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Volumn 47, Issue 7-8, 2009, Pages 547-558

Cloning and Expression of a Novel Chitinase chi58 from Chaetomium cupreum in Pichia pastoris

Author keywords

Chitin binding domain; Chitinase; Inverse PCR; Pichia pastoris

Indexed keywords

BARIUM ION; CHITIN; CHITINASE; COBALT; COPPER ION; CYSTEINE; FERRIC ION; MAGNESIUM ION; METAL ION; POTASSIUM ION; RECOMBINANT ENZYME; ZINC ION;

EID: 67651227156     PISSN: 00062928     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10528-009-9251-5     Document Type: Article
Times cited : (17)

References (33)
  • 1
    • 0002485638 scopus 로고    scopus 로고
    • Protein motifs in filarial chitinases
    • M Blaxter 1996 Protein motifs in filarial chitinases Parasitol Today 12 42
    • (1996) Parasitol Today , vol.12 , pp. 42
    • Blaxter, M.1
  • 2
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • JL Cereghino JM Cregg 2000 Heterologous protein expression in the methylotrophic yeast Pichia pastoris FEMS Microbiol Rev 24 45 66
    • (2000) FEMS Microbiol Rev , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 3
    • 0031866632 scopus 로고    scopus 로고
    • The molecular biology of chitin digestion
    • R Cohen-Kupiec I Chet 1998 The molecular biology of chitin digestion Curr Opin Biotechnol 9 270 277
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 270-277
    • Cohen-Kupiec, R.1    Chet, I.2
  • 4
    • 33749524596 scopus 로고    scopus 로고
    • Purification and characterization of an exochitinase from Bacillus thuringiensis subsp. aizawai and its action against phytopathogenic fungi
    • LM de la Vega JE Barboza-Corona MG Aguilar-Uscanga M Ramírez-Lepe 2006 Purification and characterization of an exochitinase from Bacillus thuringiensis subsp. aizawai and its action against phytopathogenic fungi Can J Microbiol 52 651 657
    • (2006) Can J Microbiol , vol.52 , pp. 651-657
    • De La Vega, L.M.1    Barboza-Corona, J.E.2    Aguilar-Uscanga, M.G.3    Ramírez-Lepe, M.4
  • 5
    • 0027263138 scopus 로고
    • Production and properties of an alkaline protease by Aureobasidium pullulans
    • JA Donaghy AM Mckay 1993 Production and properties of an alkaline protease by Aureobasidium pullulans J Appl Bacteriol 74 662 666
    • (1993) J Appl Bacteriol , vol.74 , pp. 662-666
    • Donaghy, J.A.1    McKay, A.M.2
  • 6
    • 34848887991 scopus 로고    scopus 로고
    • Expression of a Beauveria bassiana chitinase (Bbchit1) in Escherichia coli and Pichia pastoris
    • YH Fan YJ Zhang XY Yang XQ Pei SJ Guo Y Pei 2007 Expression of a Beauveria bassiana chitinase (Bbchit1) in Escherichia coli and Pichia pastoris Protein Expr Purif 56 93 99
    • (2007) Protein Expr Purif , vol.56 , pp. 93-99
    • Fan, Y.H.1    Zhang, Y.J.2    Yang, X.Y.3    Pei, X.Q.4    Guo, S.J.5    Pei, Y.6
  • 7
    • 4744343733 scopus 로고    scopus 로고
    • Cloning, expression and functional characterization of chitinase from larvae of tomato moth (Lacanobia oleracea): A demonstration of the insecticidal activity of insect chitinase
    • E Fitches H Wilkinson H Bell DP Bown JA Gatehouse JP Edwards 2004 Cloning, expression and functional characterization of chitinase from larvae of tomato moth (Lacanobia oleracea): a demonstration of the insecticidal activity of insect chitinase Insect Biochem Mol Biol 34 1037 1050
    • (2004) Insect Biochem Mol Biol , vol.34 , pp. 1037-1050
    • Fitches, E.1    Wilkinson, H.2    Bell, H.3    Bown, D.P.4    Gatehouse, J.A.5    Edwards, J.P.6
  • 8
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • B Henrissat 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
  • 9
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • T Imoto K Yagishita 1971 A simple activity measurement of lysozyme Agric Biol Chem 35 1154 1156
    • (1971) Agric Biol Chem , vol.35 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 10
    • 0036209121 scopus 로고    scopus 로고
    • Comparative degradation of oomycete, ascomycete, and basidiomycete cell walls by mycoparasitic and biocontrol fungi
    • GD Inglis LM Kawchuk 2002 Comparative degradation of oomycete, ascomycete, and basidiomycete cell walls by mycoparasitic and biocontrol fungi Can J Microbiol 48 60 70
    • (2002) Can J Microbiol , vol.48 , pp. 60-70
    • Inglis, G.D.1    Kawchuk, L.M.2
  • 11
    • 0035206324 scopus 로고    scopus 로고
    • Purification and properties of two chitinolytic enzymes of Serratia plymuthica HRO-C48
    • F Jens L Matteo S Felice S Roland B Gabriele B Hubert 2001 Purification and properties of two chitinolytic enzymes of Serratia plymuthica HRO-C48 Arch Microbiol 176 421 426
    • (2001) Arch Microbiol , vol.176 , pp. 421-426
    • Jens, F.1    Matteo, L.2    Felice, S.3    Roland, S.4    Gabriele, B.5    Hubert, B.6
  • 12
    • 0037393710 scopus 로고    scopus 로고
    • Molecular cloning, sequencing and expression of the gene encoding a novel chitinase A from a marine bacterium, Pseudomonas sp. PE2, and its domain structure
    • E Kitamura Y Kamei 2003 Molecular cloning, sequencing and expression of the gene encoding a novel chitinase A from a marine bacterium, Pseudomonas sp. PE2, and its domain structure Appl Microbiol Biotechnol 61 140 149
    • (2003) Appl Microbiol Biotechnol , vol.61 , pp. 140-149
    • Kitamura, E.1    Kamei, Y.2
  • 14
    • 33847246862 scopus 로고    scopus 로고
    • Pichia pastoris is a valuable host for the expression of genes encoding membrane proteins from the hyperthermophilic Archeon Pyrococcus abyssi
    • C Labarre H van Tilbeurgh K Blondeau 2007 Pichia pastoris is a valuable host for the expression of genes encoding membrane proteins from the hyperthermophilic Archeon Pyrococcus abyssi Extremophiles 11 403 413
    • (2007) Extremophiles , vol.11 , pp. 403-413
    • Labarre, C.1    Van Tilbeurgh, H.2    Blondeau, K.3
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • UK Laemmli 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
  • 18
    • 48349113600 scopus 로고    scopus 로고
    • Cloning and characterization of a novel chitinase gene (chi46) from Chaetomium globosum and identification of its biological activity
    • ZH Liu Q Yang S Hu JD Zhang J Ma 2008 Cloning and characterization of a novel chitinase gene (chi46) from Chaetomium globosum and identification of its biological activity Appl Microbiol Biotechnol 80 241 252
    • (2008) Appl Microbiol Biotechnol , vol.80 , pp. 241-252
    • Liu, Z.H.1    Yang, Q.2    Hu, S.3    Zhang, J.D.4    Ma, J.5
  • 19
    • 24044455383 scopus 로고    scopus 로고
    • Chitinase from Enterobacter sp. NRG4: Its purification, characterization and reaction pattern
    • [Online]
    • Neetu D, Rupinder T, Ram PT, Gurinder SH (2005) Chitinase from Enterobacter sp. NRG4: its purification, characterization and reaction pattern [Online]. Electron J Biotechnol 8(2). Available from http://www.ejbiotechnology. info/content/vol8/issue2/full/6/index.html. ISSN: 0717-3458
    • (2005) Electron J Biotechnol , vol.8 , Issue.2
    • Neetu, D.1    Rupinder, T.2    Ram, P.T.3    Gurinder, S.H.4
  • 22
    • 0001194009 scopus 로고
    • Plant and bacterial chitinases differ in antifungal activity
    • WK Roberts CP Selitrennikoff 1988 Plant and bacterial chitinases differ in antifungal activity J Gen Microbiol 134 169 176
    • (1988) J Gen Microbiol , vol.134 , pp. 169-176
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 23
    • 0033290345 scopus 로고    scopus 로고
    • The structure and action of chitinases
    • JD Robertus AF Monzingo 1999 The structure and action of chitinases EXS 87 125 135
    • (1999) EXS , vol.87 , pp. 125-135
    • Robertus, J.D.1    Monzingo, A.F.2
  • 24
    • 3242699848 scopus 로고    scopus 로고
    • In vitro biocontrol activity of Trichoderma harzianum on Alternaria alternata in the presence of growth regulators
    • [Online]
    • Roco A, Prez LM (2001) In vitro biocontrol activity of Trichoderma harzianum on Alternaria alternata in the presence of growth regulators [Online]. Electron J Biotechnol 4(2). Available from http://www.ejbiotechnology.info/ content/vol2/issue3/full/3/index.html. ISSN: 0717-3458
    • (2001) Electron J Biotechnol , vol.4 , Issue.2
    • Roco, A.1    Prez, L.M.2
  • 25
    • 33847336822 scopus 로고    scopus 로고
    • Proteolytic activity and antibiotic production by Trichoderma harzianum in relation to pathogenicity to insects
    • J Shakeri HA Foster 2007 Proteolytic activity and antibiotic production by Trichoderma harzianum in relation to pathogenicity to insects Enzyme Microb Technol 40 961 966
    • (2007) Enzyme Microb Technol , vol.40 , pp. 961-966
    • Shakeri, J.1    Foster, H.A.2
  • 26
    • 0035929579 scopus 로고    scopus 로고
    • Different cleavage specificities of the dual catalytic domains in chitinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • T Tanaka T Fukui T Imanaka 2001 Different cleavage specificities of the dual catalytic domains in chitinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 J Biol Chem 276 35629 35635
    • (2001) J Biol Chem , vol.276 , pp. 35629-35635
    • Tanaka, T.1    Fukui, T.2    Imanaka, T.3
  • 28
    • 0024669485 scopus 로고
    • Detection of chitinase activity after polyacrylamide gel electrophoresis
    • J Trudel A Asselin 1989 Detection of chitinase activity after polyacrylamide gel electrophoresis Anal Biochem 178 362 366
    • (1989) Anal Biochem , vol.178 , pp. 362-366
    • Trudel, J.1    Asselin, A.2
  • 30
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • G von Heijne 1986 A new method for predicting signal sequence cleavage sites Nucleic Acids Res 14 4683 4690
    • (1986) Nucleic Acids Res , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 31
    • 0037339655 scopus 로고    scopus 로고
    • An extracellular Bacillus sp. chitinase for the production of chitotriose as a major chitinolytic product
    • CJ Woo HD Park 2003 An extracellular Bacillus sp. chitinase for the production of chitotriose as a major chitinolytic product Biotechnol Lett 25 409 412
    • (2003) Biotechnol Lett , vol.25 , pp. 409-412
    • Woo, C.J.1    Park, H.D.2
  • 32
    • 67651209386 scopus 로고    scopus 로고
    • Evaluation of Chaetomium for biological control of Fusarium wilt of tomato in P. R. China
    • Heilongjiang Science and Technology Press Harbin
    • Yang Q (2003) Evaluation of Chaetomium for biological control of Fusarium wilt of tomato in P. R. China. In: Yang Q (ed) Biological control and biotechnology. Heilongjiang Science and Technology Press, Harbin, pp 25-36
    • (2003) Biological Control and Biotechnology , pp. 25-36
    • Yang, Q.1    Yang, Q.2
  • 33
    • 0030561325 scopus 로고    scopus 로고
    • A method for the large scale isolation of high transformation efficiency fungal genomic DNA
    • D Zhang Y Yang LA Castlebury CE Cerniglia 1996 A method for the large scale isolation of high transformation efficiency fungal genomic DNA FEMS Microbiol Lett 145 216 265
    • (1996) FEMS Microbiol Lett , vol.145 , pp. 216-265
    • Zhang, D.1    Yang, Y.2    Castlebury, L.A.3    Cerniglia, C.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.