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Volumn 161, Issue 6, 2006, Pages 345-360

Review of fungal chitinases

Author keywords

Expression regulation; Fungal chitinase; Gene cloning; Mycoparasitism; Purification and characterization

Indexed keywords

CHITINASE;

EID: 33745039979     PISSN: 0301486X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11046-006-0024-y     Document Type: Review
Times cited : (279)

References (172)
  • 1
    • 4344713045 scopus 로고    scopus 로고
    • Fungal cell wall chitinases and glucanases
    • DJ Adams 2004 Fungal cell wall chitinases and glucanases Microbiology 150 2029 2035
    • (2004) Microbiology , vol.150 , pp. 2029-2035
    • Adams, D.J.1
  • 2
    • 0029770421 scopus 로고    scopus 로고
    • Molecular mechanisms of lytic enzymes involved in the biocontrol activity of Trichoderma harzianum
    • S Haran H Schickler I Chet 1996 Molecular mechanisms of lytic enzymes involved in the biocontrol activity of Trichoderma harzianum Microbiology 142 2321 2331
    • (1996) Microbiology , vol.142 , pp. 2321-2331
    • Haran, S.1    Schickler, H.2    Chet, I.3
  • 5
    • 0030981929 scopus 로고    scopus 로고
    • Chitin degradation proteins produced by the marine bacterium Vibrio harveyi growing on different forms of chitin
    • AL Svitil SMN Chadhain JA Moore DC Kirchman 1997 Chitin degradation proteins produced by the marine bacterium Vibrio harveyi growing on different forms of chitin Appl Environ Microbiol 63 408 413
    • (1997) Appl Environ Microbiol , vol.63 , pp. 408-413
    • Svitil, A.L.1    Chadhain, S.M.N.2    Moore, J.A.3    Kirchman, D.C.4
  • 6
    • 0030900026 scopus 로고    scopus 로고
    • Purification and characterization of two bifunctional chitinases/lysozymes extracellularly produced by Pseudomonas aeruginosa K-187 in a shrimp and crab shell power medium
    • SL Wang WT Chang 1997 Purification and characterization of two bifunctional chitinases/lysozymes extracellularly produced by Pseudomonas aeruginosa K-187 in a shrimp and crab shell power medium Appl Environ Microbiol 63 380 383
    • (1997) Appl Environ Microbiol , vol.63 , pp. 380-383
    • Wang, S.L.1    Chang, W.T.2
  • 7
    • 0346399742 scopus 로고    scopus 로고
    • Chitin metabolism in insects: Structure, function and regulation of chitin synthases and chitinases
    • H Merzendorfer L Zimoch 2003 Chitin metabolism in insects: structure, function and regulation of chitin synthases and chitinases J Exp Biol 206 4393 4412
    • (2003) J Exp Biol , vol.206 , pp. 4393-4412
    • Merzendorfer, H.1    Zimoch, L.2
  • 15
    • 0027297246 scopus 로고
    • Chitinases of fungi and plants: Their involvement in morphogenesis and host-parasite interaction
    • AS Sahai MS Manocha 1993 Chitinases of fungi and plants: their involvement in morphogenesis and host-parasite interaction FEMS Microbiol Rev 11 317 338
    • (1993) FEMS Microbiol Rev , vol.11 , pp. 317-338
    • Sahai, A.S.1    Manocha, M.S.2
  • 16
    • 0028301746 scopus 로고
    • Molecular cloning and expression of the Candida albicans beta-N-acetylglucosaminidase (HEX1) gene
    • RD Cannon K Niimi HF Jenkinson MG Shepherd 1994 Molecular cloning and expression of the Candida albicans beta-N-acetylglucosaminidase (HEX1) gene J Bacteriol 176 2640 2647
    • (1994) J Bacteriol , vol.176 , pp. 2640-2647
    • Cannon, R.D.1    Niimi, K.2    Jenkinson, H.F.3    Shepherd, M.G.4
  • 17
    • 0001194009 scopus 로고
    • Plant and bacterial chitinases differ in antifungal activity
    • WK Robert 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
    • Robert, W.K.1    Selitrennikoff, C.P.2
  • 18
    • 0027401151 scopus 로고
    • Detection and quantification of N-acetyl-β-d-glucosaminidase, chitobiosidase, and endochitinase in solutions and on gels
    • A Tronsmo G Harman 1993 Detection and quantification of N-acetyl-β-d-glucosaminidase, chitobiosidase, and endochitinase in solutions and on gels Anal Biochem 208 74 79
    • (1993) Anal Biochem , vol.208 , pp. 74-79
    • Tronsmo, A.1    Harman, G.2
  • 19
    • 77049251255 scopus 로고
    • A modified colorimetri method for the estimation of N-acetyllamino sugars
    • JL Reissig JL Strominger LF Leloir 1955 A modified colorimetri method for the estimation of N-acetyllamino sugars J Biol Chem 217 959 967
    • (1955) J Biol Chem , vol.217 , pp. 959-967
    • Reissig, J.L.1    Strominger, J.L.2    Leloir, L.F.3
  • 20
    • 0025075165 scopus 로고
    • Enhanced removal of detergent and recovery of enzymatic activity following sodium dodecyl sulfate-polyacrylamide gel electrophoresis: Use of casein in gel wash buffer
    • BR [tmp] McGrew DM Green 1990 Enhanced removal of detergent and recovery of enzymatic activity following sodium dodecyl sulfate-polyacrylamide gel electrophoresis: use of casein in gel wash buffer Anal. Biochem 189 68 74
    • (1990) Anal. Biochem , vol.189 , pp. 68-74
    • McGrew, B.R.1    Green, D.M.2
  • 21
    • 0029124479 scopus 로고
    • New components of the chitinolytic system of Trichoderma harzianum
    • S Haran H Schickler A Oppenheim I Chet 1995 New components of the chitinolytic system of Trichoderma harzianum Mycol Res 99 441 446
    • (1995) Mycol Res , vol.99 , pp. 441-446
    • Haran, S.1    Schickler, H.2    Oppenheim, A.3    Chet, I.4
  • 22
    • 0000859095 scopus 로고
    • A technique for chitinase, β-1,3-glucanase, and protein patters after a single separation using polyacrylamide gels and isoelectrofocusing
    • SQ Pan XS Ye J Kuc 1991 A technique for chitinase, β-1,3-glucanase, and protein patters after a single separation using polyacrylamide gels and isoelectrofocusing Phytopathology 81 970 974
    • (1991) Phytopathology , vol.81 , pp. 970-974
    • Pan, S.Q.1    Ye, X.S.2    Kuc, J.3
  • 23
    • 0024669485 scopus 로고
    • Detection of chitinase activity after polyacrylamide gel electrophoresis
    • J Trudel A Asslin 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    Asslin, A.2
  • 24
    • 0000369638 scopus 로고
    • Electrophoretic forms of chitinase activity in Xanthi-nc tobacco, healthy and infected with tobacco mosaic virus
    • J Trudel P Audy A Asselin 1989 Electrophoretic forms of chitinase activity in Xanthi-nc tobacco, healthy and infected with tobacco mosaic virus Mol Plant Microbe Interact 2 315 324
    • (1989) Mol Plant Microbe Interact , vol.2 , pp. 315-324
    • Trudel, J.1    Audy, P.2    Asselin, A.3
  • 25
    • 0036741161 scopus 로고    scopus 로고
    • A gel diffusion assay for visualization and quantification of chitinase activity
    • X Zou H Nonogaki GE Welbaum 2002 A gel diffusion assay for visualization and quantification of chitinase activity Mol Biotechnol 22 19 23
    • (2002) Mol Biotechnol , vol.22 , pp. 19-23
    • Zou, X.1    Nonogaki, H.2    Welbaum, G.E.3
  • 26
    • 0026315591 scopus 로고
    • Purification and characterization of an extracellular chitobiase from Trichoderma harzianum
    • CJ Ulhoa JF Peberdy 1991 Purification and characterization of an extracellular chitobiase from Trichoderma harzianum Curr Microbiol 23 285 289
    • (1991) Curr Microbiol , vol.23 , pp. 285-289
    • Ulhoa, C.J.1    Peberdy, J.F.2
  • 27
    • 0026832966 scopus 로고
    • Purification and some properties of the extracellular chitinase produced by Trichoderma harzianum
    • CJ Ulhoa JF Peberdy 1992 Purification and some properties of the extracellular chitinase produced by Trichoderma harzianum Enzyme Microb Technol 14 236 241
    • (1992) Enzyme Microb Technol , vol.14 , pp. 236-241
    • Ulhoa, C.J.1    Peberdy, J.F.2
  • 29
    • 0028055658 scopus 로고
    • Purification, characterization, and synergistic activity of a glucan 1,3-β-glucosidase and an N-acetylglucosaminidase from Trichoderma harzianum
    • M Lorito CK Hayes A Di Pietro SL Woo GE Harman 1994 Purification, characterization, and synergistic activity of a glucan 1,3-β-glucosidase and an N-acetylglucosaminidase from Trichoderma harzianum Phytopathology 84 398 405
    • (1994) Phytopathology , vol.84 , pp. 398-405
    • Lorito, M.1    Hayes, C.K.2    Di Pietro, A.3    Woo, S.L.4    Harman, G.E.5
  • 30
    • 0032478045 scopus 로고    scopus 로고
    • The purification and characterization of a Trichoderma harzianum exochitinase
    • EE Deane JM Whipps JM Lynch JF Peberdy 1998 The purification and characterization of a Trichoderma harzianum exochitinase Biochim Biophys Acta 1383 101 110
    • (1998) Biochim Biophys Acta , vol.1383 , pp. 101-110
    • Deane, E.E.1    Whipps, J.M.2    Lynch, J.M.3    Peberdy, J.F.4
  • 31
    • 1642409772 scopus 로고    scopus 로고
    • Purification and characterization of an N-acetylglucosaminidase produced by a Trichoderma harzianum strain which controls Crinipellis perniciosa
    • J De Lisboa Marco MC Valadares-Inglis CR Felix 2004 Purification and characterization of an N-acetylglucosaminidase produced by a Trichoderma harzianum strain which controls Crinipellis perniciosa Appl Microbiol Biotechnol 64 70 75
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 70-75
    • De Lisboa Marco, J.1    Valadares-Inglis, M.C.2    Felix, C.R.3
  • 32
    • 0010612922 scopus 로고
    • Purification and characterization of a chitinase from the hyperparasitic fungus Aphanocladium album
    • C Kunz O Sellam Y Bertheau 1992a Purification and characterization of a chitinase from the hyperparasitic fungus Aphanocladium album Physiol Mol Plant Pathol 40 117 131
    • (1992) Physiol Mol Plant Pathol , vol.40 , pp. 117-131
    • Kunz, C.1    Sellam, O.2    Bertheau, Y.3
  • 33
    • 0000439771 scopus 로고
    • Endochitinase from Gliocladium virens: Isolation, characterization, and synergistic antifungal activity in combination with gliotoxin
    • A Di Pietro M Lorito CK Hayes RM Broadway GE Harman 1993 Endochitinase from Gliocladium virens: isolation, characterization, and synergistic antifungal activity in combination with gliotoxin Phytopathology 83 308 313
    • (1993) Phytopathology , vol.83 , pp. 308-313
    • Di Pietro, A.1    Lorito, M.2    Hayes, C.K.3    Broadway, R.M.4    Harman, G.E.5
  • 34
    • 0031765245 scopus 로고    scopus 로고
    • Purification, characterization, and antifungal activity of chitinase from Fusarium chlamydosporum, a mycoparasite to groundnut rust, Puccinia arachidis
    • N Mathivanan V Kabilan K Murugesan 1998 Purification, characterization, and antifungal activity of chitinase from Fusarium chlamydosporum, a mycoparasite to groundnut rust, Puccinia arachidis Can J Microbiol 44 646 651
    • (1998) Can J Microbiol , vol.44 , pp. 646-651
    • Mathivanan, N.1    Kabilan, V.2    Murugesan, K.3
  • 35
    • 1942472042 scopus 로고    scopus 로고
    • Purification and characterization of a chitinase from the mycoparasitic fungus Trichothecium roseum
    • DC Li SH Zhang KQ Liu J Lu 2004 Purification and characterization of a chitinase from the mycoparasitic fungus Trichothecium roseum J Gen Appl Microbiol 50 35 39
    • (2004) J Gen Appl Microbiol , vol.50 , pp. 35-39
    • Li, D.C.1    Zhang, S.H.2    Liu, K.Q.3    Lu, J.4
  • 36
    • 0036000364 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular exochitinase, β-N-acetylhexosaminidase, from fungal mycoparasite Stachybotrys elegans
    • G Taylor S Jabaji-Hare PM Charest W Khan 2002 Purification and characterization of an extracellular exochitinase, β-N- acetylhexosaminidase, from fungal mycoparasite Stachybotrys elegans Can J Microbiol 48 311 319
    • (2002) Can J Microbiol , vol.48 , pp. 311-319
    • Taylor, G.1    Jabaji-Hare, S.2    Charest, P.M.3    Khan, W.4
  • 37
    • 18344387205 scopus 로고    scopus 로고
    • Purification and partial characterization of two chitinase from the mycoparasitic fungus Talaromyces flavus
    • DC Li S Chen J Lu 2005 Purification and partial characterization of two chitinase from the mycoparasitic fungus Talaromyces flavus Mycopathologia 159 223 229
    • (2005) Mycopathologia , vol.159 , pp. 223-229
    • Li, D.C.1    Chen, S.2    Lu, J.3
  • 38
    • 0027523283 scopus 로고
    • Partial purification and characterization of two extracellular N-acetyl-d-glucosaminidases produced by the entomopathogenic fungus Beauveria bassiana
    • MJ Bidochka KI Tong GG Khachatourians 1993 Partial purification and characterization of two extracellular N-acetyl-d-glucosaminidases produced by the entomopathogenic fungus Beauveria bassiana Can J Microbiol 39 41 45
    • (1993) Can J Microbiol , vol.39 , pp. 41-45
    • Bidochka, M.J.1    Tong, K.I.2    Khachatourians, G.G.3
  • 39
    • 12244276560 scopus 로고    scopus 로고
    • Induction and purification of two extracellular chitinases from Beauveria bassiana
    • (in Chinese)
    • RW Peng KM Guan XL Huang 1996 Induction and purification of two extracellular chitinases from Beauveria bassiana Acta Microbiol Sin 36 103 108 (in Chinese)
    • (1996) Acta Microbiol Sin , vol.36 , pp. 103-108
    • Peng, R.W.1    Guan, K.M.2    Huang, X.L.3
  • 41
    • 0030917623 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular chitinase from the entomopathogen Metarhizium anisopliae
    • DS Pinto CC Barreto A Schrank CJ Ulhoa M Henning Vainstein 1997 Purification and characterization of an extracellular chitinase from the entomopathogen Metarhizium anisopliae Can J Microbiol 43 322 327
    • (1997) Can J Microbiol , vol.43 , pp. 322-327
    • Pinto, D.S.1    Barreto, C.C.2    Schrank, A.3    Ulhoa, C.J.4    Henning Vainstein, M.5
  • 42
    • 13344279428 scopus 로고    scopus 로고
    • Characterization and ultrastructural localization of chitinase from Metarhizium anisopliae, M. flavoviride and Beauveria bassiana during fungal invasion of host (Manduca sexta) cuticle
    • RJ St. Leger L Joshi MJ Bidochka NW Rizzo DW Roberts 1996 Characterization and ultrastructural localization of chitinase from Metarhizium anisopliae, M. flavoviride and Beauveria bassiana during fungal invasion of host (Manduca sexta) cuticle Appl Environ Microbiol 62 907 912
    • (1996) Appl Environ Microbiol , vol.62 , pp. 907-912
    • St. Leger, R.J.1    Joshi, L.2    Bidochka, M.J.3    Rizzo, N.W.4    Roberts, D.W.5
  • 43
    • 0033129067 scopus 로고    scopus 로고
    • Purification and characterization of a novel chitinase from the entomopathogenic fungus Metarhizium anisopliae
    • SC Kang S Park DG Lee 1999 Purification and characterization of a novel chitinase from the entomopathogenic fungus Metarhizium anisopliae J Invertebr Pathol 73 276 281
    • (1999) J Invertebr Pathol , vol.73 , pp. 276-281
    • Kang, S.C.1    Park, S.2    Lee, D.G.3
  • 44
    • 0036352560 scopus 로고    scopus 로고
    • Purification and characterization of chitinases from the nematophagous fungi Verticillium chamydosporium and V. suchlasporium
    • VE Tikhonov LV Lopez-Llorca J Salinas HB Jansson 2002 Purification and characterization of chitinases from the nematophagous fungi Verticillium chamydosporium and V. suchlasporium Fungal Genet. Biol 35 67 78
    • (2002) Fungal Genet. Biol , vol.35 , pp. 67-78
    • Tikhonov, V.E.1    Lopez-Llorca, L.V.2    Salinas, J.3    Jansson, H.B.4
  • 45
    • 33745056601 scopus 로고    scopus 로고
    • Purification and properties of a thermostable chitinase from thermophilic fungus Thermomyces lanuginosus
    • (in Chinese)
    • RF Guo DC Li R Wang 2005 Purification and properties of a thermostable chitinase from thermophilic fungus Thermomyces lanuginosus Acta Microbiol Sin 45 270 274 (in Chinese)
    • (2005) Acta Microbiol Sin , vol.45 , pp. 270-274
    • Guo, R.F.1    Li, D.C.2    Wang, R.3
  • 46
    • 0028304284 scopus 로고
    • Purification and characterization of chitinase from Candida albicans
    • KJ Mellor RO Nicholas DJ Adams 1994 Purification and characterization of chitinase from Candida albicans FEMS Microbiol Lett 119 117 119
    • (1994) FEMS Microbiol Lett , vol.119 , pp. 117-119
    • Mellor, K.J.1    Nicholas, R.O.2    Adams, D.J.3
  • 47
    • 0026002418 scopus 로고
    • Chitinase is required for cell separation during growth of Saccharomyces cerevisiae
    • MJ Kuranda PW Robbins 1991 Chitinase is required for cell separation during growth of Saccharomyces cerevisiae J Biol Chem 266 19758 19767
    • (1991) J Biol Chem , vol.266 , pp. 19758-19767
    • Kuranda, M.J.1    Robbins, P.W.2
  • 48
    • 2542420910 scopus 로고    scopus 로고
    • Regulation of two homodimer hexosaminidases in the mycoparasitic fungus Trichoderma asperellum by glucosamine
    • Ramot O, Viterbo A, Friesem D, Oppenheim A, Chet I. Regulation of two homodimer hexosaminidases in the mycoparasitic fungus Trichoderma asperellum by glucosamine. Curr Genet 2004; : 45-205-213.
    • (2004) Curr Genet , vol.45 , pp. 205-213
    • Ramot, O.1    Viterbo, A.2    Friesem, D.3    Oppenheim, A.4    Chet, I.5
  • 49
    • 33745041857 scopus 로고    scopus 로고
    • Purification, characterization, and gene cloning of 46 kDa chitinase (Chi46) from Trichoderma reesei PC-3-7 and its expression in Escherichia coli
    • (Online)
    • Ike M, Nagamatsu K, Shioya A, Nogawa M, Ogasawara W, Okada H, Morikawa Y. Purification, characterization, and gene cloning of 46 kDa chitinase (Chi46) from Trichoderma reesei PC-3-7 and its expression in Escherichia coli. Appl Micribiol Biotechnol 2005; 1432-0614 (Online)
    • (2005) Appl Micribiol Biotechnol , pp. 1432-0614
    • Ike, M.1    Nagamatsu, K.2    Shioya, A.3    Nogawa, M.4    Ogasawara, W.5    Okada, H.6    Morikawa, Y.7
  • 50
    • 0037987856 scopus 로고    scopus 로고
    • Purification and characterization of an endochitinase produced by Colletotrichum gloeosporioides
    • RF Souza RC Gomes RR Coelho CS Alviano RM Soares 2003 Purification and characterization of an endochitinase produced by Colletotrichum gloeosporioides FEMS Microbiol Lett 222 45 50
    • (2003) FEMS Microbiol Lett , vol.222 , pp. 45-50
    • Souza, R.F.1    Gomes, R.C.2    Coelho, R.R.3    Alviano, C.S.4    Soares, R.M.5
  • 51
    • 0026539865 scopus 로고
    • Purification of two chitinases from Rhizopus oligosporus and isolation and sequencing of the encoding genes
    • K Yanai N Takaya N Kojima H Horiuchi A Ohta M Takagi 1992 Purification of two chitinases from Rhizopus oligosporus and isolation and sequencing of the encoding genes J Bacteriol 174 7398 7406
    • (1992) J Bacteriol , vol.174 , pp. 7398-7406
    • Yanai, K.1    Takaya, N.2    Kojima, N.3    Horiuchi, H.4    Ohta, A.5    Takagi, M.6
  • 52
    • 0031669733 scopus 로고    scopus 로고
    • Intracellular chitinase gene from Rhizopus oligosporus: Molecular cloning and characterization
    • N Takaya D Yamazaki H Horiuchi A Ohta M Takagi 1998b Intracellular chitinase gene from Rhizopus oligosporus: molecular cloning and characterization Microbiology 144 2647 2654
    • (1998) Microbiology , vol.144 , pp. 2647-2654
    • Takaya, N.1    Yamazaki, D.2    Horiuchi, H.3    Ohta, A.4    Takagi, M.5
  • 53
    • 0022494319 scopus 로고
    • Purification and properties of β-N-acetylhexosaminidase from Mucor fragilis grown in bovine blood
    • K Yamamoto Y Tsuji S Matsushita H Kumagai T Tochikura 1986 Purification and properties of β-N-acetylhexosaminidase from Mucor fragilis grown in bovine blood Appl Environ Microbiol 51 1019 1023
    • (1986) Appl Environ Microbiol , vol.51 , pp. 1019-1023
    • Yamamoto, K.1    Tsuji, Y.2    Matsushita, S.3    Kumagai, H.4    Tochikura, T.5
  • 54
    • 0034834977 scopus 로고    scopus 로고
    • A novel chitinase having a unique mode of action from Aspergillus fumigatus YJ-407
    • G Xia C Jin J Zhou S Yang S Zhang C Jin 2001 A novel chitinase having a unique mode of action from Aspergillus fumigatus YJ-407 Eur J Biochem 268 4079 4085
    • (2001) Eur J Biochem , vol.268 , pp. 4079-4085
    • Xia, G.1    Jin, C.2    Zhou, J.3    Yang, S.4    Zhang, S.5    Jin, C.6
  • 55
    • 0031781440 scopus 로고    scopus 로고
    • Inducible chitinolytic system of Aspergillus fumigatus
    • GM Escott VM Hearn DJ Adams 1998 Inducible chitinolytic system of Aspergillus fumigatus Microbiology 144 1575 1581
    • (1998) Microbiology , vol.144 , pp. 1575-1581
    • Escott, G.M.1    Hearn, V.M.2    Adams, D.J.3
  • 56
    • 0024757890 scopus 로고
    • β-N-acetylglucosaminidase from Aspergillus nidulans which degrades chitin oligomers during autolysis
    • F Reyes J Calatayud C Vazquez MJ Martinez 1989b β-N- acetylglucosaminidase from Aspergillus nidulans which degrades chitin oligomers during autolysis FEMS Microbiol Lett 65 83 88
    • (1989) FEMS Microbiol Lett , vol.65 , pp. 83-88
    • Reyes, F.1    Calatayud, J.2    Vazquez, C.3    Martinez, M.J.4
  • 57
    • 0024696560 scopus 로고
    • Endochitinase from Aspergillus nidulans implicated in the autolysis of its cell wall
    • F Reyes J Calatayud MJ Martinez 1989a Endochitinase from Aspergillus nidulans implicated in the autolysis of its cell wall FEMS Microbiol Lett 51 119 124
    • (1989) FEMS Microbiol Lett , vol.51 , pp. 119-124
    • Reyes, F.1    Calatayud, J.2    Martinez, M.J.3
  • 58
    • 0035720520 scopus 로고    scopus 로고
    • The chitinolytic activity of Penicillium janthinellum P9: Purification, partial characterization and potential applications
    • R Di Giambattista F Federici M Petruccioli M Fenice 2001 The chitinolytic activity of Penicillium janthinellum P9: purification, partial characterization and potential applications J Appl Microbiol 91 498 505
    • (2001) J Appl Microbiol , vol.91 , pp. 498-505
    • Di Giambattista, R.1    Federici, F.2    Petruccioli, M.3    Fenice, M.4
  • 61
    • 0030974212 scopus 로고    scopus 로고
    • Purification and characteristics of an autolytic chitinase of Piromyces communis OTS1 from culture medium
    • M Sakurada DP Morgavi K Komatani T Tomita R Onodera 1997 Purification and characteristics of an autolytic chitinase of Piromyces communis OTS1 from culture medium Curr Microbiol 35 48 51
    • (1997) Curr Microbiol , vol.35 , pp. 48-51
    • Sakurada, M.1    Morgavi, D.P.2    Komatani, K.3    Tomita, T.4    Onodera, R.5
  • 62
    • 0027962712 scopus 로고
    • Partial purification and properties of extracellular chitinase produced by Acremonium obclavatum, an antagonist to groundnut rust, Puccinia arachidis
    • KR Gunaratna R Balasubramanian 1994 Partial purification and properties of extracellular chitinase produced by Acremonium obclavatum, an antagonist to groundnut rust, Puccinia arachidis World J. Microbiol. Biotechnol 10 342 345
    • (1994) World J. Microbiol. Biotechnol , vol.10 , pp. 342-345
    • Gunaratna, K.R.1    Balasubramanian, R.2
  • 64
    • 0000424066 scopus 로고
    • Characterization of chitinase and chitobiase produced by the entomopathogenic fungus Metarhizium anisopliae
    • RJ St. Leger RM Cooper AK Charnley 1991 Characterization of chitinase and chitobiase produced by the entomopathogenic fungus Metarhizium anisopliae J Invertebr Pathol 58 415 426
    • (1991) J Invertebr Pathol , vol.58 , pp. 415-426
    • St. Leger, R.J.1    Cooper, R.M.2    Charnley, A.K.3
  • 65
    • 0000113161 scopus 로고
    • Chitinolytic enzymes produced by Trichoderma harzianum: Antifungal activity of purified endochitinase and chitobiosidase
    • M Lorito GE Harman CK Hayes RM Broadway A Tronsmo SL Woo A Di Pietro 1993 Chitinolytic enzymes produced by Trichoderma harzianum: antifungal activity of purified endochitinase and chitobiosidase Phytopathology 83 302 307
    • (1993) Phytopathology , vol.83 , pp. 302-307
    • Lorito, M.1    Harman, G.E.2    Hayes, C.K.3    Broadway, R.M.4    Tronsmo, A.5    Woo, S.L.6    Di Pietro, A.7
  • 66
    • 0029328434 scopus 로고
    • Enhanced quantitative resistance against fungal disease by combinatorial expression of different antifungal proteins in transgenic tobacco
    • G Jach B Gomhardt J Mundy J Logemann E Pinsdorf R Leah J Schell C Mass 1995 Enhanced quantitative resistance against fungal disease by combinatorial expression of different antifungal proteins in transgenic tobacco Plant J 8 97 109
    • (1995) Plant J , vol.8 , pp. 97-109
    • Jach, G.1    Gomhardt, B.2    Mundy, J.3    Logemann, J.4    Pinsdorf, E.5    Leah, R.6    Schell, J.7    Mass, C.8
  • 67
    • 0036562588 scopus 로고    scopus 로고
    • Chitinases, A, B and C1 of Serratia marcescens 2170 produced by recombinant E. coli: Enzymatic properties and synergist on chitin degradation
    • K Suzuki N Sugawara M Suzuki T Uchiyama F Katouno N Nikaidou T Watanabe 2002 Chitinases, A, B and C1 of Serratia marcescens 2170 produced by recombinant E. coli: enzymatic properties and synergist on chitin degradation Biosci Biotechnol Biochem 66 1075 1083
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 1075-1083
    • Suzuki, K.1    Sugawara, N.2    Suzuki, M.3    Uchiyama, T.4    Katouno, F.5    Nikaidou, N.6    Watanabe, T.7
  • 69
    • 0026599547 scopus 로고
    • Evaluation of the antifungal activity of the purified chitinase 1 from the filamentus fungus Aphanocladium album
    • C Kunz A Ludwig Y Bertheau T Boller 1992 Evaluation of the antifungal activity of the purified chitinase 1 from the filamentus fungus Aphanocladium album FEMS Microbiol Lett 90 105 110
    • (1992) FEMS Microbiol Lett , vol.90 , pp. 105-110
    • Kunz, C.1    Ludwig, A.2    Bertheau, Y.3    Boller, T.4
  • 70
    • 0023256310 scopus 로고
    • Cloning and heterologous expression of glycosidase genes from Saccharomyces cerevisiae
    • MJ Kuranda PW Robbins 1987 Cloning and heterologous expression of glycosidase genes from Saccharomyces cerevisiae Proc Natl Acad Sci USA 84 2585 2589
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 2585-2589
    • Kuranda, M.J.1    Robbins, P.W.2
  • 71
    • 0028913997 scopus 로고
    • Molecular cloning and characterization of chitinase genes from Candida albicans
    • KJ [tmp] McCreath CA Specht PW Robbins 1995 Molecular cloning and characterization of chitinase genes from Candida albicans Proc Natl Acad Sci USA 92 2544 2548
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2544-2548
    • McCreath, K.J.1    Specht, C.A.2    Robbins, P.W.3
  • 72
    • 0029891542 scopus 로고    scopus 로고
    • Molecular cloning of a third chitinase gene (CHT1) from Candida albicans
    • KJ [tmp] McCreath CA Specht Y Liu PW Robbins 1996 Molecular cloning of a third chitinase gene (CHT1) from Candida albicans Yeast 12 501 504
    • (1996) Yeast , vol.12 , pp. 501-504
    • McCreath, K.J.1    Specht, C.A.2    Liu, Y.3    Robbins, P.W.4
  • 74
    • 0022763345 scopus 로고    scopus 로고
    • The killer toxin of Kluyveromyces lactis: Characterization of the toxin subunits and identification of the genes that encode them
    • MJR Stark A Boyd 1996 The killer toxin of Kluyveromyces lactis: characterization of the toxin subunits and identification of the genes that encode them EMBO J 3 1995 2002
    • (1996) EMBO J , vol.3 , pp. 1995-2002
    • Stark, M.J.R.1    Boyd, A.2
  • 75
    • 20444364443 scopus 로고    scopus 로고
    • Characterization of a nucleus-encoded chitinase from the yeast Kluyveromyces lactis
    • PA Colussi CA Specht CH Taron 2005 Characterization of a nucleus-encoded chitinase from the yeast Kluyveromyces lactis Appl Environ Microbiol 71 2862 2869
    • (2005) Appl Environ Microbiol , vol.71 , pp. 2862-2869
    • Colussi, P.A.1    Specht, C.A.2    Taron, C.H.3
  • 76
    • 0029558952 scopus 로고
    • Isolation and characterization of two chitinase-endoding genes (cts1, cts2) from the fungus Coccidioides immitis
    • EJ Pishko TN Kirkland GT Cole 1995 Isolation and characterization of two chitinase-endoding genes (cts1, cts2) from the fungus Coccidioides immitis Gene 167 173 177
    • (1995) Gene , vol.167 , pp. 173-177
    • Pishko, E.J.1    Kirkland, T.N.2    Cole, G.T.3
  • 78
    • 33645081716 scopus 로고    scopus 로고
    • Chitinase from Paracoccidioides brasiliensis: Molecular cloning, structural, phylogenitic, expression and activity analysis
    • SMRC Bonfim AHS Cruz RSA Jesuino CJ Ulhoa EEWI Molinari-Madlum CMA Soares M Pereira 2006 Chitinase from Paracoccidioides brasiliensis: molecular cloning, structural, phylogenitic, expression and activity analysis FEMS Immunol Med Microbiol 46 269 283
    • (2006) FEMS Immunol Med Microbiol , vol.46 , pp. 269-283
    • Smrc, B.1    Cruz, A.H.S.2    Jesuino, R.S.A.3    Ulhoa, C.J.4    Eewi, M.5    Soares, C.M.A.6    Pereira, M.7
  • 80
    • 0037626913 scopus 로고    scopus 로고
    • The nag1 N-acetylglucosaminidase of Trichoderma atroviride is essential for chitinase induction by chitin and of major relevance to biocontrol
    • K Brunner CK Peterbauer RL Mach M Lorito S Zeilinger CP Kubicek 2003a The nag1 N-acetylglucosaminidase of Trichoderma atroviride is essential for chitinase induction by chitin and of major relevance to biocontrol Curr Genet 43 289 295
    • (2003) Curr Genet , vol.43 , pp. 289-295
    • Brunner, K.1    Peterbauer, C.K.2    MacH, R.L.3    Lorito, M.4    Zeilinger, S.5    Kubicek, C.P.6
  • 81
    • 0029799714 scopus 로고    scopus 로고
    • Molecular cloning and expression of the nag1 gene (N-acetyl-β-D- glucosaminidase-encoding gene) from Trichoderma harzianum P1
    • CK Peterbauer M Lorito CK Hayes GE Harman CP Kubicek 1996 Molecular cloning and expression of the nag1 gene (N-acetyl-β-D-glucosaminidase- encoding gene) from Trichoderma harzianum P1 Curr Genet 30 325 331
    • (1996) Curr Genet , vol.30 , pp. 325-331
    • Peterbauer, C.K.1    Lorito, M.2    Hayes, C.K.3    Harman, G.E.4    Kubicek, C.P.5
  • 82
    • 0028880835 scopus 로고
    • Primary structure and expression pattern of the 33-kDa chitinase gene from the mycoparasitic fungus Trichoderma harzianum
    • MC Limon JM Lora I Garcia J De La Cruz A Llobell T Benitez JA Pintor-Toro 1995 Primary structure and expression pattern of the 33-kDa chitinase gene from the mycoparasitic fungus Trichoderma harzianum Curr Genet 28 478 483
    • (1995) Curr Genet , vol.28 , pp. 478-483
    • Limon, M.C.1    Lora, J.M.2    Garcia, I.3    De La Cruz, J.4    Llobell, A.5    Benitez, T.6    Pintor-Toro, J.A.7
  • 83
    • 0028135314 scopus 로고
    • Cloning and characterization of a chitinase (CHIT42) cDNA from the mycoparasitic fungus Trichoderma harzianum
    • I Garcia JM Lora J De La Cruz T Benitez A Llobell JA Pintor-Toro 1994 Cloning and characterization of a chitinase (CHIT42) cDNA from the mycoparasitic fungus Trichoderma harzianum Curr Genet 27 83 89
    • (1994) Curr Genet , vol.27 , pp. 83-89
    • Garcia, I.1    Lora, J.M.2    De La Cruz, J.3    Benitez, T.4    Llobell, A.5    Pintor-Toro, J.A.6
  • 84
    • 0035948245 scopus 로고    scopus 로고
    • Antifungal activity of a novel endochitinase gene (chit36) from Trichoderma harzianum Rifai TM
    • A Viterbo S Haran D Friesem O Ramot I Chet 2001 Antifungal activity of a novel endochitinase gene (chit36) from Trichoderma harzianum Rifai TM FEMS Microbiol Lett 200 169 174
    • (2001) FEMS Microbiol Lett , vol.200 , pp. 169-174
    • Viterbo, A.1    Haran, S.2    Friesem, D.3    Ramot, O.4    Chet, I.5
  • 85
    • 0036873374 scopus 로고    scopus 로고
    • Expression regulation of the endochitinase vhit36 from Trichoderma asperellum (T. harzianum T-203)
    • A Viterbo M Montero O Ramot D Friesem E Monte A Llodell I Chet 2002 Expression regulation of the endochitinase vhit36 from Trichoderma asperellum (T. harzianum T-203) Curr Genet 42 114 122
    • (2002) Curr Genet , vol.42 , pp. 114-122
    • Viterbo, A.1    Montero, M.2    Ramot, O.3    Friesem, D.4    Monte, E.5    Llodell, A.6    Chet, I.7
  • 87
    • 0029555549 scopus 로고
    • Molecular cloning and expression in S. cerevisiae of two exochitinases from Trichoderma harzianum
    • H Draborg S Kauppinen H Dalboge S Christgau 1995 Molecular cloning and expression in S. cerevisiae of two exochitinases from Trichoderma harzianum Biochem. Mol Biol Int 36 781 791
    • (1995) Biochem. Mol Biol Int , vol.36 , pp. 781-791
    • Draborg, H.1    Kauppinen, S.2    Dalboge, H.3    Christgau, S.4
  • 88
    • 28044450149 scopus 로고    scopus 로고
    • A complete survey of Trichoderma chitinases reveals three distinct subgroups of family 18 chitinases
    • V Seidl B Huemer B Seiboth CP Kubicek 2005 A complete survey of Trichoderma chitinases reveals three distinct subgroups of family 18 chitinases FEBS J 272 5923 5939
    • (2005) FEBS J , vol.272 , pp. 5923-5939
    • Seidl, V.1    Huemer, B.2    Seiboth, B.3    Kubicek, C.P.4
  • 89
    • 0034059255 scopus 로고    scopus 로고
    • Enzyme diffusion from Trichoderma atroviride (=T. harzianum P1) to Rhizoctonia solani is a prerequisite for triggering of Trichoderma ech42 gene expression before mycoparasitic contact
    • CM Kulling RL Mach M Lorito CP Kubicek 2000 Enzyme diffusion from Trichoderma atroviride (=T. harzianum P1) to Rhizoctonia solani is a prerequisite for triggering of Trichoderma ech42 gene expression before mycoparasitic contact Appl Environ Microbiol 66 2232 2234
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2232-2234
    • Kulling, C.M.1    MacH, R.L.2    Lorito, M.3    Kubicek, C.P.4
  • 91
    • 0033057503 scopus 로고    scopus 로고
    • The role of an extracellular chitinase from Trichoderma virens Gv29-8 in the biocontrol of Rhizoctonia solani
    • JM Baek CR Howell CM Kenerley 1999 The role of an extracellular chitinase from Trichoderma virens Gv29-8 in the biocontrol of Rhizoctonia solani Curr Genet 35 41 50
    • (1999) Curr Genet , vol.35 , pp. 41-50
    • Baek, J.M.1    Howell, C.R.2    Kenerley, C.M.3
  • 92
    • 0036227209 scopus 로고    scopus 로고
    • Cloning and characterization of multiple glycosyl hydrolase genes from Trichoderma rirens
    • DJ Kim JM Baek P Uribe CM Kenerley Cook 2002 Cloning and characterization of multiple glycosyl hydrolase genes from Trichoderma rirens Curr Genet 40 374 384
    • (2002) Curr Genet , vol.40 , pp. 374-384
    • Kim, D.J.1    Baek, J.M.2    Uribe, P.3    Kenerley, C.M.4    Cook5
  • 93
    • 28344455221 scopus 로고    scopus 로고
    • Expression of the chitinase gene from Trichoderma aureoviride in Saccharomyces cerevisiae
    • J Song Q Yang B Liu D Chen 2005 Expression of the chitinase gene from Trichoderma aureoviride in Saccharomyces cerevisiae Appl Microbiol Biotechnol 69 39 43
    • (2005) Appl Microbiol Biotechnol , vol.69 , pp. 39-43
    • Song, J.1    Yang, Q.2    Liu, B.3    Chen, D.4
  • 94
    • 0031606334 scopus 로고    scopus 로고
    • Cloning and characterization of a chitinase-encoding gene (chiA) from Aspergillus nidulans, disruption of which decreases germination frequency and hyphal growth
    • N Takaya D Yamazaki H Horiuchi A Ohta M Takagi 1998a Cloning and characterization of a chitinase-encoding gene (chiA) from Aspergillus nidulans, disruption of which decreases germination frequency and hyphal growth Biosci Biotechnol Biochem 62 60 65
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 60-65
    • Takaya, N.1    Yamazaki, D.2    Horiuchi, H.3    Ohta, A.4    Takagi, M.5
  • 95
    • 1842837225 scopus 로고    scopus 로고
    • Cloning and characterization of the nagA gene that encoded β-N-acetylglucosaminidase from Aspergillus nidulans and its expression in Aspergillus oryzae
    • S Kim I Matsuo K Ajisaka H Nakajima K Kitamoto 2002 Cloning and characterization of the nagA gene that encoded β-N-acetylglucosaminidase from Aspergillus nidulans and its expression in Aspergillus oryzae Biosci Biotechnol Biochem 66 2168 2175
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 2168-2175
    • Kim, S.1    Matsuo, I.2    Ajisaka, K.3    Nakajima, H.4    Kitamoto, K.5
  • 97
    • 0030807676 scopus 로고    scopus 로고
    • Sequence analysis of catalytic domain of a Metarhizium anisopliae chitinase
    • MC Valadares-Inglis PW Inglis JF Peberdy 1997 Sequence analysis of catalytic domain of a Metarhizium anisopliae chitinase Braz J Genet 20 161 164
    • (1997) Braz J Genet , vol.20 , pp. 161-164
    • Valadares-Inglis, M.C.1    Inglis, P.W.2    Peberdy, J.F.3
  • 98
    • 0031695855 scopus 로고    scopus 로고
    • A chitinase encoding gene (chit1 gene) from the entomopathogen Metarhizium anisopliae: Isolation and characterization of genomic and full-length cDNA
    • MR Bogo CA Rota H JR Pinto M Ocampos CT Correa MH Vainstein A Schrank 1998 A chitinase encoding gene (chit1 gene) from the entomopathogen Metarhizium anisopliae: isolation and characterization of genomic and full-length cDNA Curr Microbiol 37 221 225
    • (1998) Curr Microbiol , vol.37 , pp. 221-225
    • Bogo, M.R.1    Rota, C.A.2    Pinto Jr., H.3    Ocampos, M.4    Correa, C.T.5    Vainstein, M.H.6    Schrank, A.7
  • 99
    • 0035545111 scopus 로고    scopus 로고
    • Transformants of Metarhizium anisopliae sf. anisopliae overexpressing chitinase from Metarhizium anisopliae sf. acridum show early induction of native chitinase but are not altered in pathogenicity to Manduca sexta
    • SE Screen G Hu RT St Leger 2001 Transformants of Metarhizium anisopliae sf. anisopliae overexpressing chitinase from Metarhizium anisopliae sf. acridum show early induction of native chitinase but are not altered in pathogenicity to Manduca sexta J. Invertebr. Pathol 78 260 266
    • (2001) J. Invertebr. Pathol , vol.78 , pp. 260-266
    • Screen, S.E.1    Hu, G.2    St Leger, R.T.3
  • 101
    • 0032469706 scopus 로고    scopus 로고
    • Isolation and characterization of a chitinase cDNA from the entomopathogenic fungus, Metarhizium anisopliae
    • SC Kang S Park DG Lee 1998 Isolation and characterization of a chitinase cDNA from the entomopathogenic fungus, Metarhizium anisopliae FEMS Microbiol Lett 165 267 271
    • (1998) FEMS Microbiol Lett , vol.165 , pp. 267-271
    • Kang, S.C.1    Park, S.2    Lee, D.G.3
  • 102
    • 0026761188 scopus 로고
    • Primary structure of a chitinase-encoding gene (chi1) from the filamentous fungus Aphanocladium album: Similarity to bacterial chitinases
    • PL Blaiseau J Lafay 1992a Primary structure of a chitinase-encoding gene (chi1) from the filamentous fungus Aphanocladium album: similarity to bacterial chitinases Gene 120 243 248
    • (1992) Gene , vol.120 , pp. 243-248
    • Blaiseau, P.L.1    Lafay, J.2
  • 104
    • 0042668493 scopus 로고    scopus 로고
    • Molecular cloning, characterization, and expression of a cDNA encoding an endochitinase gene from the mycoparasite Stachybotrys elegans
    • DC Morissette BT Driscoll S Jabaji-Hare 2003 Molecular cloning, characterization, and expression of a cDNA encoding an endochitinase gene from the mycoparasite Stachybotrys elegans Fungal Genet Biol 39 276 285
    • (2003) Fungal Genet Biol , vol.39 , pp. 276-285
    • Morissette, D.C.1    Driscoll, B.T.2    Jabaji-Hare, S.3
  • 105
    • 0242676046 scopus 로고    scopus 로고
    • Isolation of genes expressed during compatible interactions between leaf rust (Puccinia triticina) and wheat using cDNA-AFLP
    • L Zhang H Meakin M Dickinson 2003 Isolation of genes expressed during compatible interactions between leaf rust (Puccinia triticina) and wheat using cDNA-AFLP Mol Plant Pathol 4 469 477
    • (2003) Mol Plant Pathol , vol.4 , pp. 469-477
    • Zhang, L.1    Meakin, H.2    Dickinson, M.3
  • 107
    • 33745012223 scopus 로고    scopus 로고
    • Molecular cloning and expression of a chitinase gene from the thermophilic fungus Thermomyces lanuginosus
    • (in Chinese)
    • RF Guo DC Li 2006 Molecular cloning and expression of a chitinase gene from the thermophilic fungus Thermomyces lanuginosus Acta Microbiol Sin 46 99 103 (in Chinese)
    • (2006) Acta Microbiol Sin , vol.46 , pp. 99-103
    • Guo, R.F.1    Li, D.C.2
  • 109
    • 0026599366 scopus 로고
    • Cloning and expression of chitinase gene from the hyperparasitic fungus Aphanocladium album
    • PL Blaiseau C Kunz R Grison Y Bertheau Y Brygoo 1992 Cloning and expression of chitinase gene from the hyperparasitic fungus Aphanocladium album Curr. Genet 21 61 66
    • (1992) Curr. Genet , vol.21 , pp. 61-66
    • Blaiseau, P.L.1    Kunz, C.2    Grison, R.3    Bertheau, Y.4    Brygoo, Y.5
  • 110
    • 0029936389 scopus 로고    scopus 로고
    • Improved production of Trichoderma harzianum endochitinase by expression in Trichoderma reesei
    • E Margolles-Clark CK Hayes GE Harman ME Penttila 1996 Improved production of Trichoderma harzianum endochitinase by expression in Trichoderma reesei Appl Environ Microbiol 62 2145 2151
    • (1996) Appl Environ Microbiol , vol.62 , pp. 2145-2151
    • Margolles-Clark, E.1    Hayes, C.K.2    Harman, G.E.3    Penttila, M.E.4
  • 113
    • 0033959611 scopus 로고    scopus 로고
    • Expression of endochitinase from Trichoderma harzianum in transgenic apple increases resistance to apple scab and reduces vigor
    • JP Bolar JL Norelli KW Wong CK Hayes GE Harman HS Aldwinckle 2000 Expression of endochitinase from Trichoderma harzianum in transgenic apple increases resistance to apple scab and reduces vigor Phytopathology 90 72 77
    • (2000) Phytopathology , vol.90 , pp. 72-77
    • Bolar, J.P.1    Norelli, J.L.2    Wong, K.W.3    Hayes, C.K.4    Harman, G.E.5    Aldwinckle, H.S.6
  • 114
    • 0029870606 scopus 로고    scopus 로고
    • Secretion of an enzymatically active Trichoderma harzianum endochitinase by Saccharomyces cerevisiae
    • H Draborg S Christgau T Halkier G Rasmussen H Dalboge S Kauppinen 1996 Secretion of an enzymatically active Trichoderma harzianum endochitinase by Saccharomyces cerevisiae Curr Genet 29 404 409
    • (1996) Curr Genet , vol.29 , pp. 404-409
    • Draborg, H.1    Christgau, S.2    Halkier, T.3    Rasmussen, G.4    Dalboge, H.5    Kauppinen, S.6
  • 115
    • 0028135314 scopus 로고
    • Cloning and characterization of chitinase (CHIT 42) cDNA from mycoparasitic fungus Trichoderma harzianum
    • G Irene ML Jose J De La Cruz B Tahia L Antonio A Jose T Pintor 1994 Cloning and characterization of chitinase (CHIT 42) cDNA from mycoparasitic fungus Trichoderma harzianum Curr Genet 27 83 89
    • (1994) Curr Genet , vol.27 , pp. 83-89
    • Irene, G.1    Jose, M.L.2    De La Cruz, J.3    Tahia, B.4    Antonio, L.5    Jose, A.6    Pintor, T.7
  • 117
    • 33644819734 scopus 로고    scopus 로고
    • Molecular cloning, characterization, and expression studies of a novel chitinase gene (ech30) from the mycoparasite Trichoderma atroviride strain P1
    • SS Klemsdal JL Clarke IA Hoell VG Eijsink MB Brurberg 2006 Molecular cloning, characterization, and expression studies of a novel chitinase gene (ech30) from the mycoparasite Trichoderma atroviride strain P1 FEMS Microbiol Lett 256 282 289
    • (2006) FEMS Microbiol Lett , vol.256 , pp. 282-289
    • Klemsdal, S.S.1    Clarke, J.L.2    Hoell, I.A.3    Eijsink, V.G.4    Brurberg, M.B.5
  • 118
    • 28344455221 scopus 로고    scopus 로고
    • Expression of the chitinase gene from Trichoderma aureviride in Saccharomyces cerevisiae
    • JZ Song Q Yang BD Liu DF Chen 2005 Expression of the chitinase gene from Trichoderma aureviride in Saccharomyces cerevisiae Appl Microbiol Biotechnol 69 39 43
    • (2005) Appl Microbiol Biotechnol , vol.69 , pp. 39-43
    • Song, J.Z.1    Yang, Q.2    Liu, B.D.3    Chen, D.F.4
  • 119
    • 0027225980 scopus 로고
    • New families in the classification of glycosylhydrolases based on amino acid sequence similarities
    • B Henrissat A Bairoch 1993 New families in the classification of glycosylhydrolases based on amino acid sequence similarities Biochem J 293 781 788
    • (1993) Biochem J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 122
    • 0030909499 scopus 로고    scopus 로고
    • Structural and evolutionary relationships among chitinases of flowering plants
    • F Hamel R Boivin C Tremblay G Bellemare 1997 Structural and evolutionary relationships among chitinases of flowering plants J Mol Evol 44 614 624
    • (1997) J Mol Evol , vol.44 , pp. 614-624
    • Hamel, F.1    Boivin, R.2    Tremblay, C.3    Bellemare, G.4
  • 123
    • 0033229842 scopus 로고    scopus 로고
    • The third chitinase gene (chiC) of Serratia marcescens 2170 and the relationship of its product to other bacterial chitinases
    • K Suzuki M Taiyoji N Sugawara N Nikaidou B Henrissat T Watanabe 1999 The third chitinase gene (chiC) of Serratia marcescens 2170 and the relationship of its product to other bacterial chitinases Biochem. J 343 587 596
    • (1999) Biochem. J , vol.343 , pp. 587-596
    • Suzuki, K.1    Taiyoji, M.2    Sugawara, N.3    Nikaidou, N.4    Henrissat, B.5    Watanabe, T.6
  • 125
    • 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
  • 126
    • 0024962351 scopus 로고
    • Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing
    • J Kraulis GM Clore M Nilges TA Jones G Pettersson J Knowles AM Gronenborn 1989 Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing Biochemistry 28 7241 7257
    • (1989) Biochemistry , vol.28 , pp. 7241-7257
    • Kraulis, J.1    Clore, G.M.2    Nilges, M.3    Jones, T.A.4    Pettersson, G.5    Knowles, J.6    Gronenborn, A.M.7
  • 127
    • 0035917427 scopus 로고    scopus 로고
    • Addition of substrate-binding domains increases substrate-binding capacity and specific activity of a chitinase from Trichoderma harzianum
    • MC Limon E Margolles-Clark T Benitez M Penttila 2001 Addition of substrate-binding domains increases substrate-binding capacity and specific activity of a chitinase from Trichoderma harzianum FEMS Microbiol Lett 198 57 63
    • (2001) FEMS Microbiol Lett , vol.198 , pp. 57-63
    • Limon, M.C.1    Margolles-Clark, E.2    Benitez, T.3    Penttila, M.4
  • 128
    • 0036220190 scopus 로고    scopus 로고
    • The use of trypsin to solubilize wall proteins from Candida albicans led to the identification of chitinase 2 as an enzyme covalently linked to the yeast wall structure
    • M Iranzo C Aguado C Pallotti JT Canizares S Mormeneo 2002 The use of trypsin to solubilize wall proteins from Candida albicans led to the identification of chitinase 2 as an enzyme covalently linked to the yeast wall structure Res Microbiol 153 227 232
    • (2002) Res Microbiol , vol.153 , pp. 227-232
    • Iranzo, M.1    Aguado, C.2    Pallotti, C.3    Canizares, J.T.4    Mormeneo, S.5
  • 130
    • 25144468884 scopus 로고    scopus 로고
    • Methylxanthine drugs are chitinase inhibits: Investigation of inhibition and binding model
    • FV Rao OA Anderson KA Vora JA Demartino DM Van Aalten 2005 Methylxanthine drugs are chitinase inhibits: investigation of inhibition and binding model Chem Biol 12 973 980
    • (2005) Chem Biol , vol.12 , pp. 973-980
    • Rao, F.V.1    Anderson, O.A.2    Vora, K.A.3    Demartino, J.A.4    Van Aalten, D.M.5
  • 131
    • 0031466989 scopus 로고    scopus 로고
    • Serratia marcescens chitobiase is a retaining glycosidase utilizing substrate acetamido group participation
    • S Drouillard S Armand GJ Davies CE Vorgias B Henrissat 1997 Serratia marcescens chitobiase is a retaining glycosidase utilizing substrate acetamido group participation Biochem J 328 945 949
    • (1997) Biochem J , vol.328 , pp. 945-949
    • Drouillard, S.1    Armand, S.2    Davies, G.J.3    Vorgias, C.E.4    Henrissat, B.5
  • 132
  • 133
    • 0027216435 scopus 로고
    • Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity
    • T Watanabe K Kobori K Miyashita T Fujii H Sakai M Usshida H Tanaka 1993 Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity J Biol Chem 268 18567 18572
    • (1993) J Biol Chem , vol.268 , pp. 18567-18572
    • Watanabe, T.1    Kobori, K.2    Miyashita, K.3    Fujii, T.4    Sakai, H.5    Usshida, M.6    Tanaka, H.7
  • 136
    • 0029856938 scopus 로고    scopus 로고
    • Mycoparasitic interaction relieves binding of Cre1 carbon catabolite repressor protein to promoter sequence of ech-42 (endochitinase-encoding) gene of Trichoderma harzianum
    • M Lorito RL Mach P Sposato J Strauss CK Peterbauer CP Kubicek 1996 Mycoparasitic interaction relieves binding of Cre1 carbon catabolite repressor protein to promoter sequence of ech-42 (endochitinase-encoding) gene of Trichoderma harzianum Proc Natl Acad Sci USA 93 14868 14872
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14868-14872
    • Lorito, M.1    MacH, R.L.2    Sposato, P.3    Strauss, J.4    Peterbauer, C.K.5    Kubicek, C.P.6
  • 138
    • 0028100107 scopus 로고
    • Parallel formation and synergism of hydrolytic enzymes and peptaibol antibiotics: Molecular mechanisms involved in the antagonistic action of Trichoderma harzianum against phytopathogenic fungi
    • M Schirmbock M Lorito YL Wang CK Hayes I Arisan-Atac F Scala GE Harman CP Kubicek 1994 Parallel formation and synergism of hydrolytic enzymes and peptaibol antibiotics: molecular mechanisms involved in the antagonistic action of Trichoderma harzianum against phytopathogenic fungi Appl Environ Microbiol 60 4364 4370
    • (1994) Appl Environ Microbiol , vol.60 , pp. 4364-4370
    • Schirmbock, M.1    Lorito, M.2    Wang, Y.L.3    Hayes, C.K.4    Arisan-Atac, I.5    Scala, F.6    Harman, G.E.7    Kubicek, C.P.8
  • 139
    • 0027156915 scopus 로고
    • A Saccharomyces cerevisiae AUS element controlled by a protein kinase a activates transcription in response to a variety of stress conditions
    • G Marchler C Schuller G Adam H Ruis 1993 A Saccharomyces cerevisiae AUS element controlled by a protein kinase A activates transcription in response to a variety of stress conditions EMBO J 12 1997 2003
    • (1993) EMBO J , vol.12 , pp. 1997-2003
    • Marchler, G.1    Schuller, C.2    Adam, G.3    Ruis, H.4
  • 140
    • 0032481247 scopus 로고    scopus 로고
    • Functional analysis of the stress response element and its role in the multistress response of Saccharomyces cerevisiae
    • JM Treger TR Magee K [tmp] McEntee 1998 Functional analysis of the stress response element and its role in the multistress response of Saccharomyces cerevisiae Biochem Biophys Res Commun 243 13 19
    • (1998) Biochem Biophys Res Commun , vol.243 , pp. 13-19
    • Treger, J.M.1    Magee, T.R.2    McEntee, K.3
  • 141
    • 0037469301 scopus 로고    scopus 로고
    • Expression of the ech42 (endochitinase) gene of Trichoderma atroviride under carbon starvation is antagonized via a BrlA-like cis-acting element
    • K Brunner M Montero RL Mach CK Peterbauer CP Kubicek 2003b Expression of the ech42 (endochitinase) gene of Trichoderma atroviride under carbon starvation is antagonized via a BrlA-like cis-acting element FEMS Microbiol Lett 218 258 264
    • (2003) FEMS Microbiol Lett , vol.218 , pp. 258-264
    • Brunner, K.1    Montero, M.2    MacH, R.L.3    Peterbauer, C.K.4    Kubicek, C.P.5
  • 142
    • 0027475409 scopus 로고
    • Identification of Aspergillus brlA response elements (BREs) by genetic selection in yeast
    • YC Chang WE Timberlake 1993 Identification of Aspergillus brlA response elements (BREs) by genetic selection in yeast Genetics 133 29 38
    • (1993) Genetics , vol.133 , pp. 29-38
    • Chang, Y.C.1    Timberlake, W.E.2
  • 143
    • 0343581290 scopus 로고    scopus 로고
    • Expression patterns of ten hemicellulase genes in the filamentous fungus Trichoderma reesei on various carbon sources
    • E Margolles-Clark EM Ilmen ME Penttila 1997 Expression patterns of ten hemicellulase genes in the filamentous fungus Trichoderma reesei on various carbon sources J. Biotechnol 57 167 179
    • (1997) J. Biotechnol , vol.57 , pp. 167-179
    • Margolles-Clark, E.1    Ilmen, E.M.2    Penttila, M.E.3
  • 144
    • 0028809669 scopus 로고
    • The role of recognition in the induction of specific chitinases during mycoparasitism by Trichoderma harzianum
    • J Inbar I Chet 1995 The role of recognition in the induction of specific chitinases during mycoparasitism by Trichoderma harzianum Microbiology 141 2823 2829
    • (1995) Microbiology , vol.141 , pp. 2823-2829
    • Inbar, J.1    Chet, I.2
  • 145
    • 0036242325 scopus 로고    scopus 로고
    • Identification of the N-acetyl-D-glucosamine-inducible element in the promoter of the Trichoderma atroviride nag1 gene encoding N-acetyl- glucosaminidase
    • CK Peterbauer K Brunner RL Mach CP Kubicek 2002 Identification of the N-acetyl-D-glucosamine-inducible element in the promoter of the Trichoderma atroviride nag1 gene encoding N-acetyl-glucosaminidase Mol. Genet. Genom 267 162 170
    • (2002) Mol. Genet. Genom , vol.267 , pp. 162-170
    • Peterbauer, C.K.1    Brunner, K.2    MacH, R.L.3    Kubicek, C.P.4
  • 146
    • 8844227515 scopus 로고    scopus 로고
    • Gene discovery and gene expression in the rice blast fungus, Magnaporthe grisea: Analysis of expressed sequence tags
    • DJ Ebbole Y Jin M Thon H Pan E Bhattarai T Thomas R Dean 2004 Gene discovery and gene expression in the rice blast fungus, Magnaporthe grisea: analysis of expressed sequence tags Mol Plant Microbe Interact 17 1337 1347
    • (2004) Mol Plant Microbe Interact , vol.17 , pp. 1337-1347
    • Ebbole, D.J.1    Jin, Y.2    Thon, M.3    Pan, H.4    Bhattarai, E.5    Thomas, T.6    Dean, R.7
  • 147
    • 0030036051 scopus 로고    scopus 로고
    • The glucose repressor gene cre1 of Trichoderma: Isolation and expression of a full-length and a truncated mutant form
    • M Ilmen C Thrane M Penttila 1996 The glucose repressor gene cre1 of Trichoderma: isolation and expression of a full-length and a truncated mutant form Mol Gen Genet 251 451 460
    • (1996) Mol Gen Genet , vol.251 , pp. 451-460
    • Ilmen, M.1    Thrane, C.2    Penttila, M.3
  • 149
    • 0142125683 scopus 로고    scopus 로고
    • Carbon repression of cellobiose dehydrogenase production in the white rot fungus Trametes versicolor is mediated at the level of gene transcription
    • PC Stapleton ADW Dobson 2003 Carbon repression of cellobiose dehydrogenase production in the white rot fungus Trametes versicolor is mediated at the level of gene transcription FEMS Microbiol Lett 221 167 172
    • (2003) FEMS Microbiol Lett , vol.221 , pp. 167-172
    • Stapleton, P.C.1    Dobson, A.D.W.2
  • 150
    • 0038192401 scopus 로고    scopus 로고
    • Carbon and pH modulate the expression of the fungal glucose repressor encoding genes
    • G Vautard-Mey M Ferre 2003 Carbon and pH modulate the expression of the fungal glucose repressor encoding genes Curr Microbiol 46 146 150
    • (2003) Curr Microbiol , vol.46 , pp. 146-150
    • Vautard-Mey, G.1    Ferre, M.2
  • 152
    • 0031735241 scopus 로고    scopus 로고
    • The expression of genes involved in parasitism by Trichoderma harzianum is triggered by a diffusible factor
    • C Cortes A Gutierrez V Olmedo J Inbar I Chet A Herrera-Estrella 1998 The expression of genes involved in parasitism by Trichoderma harzianum is triggered by a diffusible factor Mol Gen Genet 260 218 225
    • (1998) Mol Gen Genet , vol.260 , pp. 218-225
    • Cortes, C.1    Gutierrez, A.2    Olmedo, V.3    Inbar, J.4    Chet, I.5    Herrera-Estrella, A.6
  • 154
    • 0026599187 scopus 로고
    • Biomimics of fungal cell-cell recognition by use of lectin-coated nylon fibers
    • J Inbar I Chet 1992 Biomimics of fungal cell-cell recognition by use of lectin-coated nylon fibers J Bacteriol 174 1055 1059
    • (1992) J Bacteriol , vol.174 , pp. 1055-1059
    • Inbar, J.1    Chet, I.2
  • 155
    • 0028264938 scopus 로고
    • A newly isolated lectin from the plant pathogenic fungus Sclerotium rolfsii: Purification, characterization and its role in mycoparasitism
    • J Inbar I Chet 1994 A newly isolated lectin from the plant pathogenic fungus Sclerotium rolfsii: purification, characterization and its role in mycoparasitism Microbiology 140 651 657
    • (1994) Microbiology , vol.140 , pp. 651-657
    • Inbar, J.1    Chet, I.2
  • 157
    • 0031717286 scopus 로고    scopus 로고
    • Ace2p, a regulator of CTS1 (chitinase) expression, affects pseudohyphal production in Saccharomyces cerevisiae
    • L King G Butler 1998 Ace2p, a regulator of CTS1 (chitinase) expression, affects pseudohyphal production in Saccharomyces cerevisiae Curr Genet 34 183 191
    • (1998) Curr Genet , vol.34 , pp. 183-191
    • King, L.1    Butler, G.2
  • 158
    • 0037173615 scopus 로고    scopus 로고
    • Functional profiling of the Saccharomyces cerevisiae genome
    • G Giaver AM Chu L Ni 2002 Functional profiling of the Saccharomyces cerevisiae genome Nature 418 387 391
    • (2002) Nature , vol.418 , pp. 387-391
    • Giaver, G.1    Chu, A.M.2    Ni, L.3
  • 159
    • 27544509874 scopus 로고    scopus 로고
    • Candida albicans CHT3 encodes the functional homolog of the Cts1 chitinase of Saccharomyces cerevisiae
    • A Dunkler A Walther CA Specht J Wendland 2005 Candida albicans CHT3 encodes the functional homolog of the Cts1 chitinase of Saccharomyces cerevisiae Fungal Genet Biol 42 935 947
    • (2005) Fungal Genet Biol , vol.42 , pp. 935-947
    • Dunkler, A.1    Walther, A.2    Specht, C.A.3    Wendland, J.4
  • 160
    • 0034571968 scopus 로고    scopus 로고
    • Dimorphism in Benjaminiella poitrasii: Involvement of intracellular endochitinase and N-acetylglucosaminidase activities in the yeast-mycelium transition
    • VS Ghormade SA Lachke MV Deshpande 2000 Dimorphism in Benjaminiella poitrasii: involvement of intracellular endochitinase and N- acetylglucosaminidase activities in the yeast-mycelium transition Folia Microbiol 45 231 238
    • (2000) Folia Microbiol , vol.45 , pp. 231-238
    • Ghormade, V.S.1    Lachke, S.A.2    Deshpande, M.V.3
  • 162
    • 0033764315 scopus 로고    scopus 로고
    • Genetics and molecular physiology of the yeast Kluyveromyces lactis
    • R Schaffrath KD Breunig 2000 Genetics and molecular physiology of the yeast Kluyveromyces lactis Fungal Genet Biol 30 173 190
    • (2000) Fungal Genet Biol , vol.30 , pp. 173-190
    • Schaffrath, R.1    Breunig, K.D.2
  • 163
    • 0344301942 scopus 로고    scopus 로고
    • Allosamidin inhibits the fragmentation of Acremonium chrysogenum but does not influence the cephalosporin-C production of the fungus
    • E Sandor T Pusztahelyi L Karaffa Z Karanyi I Pocsi S Biro A Szentirmai I Pocsi 1998 Allosamidin inhibits the fragmentation of Acremonium chrysogenum but does not influence the cephalosporin-C production of the fungus FEMS Microbiol Lett 164 231 236
    • (1998) FEMS Microbiol Lett , vol.164 , pp. 231-236
    • Sandor, E.1    Pusztahelyi, T.2    Karaffa, L.3    Karanyi, Z.4    Pocsi, I.5    Biro, S.6    Szentirmai, A.7    Pocsi, I.8
  • 164
    • 0033806199 scopus 로고    scopus 로고
    • Disruption of the gene which encodes a serodiagnostic antigen and chitinase of the human fungal pathogen Coccidioides immitis
    • U Reichard CY Hung PW Thomas GT Cole 2000 Disruption of the gene which encodes a serodiagnostic antigen and chitinase of the human fungal pathogen Coccidioides immitis Infect Immunnol 68 5830 5838
    • (2000) Infect Immunnol , vol.68 , pp. 5830-5838
    • Reichard, U.1    Hung, C.Y.2    Thomas, P.W.3    Cole, G.T.4
  • 165
    • 0000330438 scopus 로고
    • Degradation of plant pathogenic fungi by Trichoderma harzianum
    • Y Elad I Chet Y Henis 1982 Degradation of plant pathogenic fungi by Trichoderma harzianum Can J Microbiol 28 719 725
    • (1982) Can J Microbiol , vol.28 , pp. 719-725
    • Elad, Y.1    Chet, I.2    Henis, Y.3
  • 166
    • 0003028612 scopus 로고
    • Parasitism of Trichoderma spp. on Rhizoctonia solani and Sclerotium rolfsii - Scanning electron microcopy studies and fluorescence microscopy
    • Y Elad I Chet P Boyle Y Henis 1983 Parasitism of Trichoderma spp. on Rhizoctonia solani and Sclerotium rolfsii - scanning electron microcopy studies and fluorescence microscopy Phytopathology 73 85 88
    • (1983) Phytopathology , vol.73 , pp. 85-88
    • Elad, Y.1    Chet, I.2    Boyle, P.3    Henis, Y.4
  • 169
    • 0042360627 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae chitinase, encoded by the CTS1-2 gene, confers antifungal activity against Botrytis cinerea to transgenic tobacco
    • M Carstens MA Vivier IS Pretorius 2003 The Saccharomyces cerevisiae chitinase, encoded by the CTS1-2 gene, confers antifungal activity against Botrytis cinerea to transgenic tobacco Trans Res 12 497 508
    • (2003) Trans Res , vol.12 , pp. 497-508
    • Carstens, M.1    Vivier, M.A.2    Pretorius, I.S.3
  • 170
    • 0023888714 scopus 로고
    • A simple method of protoplast formation and protoplast regeneration from various fungi using an enzyme from Trichoderma harzianum
    • Y Kitomoto N Mori M Yamamoto T Ohiwa Y Ichiwaka 1988 A simple method of protoplast formation and protoplast regeneration from various fungi using an enzyme from Trichoderma harzianum Appl Microbiol Biotechnol 28 445 450
    • (1988) Appl Microbiol Biotechnol , vol.28 , pp. 445-450
    • Kitomoto, Y.1    Mori, N.2    Yamamoto, M.3    Ohiwa, T.4    Ichiwaka, Y.5
  • 171
    • 0026091077 scopus 로고
    • Enzymatic hydrolysis of chitin by Myrothecium verrucaria chitinase complex and its utilization to produce SCP
    • PR Vyas MV Deshpande 1991 Enzymatic hydrolysis of chitin by Myrothecium verrucaria chitinase complex and its utilization to produce SCP J Gen Appl Microbiol 37 267 275
    • (1991) J Gen Appl Microbiol , vol.37 , pp. 267-275
    • Vyas, P.R.1    Deshpande, M.V.2
  • 172
    • 0025227062 scopus 로고
    • Screening microorganisms for chitin hydrolysis and production of ethanol from aminosugars
    • RM Cody ND Davis J Lin D Shaw 1990 Screening microorganisms for chitin hydrolysis and production of ethanol from aminosugars Biomass 21 285 295
    • (1990) Biomass , vol.21 , pp. 285-295
    • Cody, R.M.1    Davis, N.D.2    Lin, J.3    Shaw, D.4


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