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Volumn 68, Issue 4, 2014, Pages 495-502

Protein engineering of chit42 towards improvement of chitinase and antifungal activities

Author keywords

[No Author keywords available]

Indexed keywords

ANTIFUNGAL AGENTS; BINDING SITES; CHITIN; CHITINASE; FUNGAL PROTEINS; PROTEIN ENGINEERING; RECOMBINANT FUSION PROTEINS; TRANSFECTION; TRICHODERMA;

EID: 84893941074     PISSN: 03438651     EISSN: 14320991     Source Type: Journal    
DOI: 10.1007/s00284-013-0494-3     Document Type: Article
Times cited : (30)

References (32)
  • 1
    • 0028846149 scopus 로고
    • Properties of a single-chain antibody containing different linker peptides
    • 1:CAS:528:DyaK2MXptlOhsL4%3D 8577701 10.1093/protein/8.7.725
    • Alfthan K, Takkinen K, Sizmann D et al (1995) Properties of a single-chain antibody containing different linker peptides. Protein Eng 8:725-731
    • (1995) Protein Eng , vol.8 , pp. 725-731
    • Alfthan, K.1    Takkinen, K.2    Sizmann, D.3
  • 2
    • 0038130870 scopus 로고    scopus 로고
    • Properties of catalytic, linker and chitin-binding domains of insect chitinase
    • 1:CAS:528:DC%2BD3sXktFGjs70%3D 12770581 10.1016/S0965-1748(03)00049-3
    • Arakane Y, Zhu Q, Matsumiya M, Muthukrishnan S et al (2003) Properties of catalytic, linker and chitin-binding domains of insect chitinase. Insect Biochem Mol Biol 33:631-648
    • (2003) Insect Biochem Mol Biol , vol.33 , pp. 631-648
    • Arakane, Y.1    Zhu, Q.2    Matsumiya, M.3    Muthukrishnan, S.4
  • 3
    • 68449083191 scopus 로고    scopus 로고
    • Functional characterization of chitin and chitosan
    • 1:CAS:528:DC%2BD1MXmvVWru7Y%3D
    • Aranaz I, MengIbar M, Harris R, Panos I, Miralles B et al (2009) Functional characterization of chitin and chitosan. Curr Chem Biol 3:203-230
    • (2009) Curr Chem Biol , vol.3 , pp. 203-230
    • Aranaz, I.1    Mengibar, M.2    Harris, R.3    Panos, I.4    Miralles, B.5
  • 4
    • 77957057475 scopus 로고
    • Colorimetric assay for chitinase
    • 10.1016/0076-6879(88)61052-4
    • BollerT Mauch F (1988) Colorimetric assay for chitinase. Methods Enzymol 161:430-435
    • (1988) Methods Enzymol , vol.161 , pp. 430-435
    • Bollert, M.F.1
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • 10.1016/0003-2697(76)90527-3
    • Bradford M (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:249-254
    • (1976) Anal Biochem , vol.72 , pp. 249-254
    • Bradford, M.1
  • 6
    • 18144390619 scopus 로고    scopus 로고
    • Chitin-binding domain based immobilization of d-hydantoinase
    • 1:CAS:528:DC%2BD2MXjvVKmsLY%3D 15862357 10.1016/j.jbiotec.2005.02.001
    • Chern JT, Chao YP (2005) Chitin-binding domain based immobilization of d-hydantoinase. J Biotechnol 117:267-275
    • (2005) J Biotechnol , vol.117 , pp. 267-275
    • Chern, J.T.1    Chao, Y.P.2
  • 7
    • 0026777916 scopus 로고
    • Isolation and characterization of three chitinases from Trichoderma harzianum
    • 1606968 10.1111/j.1432-1033.1992.tb16994.x
    • De la Cruz J, Hidalgo-Gallego A, Lora JM, Benítez T et al (1992) Isolation and characterization of three chitinases from Trichoderma harzianum. Eur J Biochem 206:859-867
    • (1992) Eur J Biochem , vol.206 , pp. 859-867
    • De La Cruz, J.1    Hidalgo-Gallego, A.2    Lora, J.M.3    Benítez, T.4
  • 8
    • 0036266680 scopus 로고    scopus 로고
    • Aspartyl protease from Trichoderma harzianum CECT 2413: Cloning and characterization
    • 1:CAS:528:DC%2BD38XktFShsLk%3D 11988504
    • Delgado-Jarana J, Rincon AM, Benitez T (2002) Aspartyl protease from Trichoderma harzianum CECT 2413: cloning and characterization. Microbiology 148:1305-1315
    • (2002) Microbiology , vol.148 , pp. 1305-1315
    • Delgado-Jarana, J.1    Rincon, A.M.2    Benitez, T.3
  • 9
    • 33846122293 scopus 로고    scopus 로고
    • Increased insect virulence in Beauveria bassiana strains overexpressing an engineered chitinase
    • 1:CAS:528:DC%2BD2sXms1Wrsg%3D%3D 1797141 17085713 10.1128/AEM.01974-06
    • Fan Y, Fang W, Guo S, Pei X et al (2007) Increased insect virulence in Beauveria bassiana strains overexpressing an engineered chitinase. Appl Environ Microbiol 73:295-302
    • (2007) Appl Environ Microbiol , vol.73 , pp. 295-302
    • Fan, Y.1    Fang, W.2    Guo, S.3    Pei, X.4
  • 10
    • 0028135314 scopus 로고
    • Cloning and characterization of a chitinase (CHIT42) cDNA from the mycoparasitic fungus Trichoderma harzianum
    • 7750151 10.1007/BF00326583
    • García I, Lora JM, De la Cruz J, Benítez T et al (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
    • García, I.1    Lora, J.M.2    De La Cruz, J.3    Benítez, T.4
  • 11
    • 0028969372 scopus 로고
    • Development of primer sets designed for use with the PCR to amplify conserved genes from filamentous ascomycetes
    • 1:CAS:528:DyaK2MXksl2lsrY%3D 167388 7747954
    • Glass NL, Donaldson G (1995) Development of primer sets designed for use with the PCR to amplify conserved genes from filamentous ascomycetes. Appl Environ Microbiol 61:1323-1330
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1323-1330
    • Glass, N.L.1    Donaldson, G.2
  • 12
    • 27844461471 scopus 로고    scopus 로고
    • An improved method for detection and quantification of chitinase activities
    • 1:CAS:528:DC%2BD2MXhtFygsbvL 16121227 10.1139/w05-020
    • Guthrie JL, Khalif S, Castle AJ (2005) An improved method for detection and quantification of chitinase activities. Can J Microbiol 51:491-495
    • (2005) Can J Microbiol , vol.51 , pp. 491-495
    • Guthrie, J.L.1    Khalif, S.2    Castle, A.J.3
  • 13
    • 2542475295 scopus 로고    scopus 로고
    • Mutation of active site residues in the chitin-binding domain ChBDChiA1 from chitinase A1 of Bacillus circulans alters substrate specificity: Use of a green fluorescent protein binding assay
    • 1:CAS:528:DC%2BD2cXkt1Wrt78%3D 15158679 10.1016/j.abb.2004.03.017
    • Hardt M, Laine RA (2004) Mutation of active site residues in the chitin-binding domain ChBDChiA1 from chitinase A1 of Bacillus circulans alters substrate specificity: use of a green fluorescent protein binding assay. Arch Biochem Biophys 426:286-297
    • (2004) Arch Biochem Biophys , vol.426 , pp. 286-297
    • Hardt, M.1    Laine, R.A.2
  • 14
    • 0034127684 scopus 로고    scopus 로고
    • Expression and characterization of the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12
    • 1:CAS:528:DC%2BD3cXjsVyltr0%3D 94488 10809681 10.1128/JB.182.11.3045- 3054.2000
    • Hashimoto M, Ikegami T, Seino S, Ohuchi N et al (2000) Expression and characterization of the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12. J Bacteriol 182:3045-3054
    • (2000) J Bacteriol , vol.182 , pp. 3045-3054
    • Hashimoto, M.1    Ikegami, T.2    Seino, S.3    Ohuchi, N.4
  • 15
    • 79955115574 scopus 로고    scopus 로고
    • Comparative genome sequence analysis underscores mycoparasitism as the ancestral life style of Trichoderma
    • 1:CAS:528:DC%2BC3MXlslGnur0%3D 3218866 21501500 10.1186/gb-2011-12-4-r40
    • Kubicek CP, Herrera-Estrella A, Seidl-Seiboth V, Martinez DA, Druzhinina IS, Thon M, Zeilinger S et al (2011) Comparative genome sequence analysis underscores mycoparasitism as the ancestral life style of Trichoderma. Genome Biol 12:R40
    • (2011) Genome Biol , vol.12 , pp. 40
    • Kubicek, C.P.1    Herrera-Estrella, A.2    Seidl-Seiboth, V.3    Martinez, D.A.4    Druzhinina, I.S.5    Thon, M.6    Zeilinger, S.7
  • 16
    • 0000856986 scopus 로고
    • Isolation of DNA from fungal mycelia and single spores
    • D.G.M. Innis J. Sninsky T. White (eds) 34 Academic Press Orlando
    • Lee SB, Taylor JW (1990) Isolation of DNA from fungal mycelia and single spores. In: Innis DGM, Sninsky J, White T (eds) In: PCR protocols: a guide to methods and applications, vol 34. Academic Press, Orlando
    • (1990) PCR Protocols: A Guide to Methods and Applications
    • Lee, S.B.1    Taylor, J.W.2
  • 17
    • 0028880835 scopus 로고
    • Primary structure and expression pattern of the 33 kDa chitinase gene from the mycoparasitic fungus Trichoderma harzianum
    • 8575023 10.1007/BF00310819
    • Limón MC, Lora JM, García I, De la Cruz J, Llobell A et al (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
    • Limón, M.C.1    Lora, J.M.2    García, I.3    De La Cruz, J.4    Llobell, A.5
  • 18
    • 0035917427 scopus 로고    scopus 로고
    • Addition of substrate-binding domains increases substrate-binding capacity and specific activity of a chitinase from Trichoderma harzianum
    • 1:CAS:528:DC%2BD3MXivFehs7k%3D 11325554 10.1016/S0378-1097(01)00124-0
    • Limon MC, Margolles-Clark E, Benitez T, Penttila M (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
  • 19
    • 3042520658 scopus 로고    scopus 로고
    • Increased antifungal and chitinase specific activities of Trichoderma harzianum CECT 2413 by addition of a cellulose binding domain
    • 1:CAS:528:DC%2BD2cXjs1eiu7w%3D 14740190 10.1007/s00253-003-1538-6
    • Limon MC, Chacon MR, Mejias R, Delgado-Jarana J et al (2004) Increased antifungal and chitinase specific activities of Trichoderma harzianum CECT 2413 by addition of a cellulose binding domain. Appl Microbiol Biotechnol 64:675-685
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 675-685
    • Limon, M.C.1    Chacon, M.R.2    Mejias, R.3    Delgado-Jarana, J.4
  • 20
    • 0035710746 scopus 로고    scopus 로고
    • -ΔΔCT method
    • 1:CAS:528:DC%2BD38XhtFelt7s%3D 11846609 10.1006/meth.2001.1262
    • -ΔΔCT method. Methods 25:402-408
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.2
  • 21
    • 84855250877 scopus 로고    scopus 로고
    • Biocontrol of Fusarium head blight: Interactions between Trichoderma and mycotoxigenic Fusarium
    • 1:CAS:528:DC%2BC38XitVKmsro%3D 21980117 10.1099/mic.0.052639-0
    • Matarese F, Sarrocco S, Gruber S, Seidl SV, Vannacci G (2012) Biocontrol of Fusarium head blight: interactions between Trichoderma and mycotoxigenic Fusarium. Microbiology 158:98-106
    • (2012) Microbiology , vol.158 , pp. 98-106
    • Matarese, F.1    Sarrocco, S.2    Gruber, S.3    Seidl, S.V.4    Vannacci, G.5
  • 22
    • 0031695312 scopus 로고    scopus 로고
    • Transformants of Trichoderma longibrachiatum overexpressing the β-1,4-endoglucanase gene egl1 show enhanced biocontrol of Pythium ultimun on cucumber
    • 1:CAS:528:DyaK1cXksFClsLc%3D 18944939 10.1094/PHYTO.1998.88.7.673
    • Migheli Q, González-Candelas L, Dealessi L et al (1998) Transformants of Trichoderma longibrachiatum overexpressing the β-1,4-endoglucanase gene egl1 show enhanced biocontrol of Pythium ultimun on cucumber. Phytopathology 88:673-677
    • (1998) Phytopathology , vol.88 , pp. 673-677
    • Migheli, Q.1    González-Candelas, L.2    Dealessi, L.3
  • 23
    • 0023553310 scopus 로고
    • A versatile transformation system for the cellulolytic filamentous fungus Trichoderma reesei
    • 3127274 10.1016/0378-1119(87)90110-7
    • Penttilä M, Nevalainen H, Rättö M, Salminen E, Knowles J (1987) A versatile transformation system for the cellulolytic filamentous fungus Trichoderma reesei. Gene 61:155-164
    • (1987) Gene , vol.61 , pp. 155-164
    • Penttilä, M.1    Nevalainen, H.2    Rättö, M.3    Salminen, E.4    Knowles, J.5
  • 24
    • 67349131901 scopus 로고    scopus 로고
    • Chitin and chitosan polymers: Chemistry, solubility and fiber formation
    • 1:CAS:528:DC%2BD1MXlslWqtb4%3D 10.1016/j.progpolymsci.2009.04.001
    • Pillai CKS, Paul W, Chandra PS (2009) Chitin and chitosan polymers: chemistry, solubility and fiber formation. Prog Polym Sci 34:641-678
    • (2009) Prog Polym Sci , vol.34 , pp. 641-678
    • Pillai, C.K.S.1    Paul, W.2    Chandra, P.S.3
  • 25
    • 77049251255 scopus 로고
    • A modified colorimetric method for the estimation of N-acetylamino sugars
    • 1:CAS:528:DyaG28XhvFCqtA%3D%3D 13271455
    • Reissig JL, Strominger JL, Leloir L (1955) A modified colorimetric method for the estimation of N-acetylamino sugars. J Biol Chem 217:959-966
    • (1955) J Biol Chem , vol.217 , pp. 959-966
    • Reissig, J.L.1    Strominger, J.L.2    Leloir, L.3
  • 26
    • 79960087681 scopus 로고    scopus 로고
    • A identification of mycoparasitism-related genes in Trichoderma atroviride
    • 1:CAS:528:DC%2BC3MXptFWrsbw%3D 3127718 21531825 10.1128/AEM.00129-11
    • Reithner B, Ibarra-Laclette E, Mach RL, Estrella H (2011) A identification of mycoparasitism-related genes in Trichoderma atroviride. Appl Environ Microbiol 77:4361-4370
    • (2011) Appl Environ Microbiol , vol.77 , pp. 4361-4370
    • Reithner, B.1    Ibarra-Laclette, E.2    Mach, R.L.3    Estrella, H.4
  • 27
    • 84855218735 scopus 로고    scopus 로고
    • Saprotrophic competitiveness and biocontrol fitness of a genetically modified strain of the plant-growth-promoting fungus Trichoderma hamatum GD12
    • 1:CAS:528:DC%2BC38XitVKmsr0%3D 21835878 10.1099/mic.0.051854-0
    • Ryder LS, Harris BD, Soanes DM, Kershaw MJ et al (2012) Saprotrophic competitiveness and biocontrol fitness of a genetically modified strain of the plant-growth-promoting fungus Trichoderma hamatum GD12. Microbiology 158:84-97
    • (2012) Microbiology , vol.158 , pp. 84-97
    • Ryder, L.S.1    Harris, B.D.2    Soanes, D.M.3    Kershaw, M.J.4
  • 29
    • 33646470925 scopus 로고
    • In-vitro antagonism of Trichoderma spp. Against two fungal pathogens of castor
    • Sundar AR, Das ND, Krishnaveni D (1995) In-vitro antagonism of Trichoderma spp. against two fungal pathogens of castor. Indian J Plant Protec 23:152-155
    • (1995) Indian J Plant Protec , vol.23 , pp. 152-155
    • Sundar, A.R.1    Das, N.D.2    Krishnaveni, D.3
  • 30
    • 0035979240 scopus 로고    scopus 로고
    • Structural insights into the catalytic mechanism of a family 18 exo-chitinase
    • 11481469 10.1073/pnas.151103798
    • Van Aalten DMF, Komander D, Synstad B, Gaseidnes S et al (2001) Structural insights into the catalytic mechanism of a family 18 exo-chitinase. PNAS 98:8979-8984
    • (2001) PNAS , vol.98 , pp. 8979-8984
    • Van Aalten, D.M.F.1    Komander, D.2    Synstad, B.3    Gaseidnes, S.4
  • 31
    • 9644287958 scopus 로고    scopus 로고
    • Structure analysis and degree of substitution of chitin, chitosan and dibutyrylchitin by FT-IR spectroscopy and solid state 13C NMR
    • 10.1016/j.carbpol.2004.08.004
    • Van de Velde K, Kiekens P (2004) Structure analysis and degree of substitution of chitin, chitosan and dibutyrylchitin by FT-IR spectroscopy and solid state 13C NMR. Carbohydr Polym 58:409-416
    • (2004) Carbohydr Polym , vol.58 , pp. 409-416
    • Van De Velde, K.1    Kiekens, P.2
  • 32
    • 0026539865 scopus 로고
    • Purification of two chitinases from Rhizopus oligosporus and isolation and sequencing of the encoding genes
    • 1:CAS:528:DyaK3sXks1Knsb4%3D 207436 1429462
    • Yanai K, Takaya N, Kojima N, Horiuchi H et al (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


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