메뉴 건너뛰기




Volumn 6, Issue 1, 2013, Pages

Secretome diversity and quantitative analysis of cellulolytic Aspergillus fumigatus Z5 in the presence of different carbon sources

Author keywords

Aspergillus fumigatus; iTRAQ; LC MS MS; Lignocellulase; Secretome

Indexed keywords

ASPERGILLUS FUMIGATUS; ITRAQ; LC-MS/MS; LIGNOCELLULASE; SECRETOME;

EID: 84885436956     PISSN: 17546834     EISSN: None     Source Type: Journal    
DOI: 10.1186/1754-6834-6-149     Document Type: Article
Times cited : (106)

References (52)
  • 1
    • 0034922896 scopus 로고    scopus 로고
    • Fuel ethanol production from lignocellulose: A challenge for metabolic engineering and process integration
    • DOI 10.1007/s002530100624
    • Fuel ethanol production from lignocellulose: a challenge for metabolic engineering and process integration. Zaldivar J, Nielsen J, Olsson L, Applied microbiology and biotechnology 2001 56 17 34 10.1007/s002530100624 11499926 (Pubitemid 32663881)
    • (2001) Applied Microbiology and Biotechnology , vol.56 , Issue.1-2 , pp. 17-34
    • Zaldivar, J.1    Nielsen, J.2    Olsson, L.3
  • 2
    • 77954595049 scopus 로고    scopus 로고
    • Quantitative iTRAQ secretome analysis of cellulolytic Thermobifida fusca
    • 10.1021/pr901174z 20408570
    • Quantitative iTRAQ secretome analysis of cellulolytic Thermobifida fusca. Adav SS, Ng CS, Arulmani M, Sze SK, Journal of proteome research 2010 9 3016 3024 10.1021/pr901174z 20408570
    • (2010) Journal of Proteome Research , vol.9 , pp. 3016-3024
    • Adav, S.S.1    Ng, C.S.2    Arulmani, M.3    Sze, S.K.4
  • 3
    • 42149108423 scopus 로고    scopus 로고
    • Bioconversion of lignocellulosic biomass: Biochemical and molecular perspectives
    • 10.1007/s10295-008-0327-8 18338189
    • Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives. Kumar R, Singh S, Singh OV, Journal of industrial microbiology & biotechnology 2008 35 377 391 10.1007/s10295-008-0327-8 18338189
    • (2008) Journal of Industrial Microbiology & Biotechnology , vol.35 , pp. 377-391
    • Kumar, R.1    Singh, S.2    Singh, O.V.3
  • 4
    • 0037299771 scopus 로고    scopus 로고
    • Isolation and characteristics of Trichoderma harzianum FJ1 producing cellulases and xylanase
    • Isolation and characteristics of Trichoderma harzianum FJ1 producing cellulases and xylanase. Cheol KK, Yoo S-S, Y-A OH, Seong-Jun K, Journal of microbiology and biotechnology 2003 13 1 8 (Pubitemid 36348175)
    • (2003) Journal of Microbiology and Biotechnology , vol.13 , Issue.1 , pp. 1-8
    • Kim, K.C.1    Yoo, S.-S.2    Oh, Y.-A.3    Kim, S.-J.4
  • 5
    • 0037015407 scopus 로고    scopus 로고
    • Secretion, purification and characterisation of a recombinant Volvariella volvacea endoglucanase expressed in the yeast Pichia pastoris
    • DOI 10.1016/S0141-0229(02)00168-0, PII S0141022902001680
    • Secretion, purification and characterisation of a recombinant Volvariella volvacea endoglucanase expressed in the yeast Pichia pastoris. Ding S-j, Ge W, Buswell JA, Enzyme Microb Technol 2002 31 621 626 10.1016/S0141-0229(02)00168-0 (Pubitemid 35239849)
    • (2002) Enzyme and Microbial Technology , vol.31 , Issue.5 , pp. 621-626
    • Ding, S.-J.1    Ge, W.2    Buswell, J.A.3
  • 6
    • 82455171991 scopus 로고    scopus 로고
    • ITRAQ-based quantitative secretome analysis of Phanerochaete chrysosporium
    • 10.1016/j.jprot.2011.09.001 21945728
    • iTRAQ-based quantitative secretome analysis of Phanerochaete chrysosporium. Manavalan A, Adav SS, Sze SK, Journal of proteomics 2011 75 642 654 10.1016/j.jprot.2011.09.001 21945728
    • (2011) Journal of Proteomics , vol.75 , pp. 642-654
    • Manavalan, A.1    Adav, S.S.2    Sze, S.K.3
  • 7
    • 64049103021 scopus 로고    scopus 로고
    • Cloning of a GH5 endoglucanase from genus Penicillium and its binding to different lignins
    • 10.1016/j.enzmictec.2009.02.007
    • Cloning of a GH5 endoglucanase from genus Penicillium and its binding to different lignins. Krogh K, Kastberg H, Jørgensen C, Berlin A, Harris P, Olsson L, Enzyme Microb Technol 2009 44 359 367 10.1016/j.enzmictec.2009.02.007
    • (2009) Enzyme Microb Technol , vol.44 , pp. 359-367
    • Krogh, K.1    Kastberg, H.2    Jørgensen, C.3    Berlin, A.4    Harris, P.5    Olsson, L.6
  • 8
    • 11144285521 scopus 로고    scopus 로고
    • Presence and properties of cellulase and hemicellulase enzymes of the gecarcinid land crabs Gecarcoidea natalis and Discoplax hirtipes
    • DOI 10.1242/jeb.01252
    • Presence and properties of cellulase and hemicellulase enzymes of the gecarcinid land crabs Gecarcoidea natalis and Discoplax hirtipes. Linton SM, Greenaway P, Journal of experimental biology 2004 207 4095 4104 10.1242/jeb.01252 15498955 (Pubitemid 40024983)
    • (2004) Journal of Experimental Biology , vol.207 , Issue.23 , pp. 4095-4104
    • Linton, S.M.1    Greenaway, P.2
  • 9
    • 33745402798 scopus 로고    scopus 로고
    • Production of pectinase from deseeded sunflower head by Aspergillus niger in submerged and solid-state conditions
    • DOI 10.1016/j.biortech.2005.09.015, PII S0960852405004487
    • Production of pectinase from deseeded sunflower head by Aspergillus niger in submerged and solid-state conditions. Patil SR, Dayanand A, Bioresource technology 2006 97 2054 2058 10.1016/j.biortech.2005.09.015 16263274 (Pubitemid 43946669)
    • (2006) Bioresource Technology , vol.97 , Issue.16 , pp. 2054-2058
    • Patil, S.R.1    Dayanand, A.2
  • 10
    • 65249115211 scopus 로고    scopus 로고
    • Methods for pretreatment of lignocellulosic biomass for efficient hydrolysis and biofuel production
    • 10.1021/ie801542g
    • Methods for pretreatment of lignocellulosic biomass for efficient hydrolysis and biofuel production. Kumar P, Barrett DM, Delwiche MJ, Stroeve P, Ind Eng Chem Res 2009 48 3713 3729 10.1021/ie801542g
    • (2009) Ind Eng Chem Res , vol.48 , pp. 3713-3729
    • Kumar, P.1    Barrett, D.M.2    Delwiche, M.J.3    Stroeve, P.4
  • 11
    • 23744496272 scopus 로고    scopus 로고
    • Transcriptional regulation of plant cell wall degradation by filamentous fungi
    • DOI 10.1016/j.femsre.2004.11.006, PII S0168644504000920
    • Transcriptional regulation of plant cell wall degradation by filamentous fungi. Aro N, Pakula T, Penttilä M, FEMS microbiology reviews 2005 29 719 739 10.1016/j.femsre.2004.11.006 16102600 (Pubitemid 41139180)
    • (2005) FEMS Microbiology Reviews , vol.29 , Issue.4 , pp. 719-739
    • Aro, N.1    Pakula, T.2    Penttila, M.3
  • 12
    • 84861578199 scopus 로고    scopus 로고
    • Production of cellulases from Aspergillus niger NS-2 in solid state fermentation on agricultural and kitchen waste residues
    • 10.1016/j.wasman.2012.03.006 22503148
    • Production of cellulases from Aspergillus niger NS-2 in solid state fermentation on agricultural and kitchen waste residues. Bansal N, Tewari R, Soni R, Soni SK, Waste management 2012 32 1341 1346 10.1016/j.wasman.2012.03.006 22503148
    • (2012) Waste Management , vol.32 , pp. 1341-1346
    • Bansal, N.1    Tewari, R.2    Soni, R.3    Soni, S.K.4
  • 13
    • 79958019938 scopus 로고    scopus 로고
    • Thermostable cellulase production of Aspergillus fumigatus Z5 under solid-state fermentation and its application in degradation of agricultural wastes
    • 10.1016/j.ibiod.2011.04.005
    • Thermostable cellulase production of Aspergillus fumigatus Z5 under solid-state fermentation and its application in degradation of agricultural wastes. Liu D, Zhang R, Yang X, Wu H, Xu D, Tang Z, Shen Q, Int Biodeter Biodegr 2011 65 717 725 10.1016/j.ibiod.2011.04.005
    • (2011) Int Biodeter Biodegr , vol.65 , pp. 717-725
    • Liu, D.1    Zhang, R.2    Yang, X.3    Wu, H.4    Xu, D.5    Tang, Z.6    Shen, Q.7
  • 14
    • 84865572695 scopus 로고    scopus 로고
    • Production of cellulases by solid state fermentation with Aspergillus terreus and enzymatic hydrolysis of mild alkali-treated rice straw
    • 22864171
    • Production of cellulases by solid state fermentation with Aspergillus terreus and enzymatic hydrolysis of mild alkali-treated rice straw. Narra M, Dixit G, Divecha J, Madamwar D, Shah AR, Bioresour Technol 2012 121 355 361 22864171
    • (2012) Bioresour Technol , vol.121 , pp. 355-361
    • Narra, M.1    Dixit, G.2    Divecha, J.3    Madamwar, D.4    Shah, A.R.5
  • 15
    • 84859215368 scopus 로고    scopus 로고
    • Sequential solid-state and submerged cultivation of Aspergillus niger on sugarcane bagasse for the production of cellulase
    • 22409979
    • Sequential solid-state and submerged cultivation of Aspergillus niger on sugarcane bagasse for the production of cellulase. Cunha F, Esperança M, Zangirolami T, Badino A, Farinas C, Bioresour Technol 2012 112 270 274 22409979
    • (2012) Bioresour Technol , vol.112 , pp. 270-274
    • Cunha, F.1    Esperança, M.2    Zangirolami, T.3    Badino, A.4    Farinas, C.5
  • 16
    • 84865758129 scopus 로고    scopus 로고
    • Partitioning and purification of the cellulolytic complex produced by Aspergillus japonicus URM5620 using PEG-citrate in an aqueous two-phase system
    • Partitioning and purification of the cellulolytic complex produced by Aspergillus japonicus URM5620 using PEG-citrate in an aqueous two-phase system. Herculano PN, Porto TS, Maciel MH, Moreira KA, Souza-Motta CM, Porto AL, Fluid Phase Equilib 2012 335 8 13
    • (2012) Fluid Phase Equilib , vol.335 , pp. 8-13
    • Herculano, P.N.1    Porto, T.S.2    Maciel, M.H.3    Moreira, K.A.4    Souza-Motta, C.M.5    Porto, A.L.6
  • 17
    • 84865561632 scopus 로고    scopus 로고
    • Microbial cellulases and their industrial applications
    • Microbial cellulases and their industrial applications. Kuhad RC, Gupta R, Singh A, Enzyme Research 2011 2011 10
    • (2011) Enzyme Research , vol.2011 , pp. 10
    • Kuhad, R.C.1    Gupta, R.2    Singh, A.3
  • 19
    • 24944461039 scopus 로고    scopus 로고
    • Characterization of cellulases and hemicellulases produced by Trichoderma reesei on various carbon sources
    • DOI 10.1016/j.procbio.2005.03.057, PII S1359511305002035
    • Characterization of cellulases and hemicellulases produced by Trichoderma reesei on various carbon sources. Juhasz T, Szengyel Z, Reczey K, Siika-Aho M, Viikari L, Process Biochem 2005 40 3519 3525 10.1016/j.procbio.2005.03.057 (Pubitemid 41327364)
    • (2005) Process Biochemistry , vol.40 , Issue.11 , pp. 3519-3525
    • Juhasz, T.1    Szengyel, Z.2    Reczey, K.3    Siika-Aho, M.4    Viikari, L.5
  • 20
    • 80052026318 scopus 로고    scopus 로고
    • Enzyme production by filamentous fungi: Analysis of the secretome of Trichoderma reesei grown on unconventional carbon source
    • 10.1186/1475-2859-10-68 21861877
    • Enzyme production by filamentous fungi: analysis of the secretome of Trichoderma reesei grown on unconventional carbon source. Jun H, Kieselbach T, Jönsson L, Microb Cell Fact 2011 10 68 10.1186/1475-2859-10-68 21861877
    • (2011) Microb Cell Fact , vol.10 , pp. 68
    • Jun, H.1    Kieselbach, T.2    Jönsson, L.3
  • 21
    • 84855955479 scopus 로고    scopus 로고
    • Effect of different carbon sources on cellulase production by Hypocrea jecorina (Trichoderma reesei) strains
    • 22003440
    • Effect of different carbon sources on cellulase production by Hypocrea jecorina (Trichoderma reesei) strains. Mehdi Dashtban RB, Wensheng Q, Int J Biochem Mol Biol 2011 2 274 286 22003440
    • (2011) Int J Biochem Mol Biol , vol.2 , pp. 274-286
    • Mehdi Dashtban, R.B.1    Wensheng, Q.2
  • 22
    • 78049447484 scopus 로고    scopus 로고
    • Transcriptional regulator of carbon catabolite repression CreA in filamentous fungus
    • 20873228
    • Transcriptional regulator of carbon catabolite repression CreA in filamentous fungus. Chulkin AM, Vavilova EA, Benevolenskii SV, Mol Biol (Mosk) 2010 44 677 687 20873228
    • (2010) Mol Biol (Mosk) , vol.44 , pp. 677-687
    • Chulkin, A.M.1    Vavilova, E.A.2    Benevolenskii, S.V.3
  • 23
    • 0037226849 scopus 로고    scopus 로고
    • ACEI of Trichoderma reesei is a repressor of cellulase and xylanase expression
    • DOI 10.1128/AEM.69.1.56-65.2003
    • ACEI of Trichoderma reesei is a repressor of cellulase and xylanase expression. Aro N, Ilmén M, Saloheimo A, Penttilä M, Applied and environmental microbiology 2003 69 56 65 10.1128/AEM.69.1.56-65.2003 12513977 (Pubitemid 36077457)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.1 , pp. 56-65
    • Aro, N.1    Ilmen, M.2    Saloheimo, A.3    Penttila, M.4
  • 24
    • 78650849976 scopus 로고    scopus 로고
    • Production and characterization of cellulases and hemicellulases by Acremonium cellulolyticus using rice straw subjected to various pretreatments as the carbon source
    • 10.1016/j.enzmictec.2010.10.005 22112826
    • Production and characterization of cellulases and hemicellulases by Acremonium cellulolyticus using rice straw subjected to various pretreatments as the carbon source. Hideno A, Inoue H, Tsukahara K, Yano S, Fang X, Endo T, Sawayama S, Enzyme Microb Technol 2011 48 162 168 10.1016/j.enzmictec.2010.10. 005 22112826
    • (2011) Enzyme Microb Technol , vol.48 , pp. 162-168
    • Hideno, A.1    Inoue, H.2    Tsukahara, K.3    Yano, S.4    Fang, X.5    Endo, T.6    Sawayama, S.7
  • 25
    • 47249095445 scopus 로고    scopus 로고
    • Progress in bioethanol processing
    • 10.1016/j.pecs.2007.11.001
    • Progress in bioethanol processing. Balat M, Balat H, Oz C, Prog Energy Combust Sci 2008 34 551 573 10.1016/j.pecs.2007.11.001
    • (2008) Prog Energy Combust Sci , vol.34 , pp. 551-573
    • Balat, M.1    Balat, H.2    Oz, C.3
  • 26
    • 56949086429 scopus 로고    scopus 로고
    • Studies on carboxymethyl cellulase and xylanase activities of anaerobic fungal isolate CR4 from the bovine rumen
    • DOI 10.1007/s00284-008-9252-3
    • Studies on carboxymethyl cellulase and xylanase activities of anaerobic fungal isolate CR4 from the bovine rumen. Matsui H, Ban-Tokuda T, Curr Microbiol 2008 57 615 619 10.1007/s00284-008-9252-3 18791765 (Pubitemid 50270651)
    • (2008) Current Microbiology , vol.57 , Issue.6 , pp. 615-619
    • Matsui, H.1    Ban-Tokuda, T.2
  • 27
    • 77952876481 scopus 로고    scopus 로고
    • Profiling differential expression of cellulases and metabolite footprints in Aspergillus terreus
    • 10.1007/s12010-009-8775-9 19779865
    • Profiling differential expression of cellulases and metabolite footprints in Aspergillus terreus. Nazir A, Soni R, Saini HS, Kaur A, Chadha BS, Appl Biochem Biotechnol 2010 162 538 547 10.1007/s12010-009-8775-9 19779865
    • (2010) Appl Biochem Biotechnol , vol.162 , pp. 538-547
    • Nazir, A.1    Soni, R.2    Saini, H.S.3    Kaur, A.4    Chadha, B.S.5
  • 28
    • 80051657017 scopus 로고    scopus 로고
    • Functional characterization of cellulases identified from the cow rumen fungus Neocallimastix patriciarum W5 by transcriptomic and secretomic analyses
    • 10.1186/1754-6834-4-24 21849025
    • Functional characterization of cellulases identified from the cow rumen fungus Neocallimastix patriciarum W5 by transcriptomic and secretomic analyses. Wang T-Y, Chen H-L, Lu M, Chen Y-C, Sung H-M, Mao C-T, Cho H-Y, Ke H-M, Hwa T-Y, Ruan S-K, Biotechnol Biofuels 2011 4 24 10.1186/1754-6834-4-24 21849025
    • (2011) Biotechnol Biofuels , vol.4 , pp. 24
    • Wang, T.-Y.1    Chen, H.-L.2    Lu, M.3    Chen, Y.-C.4    Sung, H.-M.5    Mao, C.-T.6    Cho, H.-Y.7    Ke, H.-M.8    Hwa, T.-Y.9    Ruan, S.-K.10
  • 29
    • 77955445449 scopus 로고    scopus 로고
    • Quantitative iTRAQ secretome analysis of aspergillus niger reveals novel hydrolytic enzymes
    • 10.1021/pr100148j 20545367
    • Quantitative iTRAQ secretome analysis of aspergillus niger reveals novel hydrolytic enzymes. Adav SS, Li AA, Manavalan A, Punt P, Sze SK, J Proteome Res 2010 9 3932 3940 10.1021/pr100148j 20545367
    • (2010) J Proteome Res , vol.9 , pp. 3932-3940
    • Adav, S.S.1    Li, A.A.2    Manavalan, A.3    Punt, P.4    Sze, S.K.5
  • 30
    • 42149108423 scopus 로고    scopus 로고
    • Bioconversion of lignocellulosic biomass: Biochemical and molecular perspectives
    • 10.1007/s10295-008-0327-8
    • Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives. Kumar RS S, Singh OV, J Indust Microbiol Biotechnol 2008 35 377 391 10.1007/s10295-008-0327-8
    • (2008) J Indust Microbiol Biotechnol , vol.35 , pp. 377-391
    • Kumar Rs, S.1    Singh, O.V.2
  • 31
    • 0028017094 scopus 로고
    • A paper mill sludge as a potential source for cellulose production by Trichoderma reesei QM9123 and Aspergillus niger using mixed cultivation
    • 10.1016/0144-8617(94)90098-1
    • A paper mill sludge as a potential source for cellulose production by Trichoderma reesei QM9123 and Aspergillus niger using mixed cultivation. Maheshwari DKG S, Paul J, Verma A, Carbohydr Polym 1994 23 161 163 10.1016/0144-8617(94)90098-1
    • (1994) Carbohydr Polym , vol.23 , pp. 161-163
    • Maheshwari Dkg, S.1    Paul, J.2    Verma, A.3
  • 32
    • 0001600598 scopus 로고
    • Formation of cellulases by co-culturing of Trichoderma reesei and Aspergillus niger on cellulosic waste
    • 10.1007/BF01195843
    • Formation of cellulases by co-culturing of Trichoderma reesei and Aspergillus niger on cellulosic waste. Madamwar D, Patel S, World J Microbiol Biotechnol 1992 8 183 186 10.1007/BF01195843
    • (1992) World J Microbiol Biotechnol , vol.8 , pp. 183-186
    • Madamwar, D.1    Patel, S.2
  • 33
    • 0034253281 scopus 로고    scopus 로고
    • Alpha-L-arabinofuranosidases-biochemistry, molecular biology and application in biotechnology
    • 10.1016/S0734-9750(00)00044-6
    • Alpha-L-arabinofuranosidases-biochemistry, molecular biology and application in biotechnology. Saha BC, Biotech Adv 2000 18 403 423 10.1016/S0734-9750(00)00044-6
    • (2000) Biotech Adv , vol.18 , pp. 403-423
    • Saha, B.C.1
  • 34
    • 0027351945 scopus 로고
    • Structural models of primary cell walls in flowering plants: Consistency of molecular structure with the physical properties of the walls during growth
    • 10.1111/j.1365-313X.1993.tb00007.x 8401598
    • Structural models of primary cell walls in flowering plants: consistency of molecular structure with the physical properties of the walls during growth. Carpita NCG DM, Plant J 1993 3 1 30 10.1111/j.1365-313X.1993.tb00007.x 8401598
    • (1993) Plant J , vol.3 , pp. 1-30
    • Carpita Ncg, D.M.1
  • 35
    • 0025220288 scopus 로고
    • Molecular and genetic characterization of two pollen-expressed genes that have sequence similarity to pectate lyases of the plant pathogen Erwinia
    • 10.1007/BF00015651 1983191
    • Molecular and genetic characterization of two pollen-expressed genes that have sequence similarity to pectate lyases of the plant pathogen Erwinia. Wing RA, Yamaguchi J, Larabell SK, Ursin VM, McCormick S, Plant Mol Biol 1990 14 17 28 10.1007/BF00015651 1983191
    • (1990) Plant Mol Biol , vol.14 , pp. 17-28
    • Wing, R.A.1    Yamaguchi, J.2    Larabell, S.K.3    Ursin, V.M.4    McCormick, S.5
  • 36
    • 82455171991 scopus 로고    scopus 로고
    • ITRAQ-based quantitative secretome analysis of Phanerochaete chrysosporium
    • 10.1016/j.jprot.2011.09.001 21945728
    • iTRAQ-based quantitative secretome analysis of Phanerochaete chrysosporium. Arulmani Manavalan SSA, Siu Kwan S, Journal of proteomics 2011 75 642 654 10.1016/j.jprot.2011.09.001 21945728
    • (2011) Journal of Proteomics , vol.75 , pp. 642-654
    • Arulmani Manavalan, S.S.A.1    Siu Kwan, S.2
  • 37
    • 0000010402 scopus 로고
    • The production of cellulases
    • The production of cellulases. Mandels M, Weber J, Am Chem Soc 1969 95 391 414
    • (1969) Am Chem Soc , vol.95 , pp. 391-414
    • Mandels, M.1    Weber, J.2
  • 38
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • 10.1021/ac60147a030
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar. Miller GL, Analytical chemistry 1959 31 426 428 10.1021/ac60147a030
    • (1959) Analytical Chemistry , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 40
    • 0035156434 scopus 로고    scopus 로고
    • Biochemical characterization and mechanism of action of a thermostable beta-glucosidase purified from thermoascus aurantiacus
    • 11115405
    • Biochemical characterization and mechanism of action of a thermostable beta-glucosidase purified from thermoascus aurantiacus. Parry NJ, Beever DE, Owen E, Vandenberghe I, Van Beeumen J, Bhat MK, Biochem J 2001 353 117 11115405
    • (2001) Biochem J , vol.353 , pp. 117
    • Parry, N.J.1    Beever, D.E.2    Owen, E.3    Vandenberghe, I.4    Van Beeumen, J.5    Bhat, M.K.6
  • 42
    • 0032077271 scopus 로고    scopus 로고
    • Multiple forms of polygalacturonase from banana fruits
    • DOI 10.1016/S0031-9422(98)00005-3, PII S0031942298000053
    • Multiple forms of polygalacturonase from banana fruits. Pathak N, Sanwal G, Phytochemistry 1998 48 249 255 10.1016/S0031-9422(98)00005-3 9637063 (Pubitemid 28268162)
    • (1998) Phytochemistry , vol.48 , Issue.2 , pp. 249-255
    • Pathak, N.1    Sanwal, G.G.2
  • 43
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 10.1038/227680a0 5432063
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Laemmli UK, Nature 1970 227 680 685 10.1038/227680a0 5432063
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 44
    • 0028210294 scopus 로고
    • A zymogram method to detect endoglucanases from Bacillus subtilis, Myrothecium verrucaria and Trichoderma reesei
    • A zymogram method to detect endoglucanases from Bacillus subtilis, Myrothecium verrucaria and Trichoderma reesei. Holt SM, Hartman PA, J Ind Microbiol Biotechnol 1994 13 2 4 (Pubitemid 24104112)
    • (1994) Journal of Industrial Microbiology , vol.13 , Issue.1 , pp. 2-4
    • Holt, S.M.1    Hartman, P.A.2
  • 45
    • 38049060254 scopus 로고    scopus 로고
    • A proteomics strategy to discover β-glucosidases from Aspergillus fumigatus with two-dimensional page in-gel activity assay and tandem mass spectrometry
    • 10.1021/pr070355i 18020405
    • A proteomics strategy to discover β-glucosidases from Aspergillus fumigatus with two-dimensional page in-gel activity assay and tandem mass spectrometry. Kim KH, Brown KM, Harris PV, Langston JA, Cherry JR, Journal of proteome research 2007 6 4749 4757 10.1021/pr070355i 18020405
    • (2007) Journal of Proteome Research , vol.6 , pp. 4749-4757
    • Kim, K.H.1    Brown, K.M.2    Harris, P.V.3    Langston, J.A.4    Cherry, J.R.5
  • 46
    • 0037007498 scopus 로고    scopus 로고
    • Purification and characterization of two cellulase free xylanases from an alkaliphilic Bacillus firmus
    • DOI 10.1016/S0141-0229(02)00018-2, PII S0141022901000182
    • Purification and characterization of two cellulase free xylanases from an alkaliphilic Bacillus firmus. Tseng M-J, Yap M-N, Ratanakhanokchai K, Kyu KL, Chen S-T, Enzyme Microb Technol 2002 30 590 595 10.1016/S0141-0229(02)00018-2 (Pubitemid 34406445)
    • (2002) Enzyme and Microbial Technology , vol.30 , Issue.5 , pp. 590-595
    • Tseng, M.-J.1    Yap, M.-N.2    Ratanakhanokchai, K.3    Kyu, K.L.4    Chen, S.-T.5
  • 48
    • 77349116857 scopus 로고    scopus 로고
    • Proteomic analysis of prolactinoma cells by immuno-laser capture microdissection combined with online two-dimensional nano-scale liquid chromatography/mass spectrometry
    • 10.1186/1477-5956-8-2 20205839
    • Proteomic analysis of prolactinoma cells by immuno-laser capture microdissection combined with online two-dimensional nano-scale liquid chromatography/mass spectrometry. Liu Y, Wu J, Yan G, Hou R, Zhuang D, Chen L, Pang Q, Zhu J, Proteome Sci 2010 8 2 10.1186/1477-5956-8-2 20205839
    • (2010) Proteome Sci , vol.8 , pp. 2
    • Liu, Y.1    Wu, J.2    Yan, G.3    Hou, R.4    Zhuang, D.5    Chen, L.6    Pang, Q.7    Zhu, J.8
  • 49
    • 43049168829 scopus 로고    scopus 로고
    • Enzymatic digestion of proteins in solution
    • 18429101
    • Enzymatic digestion of proteins in solution. Riviere LR, Tempst P, Curr Protoc Protein Sci 2001 11 1 9 18429101
    • (2001) Curr Protoc Protein Sci , vol.11 , pp. 1-9
    • Riviere, L.R.1    Tempst, P.2
  • 50
    • 80052037383 scopus 로고    scopus 로고
    • ITRAQ-based quantitative proteomic analysis of Thermobifida fusca reveals metabolic pathways of cellulose utilization
    • 10.1016/j.jprot.2011.05.038 21704745
    • iTRAQ-based quantitative proteomic analysis of Thermobifida fusca reveals metabolic pathways of cellulose utilization. Adav SS, Ng CS, Sze SK, J Proteomics 2011 74 2112 2122 10.1016/j.jprot.2011.05.038 21704745
    • (2011) J Proteomics , vol.74 , pp. 2112-2122
    • Adav, S.S.1    Ng, C.S.2    Sze, S.K.3
  • 51
    • 84856341952 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of lignocellulolytic enzymes by Phanerochaete chrysosporium on different lignocellulosic biomass
    • 10.1016/j.jprot.2011.11.020 22146477
    • Quantitative proteomic analysis of lignocellulolytic enzymes by Phanerochaete chrysosporium on different lignocellulosic biomass. Adav SS, Ravindran A, Sze SK, J Proteomics 2012 75 1493 1504 10.1016/j.jprot.2011.11.020 22146477
    • (2012) J Proteomics , vol.75 , pp. 1493-1504
    • Adav, S.S.1    Ravindran, A.2    Sze, S.K.3
  • 52
    • 84863983350 scopus 로고    scopus 로고
    • ITRAQ-coupled 2D LC-MS/MS analysis on differentially expressed proteins in denervated tibialis anterior muscle of Rattus norvegicus
    • 10.1007/s11010-011-1218-2 22227918
    • iTRAQ-coupled 2D LC-MS/MS analysis on differentially expressed proteins in denervated tibialis anterior muscle of Rattus norvegicus. Sun H, Li M, Gong L, Liu M, Ding F, Gu X, Mol Cell Biochem 2012 364 193 207 10.1007/s11010-011- 1218-2 22227918
    • (2012) Mol Cell Biochem , vol.364 , pp. 193-207
    • Sun, H.1    Li, M.2    Gong, L.3    Liu, M.4    Ding, F.5    Gu, X.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.