.1
  • 7
    • 0025700259 scopus 로고
    • Production, purification and characterization of xylanase from a hyperxylanolytic mutant of Aspergillus ochraceus
    • Biswas SR, Jana SC, Mishra AK, Nanda G (1990). Production, purification and characterization of xylanase from a hyperxylanolytic mutant of Aspergillus ochraceus. Biotechnol. Bioeng. 35: 244-251.
    • (1990) Biotechnol. Bioeng , vol.35 , pp. 244-251
    • Biswas, S.R.1    Jana, S.C.2    Mishra, A.K.3    Nanda, G.4
  • 8
    • 56249146532 scopus 로고    scopus 로고
    • The screening of culture condition and properties of xylanase by white rot fungus Pleorotus ostreatus
    • Cai Q, Yue T, Cheng J, Ma Q (2003). The screening of culture condition and properties of xylanase by white rot fungus Pleorotus ostreatus. Proc. Biochem. 25: 2-6.
    • (2003) Proc. Biochem , vol.25 , pp. 2-6
    • Cai, Q.1    Yue, T.2    Cheng, J.3    Ma, Q.4
  • 10
    • 32644489795 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a xylanase 10 from Apergillus terreus (BCC129) in Pichia pastoris
    • Chantasingh D, Pootanakit K, Champreda V, Kanokratana P, Eurwilaichitr L (2006). Cloning, expression and characterization of a xylanase 10 from Apergillus terreus (BCC129) in Pichia pastoris. Protein Exp. Purif. 46: 143-149.
    • (2006) Protein Exp. Purif , vol.46 , pp. 143-149
    • Chantasingh, D.1    Pootanakit, K.2    Champreda, V.3    Kanokratana, P.4    Eurwilaichitr, L.5
  • 12
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement (+/- 10 ppm) in protein identification strategies employing MS or MS/MS and database searching
    • Clauser KR, Baker PR, Burlingame AL (1999). Role of accurate mass measurement (+/- 10 ppm) in protein identification strategies employing MS or MS/MS and database searching. Anal. Chem. 71: 2871-2882.
    • (1999) Anal. Chem , vol.71 , pp. 2871-2882
    • Clauser, K.R.1    Baker, P.R.2    Burlingame, A.L.3
  • 13
    • 12144282020 scopus 로고    scopus 로고
    • Xylanase, xylanase families and extremophilic xylanase
    • Collins T, Gerday C, Feller G (2005). Xylanase, xylanase families and extremophilic xylanase. FEMS Microbiol. Rev. 29: 2-3.
    • (2005) FEMS Microbiol. Rev , vol.29 , pp. 2-3
    • Collins, T.1    Gerday, C.2    Feller, G.3
  • 14
    • 84981976048 scopus 로고
    • 1,4-D-xylan-degrading enzyme systems: Biochemistry,molecular biology and applications
    • Coughlan MP, Hazlewood GP (1993). -1,4-D-xylan-degrading enzyme systems: biochemistry,molecular biology and applications. Biotechnol. Appl. Biochem. 17: 259-289.
    • (1993) Biotechnol. Appl. Biochem , vol.17 , pp. 259-289
    • Coughlan, M.P.1    Hazlewood, G.P.2
  • 16
    • 0032844145 scopus 로고    scopus 로고
    • Purification of Aspergillus sp. Xylanase by precipitation with an anionic polymer Eudrajit S 100
    • Gawande P, Kamat MY (1999). Purification of Aspergillus sp. Xylanase by precipitation with an anionic polymer Eudrajit S 100. Process Biochem. 34: 577-580.
    • (1999) Process Biochem , vol.34 , pp. 577-580
    • Gawande, P.1    Kamat, M.Y.2
  • 17
    • 0027284092 scopus 로고
    • Aspergillus sydowii MG 49 is a strong producer of thermostable xylanolytic enzymes
    • Ghosh M, Das A, Mishra AK, Nanda G (1993). Aspergillus sydowii MG 49 is a strong producer of thermostable xylanolytic enzymes. Enzyme Microbial. Technol. 15: 703-709.
    • (1993) Enzyme Microbial. Technol , vol.15 , pp. 703-709
    • Ghosh, M.1    Das, A.2    Mishra, A.K.3    Nanda, G.4
  • 18
    • 0027946792 scopus 로고
    • Purification and some properties of a xylanase from Aspergillus sydowii MG49
    • Ghosh M, Nanda G (1994). Purification and some properties of a xylanase from Aspergillus sydowii MG49. Appl. Environ. Microbiol. 60: 4620-4623.
    • (1994) Appl. Environ. Microbiol , vol.60 , pp. 4620-4623
    • Ghosh, M.1    Nanda, G.2
  • 19
    • 0037411739 scopus 로고    scopus 로고
    • Developments in industrially important thermostable enzymes: A review
    • Haki GD, Rakshit SK (2003). Developments in industrially important thermostable enzymes: a review. Biores. Technol. 89: 17-34.
    • (2003) Biores. Technol , vol.89 , pp. 17-34
    • Haki, G.D.1    Rakshit, S.K.2
  • 21
    • 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
  • 22
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B, Bairoch A (1993). New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochemistry. 293: 781-788.
    • (1993) Biochemistry , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 23
    • 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
  • 24
    • 0029976603 scopus 로고    scopus 로고
    • Using Clustal for multiple sequence alignments
    • Higgins DG, Thompson JD, Gibson TJ (1996). Using Clustal for multiple sequence alignments. Meth. Enzymol. 266: 383-402.
    • (1996) Meth. Enzymol , vol.266 , pp. 383-402
    • Higgins, D.G.1    Thompson, J.D.2    Gibson, T.J.3
  • 25
    • 0026029476 scopus 로고
    • Induction of cellulose and xylan-degrading enzyme systems in Aspergillus terreus by homo and hetero-disaccharides composed of glucose and xylose
    • Hrmova M, Petrakova E, Biely P (1991). Induction of cellulose and xylan-degrading enzyme systems in Aspergillus terreus by homo and hetero-disaccharides composed of glucose and xylose. J. Gen. Microbiol. 137: 541-547.
    • (1991) J. Gen. Microbiol , vol.137 , pp. 541-547
    • Hrmova, M.1    Petrakova, E.2    Biely, P.3
  • 26
    • 77950470034 scopus 로고    scopus 로고
    • Enzyme processes for pulp and paper: A review of recent development in wood deterioration and preservation
    • Goodell B, Nicholas DD, Schultz TP Eds, 1953-IV. American Chemical Society Meeting, 22st, San Diego, CA
    • Kenealy RW, Jeffries TW (2003). Enzyme processes for pulp and paper: a review of recent development in wood deterioration and preservation. In: Goodell B, Nicholas DD, Schultz TP (Eds.) 1953-IV. American Chemical Society Meeting, 22st, San Diego, CA, V. Series, 2001, pp. 210-228.
    • (2001) V. Series , pp. 210-228
    • Kenealy, R.W.1    Jeffries, T.W.2
  • 27
    • 0032984477 scopus 로고    scopus 로고
    • Molecular and biotechnological aspects of xylanases
    • Kulkarni N, Shendye A, Rao M (1999). Molecular and biotechnological aspects of xylanases. FEMS Microbiol. Rev. 23: 411-456.
    • (1999) FEMS Microbiol. Rev , vol.23 , pp. 411-456
    • Kulkarni, N.1    Shendye, A.2    Rao, M.3
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of of the head of bacteriophage T4
    • Laemmli UK (1970). Cleavage of structural proteins during the assembly of of the head of bacteriophage T4. Nature, 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 33750594268 scopus 로고    scopus 로고
    • Lee-Chiang L, Chi-Yuang C, Yen-Ru P, Yaw-Kuen L, Jing-Jer L (2006). Rapid and selective isolation of β-xylosidase through an activity-based chemicalapproach. Biotechnol. J. 1: 197-202.
    • Lee-Chiang L, Chi-Yuang C, Yen-Ru P, Yaw-Kuen L, Jing-Jer L (2006). Rapid and selective isolation of β-xylosidase through an activity-based chemicalapproach. Biotechnol. J. 1: 197-202.
  • 30
    • 32844467765 scopus 로고    scopus 로고
    • Purification and characterization of a thermosatble cellulase-free xylanase from the newly isolated Paecilomyces themophila
    • Li L, Tian H, Cheng Y, Jiang Z, Yang S (2006). Purification and characterization of a thermosatble cellulase-free xylanase from the newly isolated Paecilomyces themophila. Enzyme Microbiol. Technol. 38: 780-787.
    • (2006) Enzyme Microbiol. Technol , vol.38 , pp. 780-787
    • Li, L.1    Tian, H.2    Cheng, Y.3    Jiang, Z.4    Yang, S.5
  • 31
    • 0022054102 scopus 로고
    • Applications of cellulases
    • Mandels M (1985). Applications of cellulases. Biochem. Soc. Trans. 13: 414-416.
    • (1985) Biochem. Soc. Trans , vol.13 , pp. 414-416
    • Mandels, M.1
  • 32
    • 33747333106 scopus 로고
    • Use if dinitrosalicylic acid reagent for determination of reducing sugars
    • Miller GL (1959). Use if dinitrosalicylic acid reagent for determination of reducing sugars. Anal. Biochem. 31: 426-428.
    • (1959) Anal. Biochem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 33
    • 33748578388 scopus 로고    scopus 로고
    • Production of cellulase-free endoxylanase from novel alkalophilic thermotolerant Bacillus pumilus by solid-state fermentation and its application in wastepaper recycling
    • Poorna CA, Prema P (2007). Production of cellulase-free endoxylanase from novel alkalophilic thermotolerant Bacillus pumilus by solid-state fermentation and its application in wastepaper recycling. Bioresour. Technol. 98: 485-490.
    • (2007) Bioresour. Technol , vol.98 , pp. 485-490
    • Poorna, C.A.1    Prema, P.2
  • 34
    • 0030334262 scopus 로고
    • Xylanases: From biology to biotechnology
    • Prade RA (1995). Xylanases: from biology to biotechnology. Biotechnol. Genet. Eng. Rev. 13: 100-131.
    • (1995) Biotechnol. Genet. Eng. Rev , vol.13 , pp. 100-131
    • Prade, R.A.1
  • 35
    • 56249099234 scopus 로고    scopus 로고
    • Enzyme technology: Fundamentals of precipitation with an anionic polymer, Eudrajit S100
    • Price CN, Stevens L (1999). Enzyme technology: Fundamentals of precipitation with an anionic polymer, Eudrajit S100. Proc. Biochem. 34: 577-580.
    • (1999) Proc. Biochem , vol.34 , pp. 577-580
    • Price, C.N.1    Stevens, L.2
  • 36
    • 0028987306 scopus 로고
    • Induction of endo-β -xylanase in the fungus Thermomyces lanuginosus
    • Purkarthofer H, Steiner W (1955). Induction of endo-β -xylanase in the fungus Thermomyces lanuginosus. Enzyme Microbiol. Technol. 17: 114-118.
    • (1955) Enzyme Microbiol. Technol , vol.17 , pp. 114-118
    • Purkarthofer, H.1    Steiner, W.2
  • 37
    • 0028965927 scopus 로고
    • Production of cellulase-free xylanase from alkali tolerant Aspergillus fischeri Fxn1
    • Raj KC, Chandra TS (1995). Production of cellulase-free xylanase from alkali tolerant Aspergillus fischeri Fxn1. Biotechnol. Lett. 17: 309-314.
    • (1995) Biotechnol. Lett , vol.17 , pp. 309-314
    • Raj, K.C.1    Chandra, T.S.2
  • 38
    • 0025324677 scopus 로고
    • Interrelationship of xylanase induction and cellulose induction of Trichoderma longibrachiatum
    • Royer JC, Nakas JP (1990). Interrelationship of xylanase induction and cellulose induction of Trichoderma longibrachiatum. Appl. Environ. Microbiol. 56: 2535-2539.
    • (1990) Appl. Environ. Microbiol , vol.56 , pp. 2535-2539
    • Royer, J.C.1    Nakas, J.P.2
  • 39
    • 0036090445 scopus 로고    scopus 로고
    • Production, purification and properties of a newly isolated Fusarium proliferatum
    • Saha BC (2002). Production, purification and properties of a newly isolated Fusarium proliferatum. Proc. Biochem. 37: 1279-1284.
    • (2002) Proc. Biochem , vol.37 , pp. 1279-1284
    • Saha, B.C.1
  • 41
    • 13844272454 scopus 로고    scopus 로고
    • Xylanase production by newly isolated Aspergillus foetidus strain and its characterization
    • Shah AR, Madamwar D (2005). Xylanase production by newly isolated Aspergillus foetidus strain and its characterization. Proc. Biochem. 40: 1763-1771.
    • (2005) Proc. Biochem , vol.40 , pp. 1763-1771
    • Shah, A.R.1    Madamwar, D.2
  • 43
    • 0023645371 scopus 로고
    • Studies on wild type strain of Schizophyllum commune: Cellulase and xylanase production and formation of extracellular polysaccharide schizophyllan
    • Steiner W, Lafferty RM, Gomes I, Esterbauer H (1987). Studies on wild type strain of Schizophyllum commune: Cellulase and xylanase production and formation of extracellular polysaccharide schizophyllan. Biotechnol. Bioeng. 30: 169-178.
    • (1987) Biotechnol. Bioeng , vol.30 , pp. 169-178
    • Steiner, W.1    Lafferty, R.M.2    Gomes, I.3    Esterbauer, H.4
  • 44
    • 0036210191 scopus 로고    scopus 로고
    • Biotechnology of microbial xylanases: Enzymology, molecular biology and application
    • Subramaniyan S, Prema P (2002). Biotechnology of microbial xylanases: Enzymology, molecular biology and application. Crit. Rev. Biotechnol. 22: 33-64.
    • (2002) Crit. Rev. Biotechnol , vol.22 , pp. 33-64
    • Subramaniyan, S.1    Prema, P.2
  • 46
    • 34250512499 scopus 로고
    • Recent progress in chemistry of wood hemicellulose
    • Timell TE (1967). Recent progress in chemistry of wood hemicellulose. Wood Sci. Technol. 1: 65.
    • (1967) Wood Sci. Technol , vol.1 , pp. 65
    • Timell, T.E.1
  • 48
    • 0024087074 scopus 로고
    • Multiplicity of beta-1,4-xylanases in microorganisms: Functions and applications
    • Wong KKY, Tan LUL, Saddler JN (1988). Multiplicity of beta-1,4-xylanases in microorganisms: functions and applications. Microbiol. Rev. 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


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