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Volumn 50, Issue 9-10, 2012, Pages 722-735

Characterization of a chitinase (Chit62) from Serratia marcescens B4A and its efficacy as a bioshield against plant fungal pathogens

Author keywords

Chitinase; Fungal biocontrol; Heterologous expression; Protein activity assay

Indexed keywords

CHITINASE; RECOMBINANT CHITINASE; UNCLASSIFIED DRUG;

EID: 84866561941     PISSN: 00062928     EISSN: 15734927     Source Type: Journal    
DOI: 10.1007/s10528-012-9515-3     Document Type: Article
Times cited : (47)

References (54)
  • 1
    • 33846984593 scopus 로고    scopus 로고
    • Purification, characterization, kinetic properties, and thermal behavior of extracellular polygalacturonase produced by filamentous fungus Tetracoccosporium sp
    • Aminzadeh S, Naderi-Manesh H, Khajeh K, Naderi-Manesh M (2006) Purification, characterization, kinetic properties, and thermal behavior of extracellular polygalacturonase produced by filamentous fungus Tetracoccosporium sp. Appl Biochem Biotechnol 135:193-208
    • (2006) Appl Biochem Biotechnol , vol.135 , pp. 193-208
    • Aminzadeh, S.1    Naderi-Manesh, H.2    Khajeh, K.3    Naderi-Manesh, M.4
  • 2
    • 34249890833 scopus 로고    scopus 로고
    • Isolation and characterization of polygalacturonase produced by Tetracoccosporium sp
    • Aminzadeh S, Naderi-Manesh H, Khajeh K, Soudi M (2007) Isolation and characterization of polygalacturonase produced by Tetracoccosporium sp. Iran J Chem Chem Eng 26:47-54
    • (2007) Iran J Chem Chem Eng , vol.26 , pp. 47-54
    • Aminzadeh, S.1    Naderi-Manesh, H.2    Khajeh, K.3    Soudi, M.4
  • 3
    • 77949917402 scopus 로고    scopus 로고
    • Characterization of acidinduced partially folded conformation resembling a molten globule state of polygalacturonase from a filamentous fungus Tetracoccosporium sp
    • Aminzadeh S, Naderi-Manesh H, Khajeh K, Ranjbar B, Farrokhi N (2010) Characterization of acidinduced partially folded conformation resembling a molten globule state of polygalacturonase from a filamentous fungus Tetracoccosporium sp. Appl Biochem Biotechnol 160:1921-1932
    • (2010) Appl Biochem Biotechnol , vol.160 , pp. 1921-1932
    • Aminzadeh, S.1    Naderi-Manesh, H.2    Khajeh, K.3    Ranjbar, B.4    Farrokhi, N.5
  • 4
    • 2642550827 scopus 로고    scopus 로고
    • Isolation, cloning, and overexpression of a chitinase gene fragment from the hyperthermophilic archaeon Thermococcus chitonophagus: Semi-denaturing purification of the recombinant peptide and investigation of its relation with other chitinases
    • DOI 10.1016/j.pep.2004.02.002
    • Andronopoulou E, Vorgias CE (2004) Isolation, cloning, and overexpression of a chitinase gene fragment from the hyperthermophilic archaeon Thermococcus chitonophagus: semi-denaturing purification of the recombinant peptide and investigation of its relation with other chitinases. Protein Expr Purif 35:264-271 (Pubitemid 38718086)
    • (2004) Protein Expression and Purification , vol.35 , Issue.2 , pp. 264-271
    • Andronopoulou, E.1    Vorgias, C.E.2
  • 5
    • 84859183798 scopus 로고    scopus 로고
    • Identification of an antifungal chitinase from a potential biocontrol agent, Streptomyces plicatus strain 101, and its new antagonistic spectrum of activity
    • Baharlouei A, Sharifi-Sirchi GR, Shahidi Bonjar GH (2010) Identification of an antifungal chitinase from a potential biocontrol agent, Streptomyces plicatus strain 101, and its new antagonistic spectrum of activity. Philipp Agric Sci 93:439-445
    • (2010) Philipp Agric Sci , vol.93 , pp. 439-445
    • Baharlouei, A.1    Sharifi-Sirchi, G.R.2    Shahidi Bonjar, G.H.3
  • 6
    • 23444458378 scopus 로고    scopus 로고
    • Human acidic mammalian chitinase erroneously known as eosinophil chemotactic cytokine is not the ortholog of mouse Ym1 [2]
    • Boot RG, Bussink AP, Aerts JM (2005a) Human acidic mammalian chitinase erroneously known as eosinophil chemotactic cytokine is not the ortholog of mouse YM1. J Immunol 175:2041-2042 (Pubitemid 41113805)
    • (2005) Journal of Immunology , vol.175 , Issue.4 , pp. 2041-2042
    • Boot, R.G.1    Bussink, A.P.2    Aerts, J.M.F.G.3
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-252
    • (1976) Anal Biochem , vol.72 , pp. 248-252
    • Bradford, M.M.1
  • 9
    • 0029884662 scopus 로고    scopus 로고
    • Comparative studies of chitinases A and B from Serratia marcescens
    • Brurberg MB, Nes IF, Eijsink VG (1996) Comparative studies of chitinases A and B from Serratia marcescens. Microbiology 142:1581-1589 (Pubitemid 26248414)
    • (1996) Microbiology , vol.142 , Issue.7 , pp. 1581-1589
    • Brurberg, M.B.1    Nes, I.F.2    Eijsink, V.G.H.3
  • 10
    • 24044455383 scopus 로고    scopus 로고
    • Chitinase from Enterobacter sp. NRG4: Its purification, characterization and reaction pattern
    • DOI 10.2225/vol8-issue2-fulltext-6
    • Dahiya N, Tewari R, Tiwari RP, Hoondal GS (2005) Chitinase from Enterobacter sp. NRG4: its purification, characterization and reaction pattern. Electron J Biotechno 8:134-145 (Pubitemid 41215366)
    • (2005) Electronic Journal of Biotechnology , vol.8 , Issue.2 , pp. 134-145
    • Dahiya, N.1    Tewari, R.2    Tiwari, R.P.3    Hoondal, G.S.4
  • 11
    • 33746671918 scopus 로고    scopus 로고
    • Biotechnological aspects of chitinolytic enzymes: A review
    • DOI 10.1007/s00253-005-0183-7
    • Dahiya N, Tewari R, Hoondal GS (2006) Biotechnological aspects of chitinolytic enzymes: a review. Appl Microbiol Biotechnol 71:773-782 (Pubitemid 44162510)
    • (2006) Applied Microbiology and Biotechnology , vol.71 , Issue.6 , pp. 773-782
    • Dahiya, N.1    Tewari, R.2    Hoondal, G.S.3
  • 14
    • 0035206324 scopus 로고    scopus 로고
    • Purification and properties of two chitinolytic enzymes of Serratia plymuthica HRO-C48
    • DOI 10.1007/s002030100347
    • Frankowski J, Lorito M, Scala F, Schmid R, Berg G, Bahl H (2001) Purification and properties of two chitinolytic enzymes of Serratia plymuthica HRO-C48. Arch Microbiol 176:421-426 (Pubitemid 33139855)
    • (2001) Archives of Microbiology , vol.176 , Issue.6 , pp. 421-426
    • Frankowski, J.1    Lorito, M.2    Scala, F.3    Schmid, R.4    Berg, G.5    Bahl, H.6
  • 16
    • 84858119747 scopus 로고    scopus 로고
    • Extraction, purification and characterization of chitosan from endophytic fungi isolated from medicinal plants
    • George TS, Guru KSS, Vasanthi NS, Kannan KP (2011) Extraction, purification and characterization of chitosan from endophytic fungi isolated from medicinal plants. World J Sci Technol 1(4):43-48
    • (2011) World J Sci Technol , vol.1 , Issue.4 , pp. 43-48
    • George, T.S.1    Guru, K.S.S.2    Vasanthi, N.S.3    Kannan, K.P.4
  • 17
    • 0035073503 scopus 로고    scopus 로고
    • Purification of a thermostable endochitinase from Streptomyces RC1071 isolated from a cerrado soil and its antagonism against phytopathogenic fungi
    • DOI 10.1046/j.1365-2672.2001.01294.x
    • Gomes RC, Semedo LT, Soares RM, Soares RMA, Linhares LF, Ulhoa CJ, Alviano CS, Coelho RRR (2001) Purification of a thermostable endochitinase from Streptomyces RC1071 isolated from a cerrado soil and its antagonism against phytopathogenic fungi. J Appl Microbiol 90:653-661 (Pubitemid 32291269)
    • (2001) Journal of Applied Microbiology , vol.90 , Issue.4 , pp. 653-661
    • Gomes, R.C.1    Semedo, L.T.A.S.2    Soares, R.M.A.3    Linhares, L.F.4    Ulhoa, C.J.5    Alviano, C.S.6    Coelho, R.R.R.7
  • 18
    • 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. Biochem J 293:781-788 (Pubitemid 23244564)
    • (1993) Biochemical Journal , vol.293 , Issue.3 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 19
    • 6544291121 scopus 로고    scopus 로고
    • Expression and export of Pseudomonas putida NTU-8 creatinase by Escherichia coli using the chitinase signal sequence of Aeromonas hydrophila
    • DOI 10.1023/A:1018705831622
    • Hong MC, Chang JC, Wu ML, Chang MC (1998) Expression and export of Pseudomonas putida NTU-8 creatinase by Escherichia coli using the chitinase signal sequence of Aeromonas hydrophila. Biochem Genet 36(11/12):407-415 (Pubitemid 29202490)
    • (1998) Biochemical Genetics , vol.36 , Issue.11-12 , pp. 407-415
    • Hong, M.C.1    Chang, J.C.2    Wu, M.L.3    Chang, M.C.4
  • 20
    • 21244486744 scopus 로고    scopus 로고
    • Identification of an antifungal chitinase from a potential biocontrol agent, Bacillus cereus 28-9
    • Huang CJ, Wang TK, Chung SC, Chen CY (2005) Identification of an antifungal chitinase from a potential biocontrol agent, Bacillus cereus 28-9. J Biochem Mol Biol 38:82-88
    • (2005) J Biochem Mol Biol , vol.38 , pp. 82-88
    • Huang, C.J.1    Wang, T.K.2    Chung, S.C.3    Chen, C.Y.4
  • 21
    • 84855346039 scopus 로고    scopus 로고
    • Identification and characterization of a chitinase of Stenotrophomonas maltophilia, a bacterium that is antagonistic towards fungal phytopathogens
    • Jankiewicz U, Brzezinska MS, Saks E (2011) Identification and characterization of a chitinase of Stenotrophomonas maltophilia, a bacterium that is antagonistic towards fungal phytopathogens. J Biosci Bioeng 113:30-35
    • (2011) J Biosci Bioeng , vol.113 , pp. 30-35
    • Jankiewicz, U.1    Brzezinska, M.S.2    Saks, E.3
  • 22
    • 0001669533 scopus 로고
    • Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens
    • Jones JD, Grady KL, Suslow TV, Bedbrook JR (1986) Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens. EMBO J 5:467-473
    • (1986) EMBO J , vol.5 , pp. 467-473
    • Jones, J.D.1    Grady, K.L.2    Suslow, T.V.3    Bedbrook, J.R.4
  • 24
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H, Burk D (1934) The determination of enzyme dissociation constants. J Am Chem Soc 56:658-666
    • (1934) J Am Chem Soc , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 25
    • 77956188382 scopus 로고    scopus 로고
    • Cloning, heterologous expression, and functional characterization of a chitinase gene, Lbchi32, from Limonium bicolor
    • Liu ZH, Yang CP, Qi XT, Xiu LL, Wang YC (2010) Cloning, heterologous expression, and functional characterization of a chitinase gene, Lbchi32, from Limonium bicolor. Biochem Genet 48:669-679
    • (2010) Biochem Genet , vol.48 , pp. 669-679
    • Zh, L.1    Yang, C.P.2    Qi, X.T.3    Xiu, L.L.4    Wang, Y.C.5
  • 26
    • 0032541046 scopus 로고    scopus 로고
    • Switching of platelet-activating factor acetylhydrolase catalytic subunits in developing rat brain
    • DOI 10.1074/jbc.273.29.18567
    • Manya H, Aoki J, Watanabe M, Adachi T, Asou H, Inoue Y, Arai H, Inoue K (1998) Switching of platelet-activating factor acetylhydrolase catalytic subunits in developing rat brain. J Biol Chem 273:18567-18572 (Pubitemid 28334787)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.29 , pp. 18567-18572
    • Manya, H.1    Aoki, J.2    Watanabe, M.3    Adachi, T.4    Asou, H.5    Inoue, Y.6    Arai, H.7    Inoue, K.8
  • 28
    • 0346399742 scopus 로고    scopus 로고
    • Chitin metabolism in insects: Structure, function and regulation of chitin synthases and chitinases
    • DOI 10.1242/jeb.00709
    • Merzendorfer H, Zimoch L (2003) Chitin metabolism in insects: structure, function and regulation of chitin synthases and chitinases. J Exp Biol 206:4393-4412 (Pubitemid 38051454)
    • (2003) Journal of Experimental Biology , vol.206 , Issue.24 , pp. 4393-4412
    • Merzendorfer, H.1    Zimoch, L.2
  • 29
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31:426-428
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 30
    • 0035040869 scopus 로고    scopus 로고
    • One-step purification of chitinase from Serratia marcescens NK1, a soil isolate
    • DOI 10.1046/j.1365-2672.2001.01308.x
    • Nawani NN, Kapadnis BP (2001) One-step purification of chitinase from Serratia marcescens NK1, a soil isolate. J Appl Microbiol 90:803-808 (Pubitemid 32391787)
    • (2001) Journal of Applied Microbiology , vol.90 , Issue.5 , pp. 803-808
    • Nawani, N.N.1    Kapadnis, B.P.2
  • 31
    • 0034111127 scopus 로고    scopus 로고
    • Chitinolytic enzymes: An exploration
    • DOI 10.1016/S0141-0229(00)00134-4, PII S0141022900001344
    • Patil RS, Ghormade VV, Deshpande MV (2000) Chitinolytic enzymes: an exploration. Enzyme Microb Technol 26:473-483 (Pubitemid 30193319)
    • (2000) Enzyme and Microbial Technology , vol.26 , Issue.7 , pp. 473-483
    • Patil, R.S.1    Ghormade, V.2    Deshpande, M.V.3
  • 32
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • Peterson TN, Brunak S, von Heijne G, Nielsen H (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8:785-786
    • (2011) Nat Methods , vol.8 , pp. 785-786
    • Peterson, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 34
    • 53149149107 scopus 로고    scopus 로고
    • Cloning, characterization and expression of the chitinase gene of Enterobacter sp. NRG4
    • Salam M, Dahiya N, Sharma R, Soni SK, Hoondal GS, Tewari R (2008) Cloning, characterization and expression of the chitinase gene of Enterobacter sp. NRG4. Indian J Microbiol 48:358-364
    • (2008) Indian J Microbiol , vol.48 , pp. 358-364
    • Salam, M.1    Dahiya, N.2    Sharma, R.3    Soni, S.K.4    Hoondal, G.S.5    Tewari, R.6
  • 35
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitors of fungal growth
    • Schlumbaum A, Mauch F, Vogeli U (1986) Plant chitinases are potent inhibitors of fungal growth. Nature 324:355-356
    • (1986) Nature , vol.324 , pp. 355-356
    • Schlumbaum, A.1    Mauch, F.2    Vogeli, U.3
  • 36
    • 0041350490 scopus 로고    scopus 로고
    • Plant chitinase as a possible biocontrol agent for use instead of chemical fungicides
    • Shuji K, Shuhei T, Hiroshi K, Yuji Y, Daizo K (2003) Plant chitinase as a possible biocontrol agent for use instead of chemical fungicides. Biosci Biotech Bioch 67:221-224
    • (2003) Biosci Biotech Bioch , vol.67 , pp. 221-224
    • Shuji, K.1    Shuhei, T.2    Hiroshi, K.3    Yuji, Y.4    Daizo, K.5
  • 37
    • 84866548344 scopus 로고    scopus 로고
    • Effect of environmental factors on chitinase production by Serratia marcescens GG5
    • Singh G, Bhalla A, Singh Hoondal G (2010) Effect of environmental factors on chitinase production by Serratia marcescens GG5. IUP J Life Sci 4:16-24
    • (2010) IUP J Life Sci , vol.4 , pp. 16-24
    • Singh, G.1    Bhalla, A.2    Singh Hoondal, G.3
  • 38
    • 44649153432 scopus 로고    scopus 로고
    • Crystal structures of Vibrio harveyi chitinase A complexed with chitooligosaccharides: Implications for the catalytic mechanism
    • Songsiriritthigul C, Pantoom S, Aguda AH, Robinson RC, Suginta W (2008) Crystal structures of Vibrio harveyi chitinase A complexed with chitooligosaccharides: implications for the catalytic mechanism. J Struct Biol 162:491-499
    • (2008) J Struct Biol , vol.162 , pp. 491-499
    • Songsiriritthigul, C.1    Pantoom, S.2    Aguda, A.H.3    Robinson, R.C.4    Suginta, W.5
  • 39
    • 1642521614 scopus 로고    scopus 로고
    • Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase
    • DOI 10.1046/j.1432-1033.2003.03923.x
    • Synstad B, Gåseidnes S, Van Aalten DM, Vriend G, Nielsen JE, Eijsink VG (2004) Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase. Eur J Biochem 271(2):253-262 (Pubitemid 38130453)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.2 , pp. 253-262
    • Synstad, B.1    Gaseidnes, S.2    Van Aalten, D.M.F.3    Vriend, G.4    Nielsen, J.E.5    Eijsink, V.G.H.6
  • 40
    • 15244357854 scopus 로고    scopus 로고
    • Purification, characterization, and antifungal activity of chitinases from pineapple (Ananas comosus) leaf
    • DOI 10.1271/bbb.69.189
    • Taira T, Toma N, Ishihara M (2005) Purification, characterization, and antifungal activity of chitinases from pineapple (Ananas comosus) leaf. Biosci Biotechnol Biochem 69:189-196 (Pubitemid 40383499)
    • (2005) Bioscience, Biotechnology and Biochemistry , vol.69 , Issue.1 , pp. 189-196
    • Taira, T.1    Toma, N.2    Ishihara, M.3
  • 41
    • 83455209075 scopus 로고
    • Physical properties of chitinous materials
    • Takiguchi Y (1991) Physical properties of chitinous materials. Advanc Chitin Sci 111:1-7
    • (1991) Advanc Chitin Sci , vol.111 , pp. 1-7
    • Takiguchi, Y.1
  • 42
    • 0038697099 scopus 로고    scopus 로고
    • Purification and properties of chitinase from Enterobacter aerogenes
    • Tang Y, Zhao J, Ding S, Liu S, Yang Z (2001) Purification and properties of chitinase from Enterobacter aerogenes. Wei Sheng Wu Xue Bao 41:82-86
    • (2001) Wei Sheng Wu Xue Bao , vol.41 , pp. 82-86
    • Tang, Y.1    Zhao, J.2    Ding, S.3    Liu, S.4    Yang, Z.5
  • 44
    • 0024669485 scopus 로고
    • Detection of chitinase activity after polyacrylamide gel electrophoresis
    • Trudel J, Asselin A (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
  • 46
    • 78649328998 scopus 로고    scopus 로고
    • Chitobiose production by using a novel thermostable chitinase from Bacillus licheniformis strain JS isolated from a mushroom bed
    • Waghmare SR, Ghosh JS (2010a) Chitobiose production by using a novel thermostable chitinase from Bacillus licheniformis strain JS isolated from a mushroom bed. Carbohyd Res 345:2630-2635
    • (2010) Carbohyd Res , vol.345 , pp. 2630-2635
    • Waghmare, S.R.1    Ghosh, J.S.2
  • 47
    • 77952879130 scopus 로고    scopus 로고
    • Study of thermostable chitinases from Oerskovia xanthineolytica NCIM 2839
    • Waghmare SR, Ghosh JS (2010b) Study of thermostable chitinases from Oerskovia xanthineolytica NCIM 2839. Appl Microbiol Biotechnol 86:1849-1856
    • (2010) Appl Microbiol Biotechnol , vol.86 , pp. 1849-1856
    • Waghmare, S.R.1    Ghosh, J.S.2
  • 48
    • 67651227156 scopus 로고    scopus 로고
    • Cloning and expression of a novel chitinase chi58 from Chaetomium cupreum in Pichia pastoris
    • Wang YJ, Yang Q (2009) Cloning and expression of a novel chitinase chi58 from Chaetomium cupreum in Pichia pastoris. Biochem Genet 47:547-558
    • (2009) Biochem Genet , vol.47 , pp. 547-558
    • Wang, Y.J.1    Yang, Q.2
  • 49
    • 79954424604 scopus 로고    scopus 로고
    • Economic returns from fungicide application to control foliar fungal diseases in winter wheat
    • Wegulo SN, Zwingman MV, Breathnach JA, Baenziger PS (2011) Economic returns from fungicide application to control foliar fungal diseases in winter wheat. Crop Prot 30(6):685-692
    • (2011) Crop Prot , vol.30 , Issue.6 , pp. 685-692
    • Wegulo, S.N.1    Zwingman, M.V.2    Breathnach, J.A.3    Baenziger, P.S.4
  • 50
    • 0036307394 scopus 로고    scopus 로고
    • Purification, characterization and cloning of a chitinase from Bacillus sp. NCTU2
    • Wen CM, Tseng CS, Cheng CY, Li YK (2002) Purification, characterization and cloning of a chitinase from Bacillus sp. NCTU2. Biotechnol Appl Biochem 35:213-219
    • (2002) Biotechnol Appl Biochem , vol.35 , pp. 213-219
    • Wen, C.M.1    Tseng, C.S.2    Cheng, C.Y.3    Li, Y.K.4
  • 51
    • 0037339655 scopus 로고    scopus 로고
    • An extracellular Bacillus sp. chitinase for the production of chitotriose as a major chitinolytic product
    • Woo CJ, Park HD (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
  • 52
    • 48449103180 scopus 로고    scopus 로고
    • Control of grey mould rot of loquat with chitinase expressed in Pichia pastoris
    • Yan R, Ding D, Guan W, Hou J, Li M (2008) Control of grey mould rot of loquat with chitinase expressed in Pichia pastoris. Crop Prot 27:1312-1317
    • (2008) Crop Prot , vol.27 , pp. 1312-1317
    • Yan, R.1    Ding, D.2    Guan, W.3    Hou, J.4    Li, M.5
  • 53
    • 55549131112 scopus 로고    scopus 로고
    • Cloning and expression of an antifungal chitinase gene of a novel Bacillus subtilis isolate from Taiwan potato field
    • Yang CY, Ho YC, Pang JC, Huang SS, Tschen JSM (2009) Cloning and expression of an antifungal chitinase gene of a novel Bacillus subtilis isolate from Taiwan potato field. Bioresource Technol 100:1454-1458
    • (2009) Bioresource Technol , vol.100 , pp. 1454-1458
    • Yang, C.Y.1    Ho, Y.C.2    Pang, J.C.3    Huang, S.S.4    Jsm, T.5


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