메뉴 건너뛰기




Volumn 42, Issue 8, 2007, Pages 1237-1243

Purification and characterization of an exo-polygalacturonase produced by Penicillium viridicatum RFC3 in solid-state fermentation

Author keywords

Penicillium; Polygalacturonase; Purification; Solid state fermentation

Indexed keywords

GALACTURONIC ACID; PENICILLIUM; POLYGALACTURONASE; SOLID STATE FERMENTATION;

EID: 34447629187     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2007.05.025     Document Type: Article
Times cited : (38)

References (36)
  • 1
    • 0041990500 scopus 로고
    • Microbial pectinolytic enzymes
    • Fogarty W.M., and Kelly C.T. (Eds), Elsevier Science Ltd., London
    • Whitaker J.R. Microbial pectinolytic enzymes. In: Fogarty W.M., and Kelly C.T. (Eds). Microbial enzymes and biotechnology. 2nd ed. (1990), Elsevier Science Ltd., London 133-176
    • (1990) Microbial enzymes and biotechnology. 2nd ed. , pp. 133-176
    • Whitaker, J.R.1
  • 2
    • 0037691098 scopus 로고    scopus 로고
    • Microbial pectinases
    • Seymour G.B., and Knox J.P. (Eds), Blackwell Publishing Ltd., Oxford
    • Bene J.A.E., Vincken J.P., and Van Alebeek G.J.W.M. Microbial pectinases. In: Seymour G.B., and Knox J.P. (Eds). Pectins and their manipulation (2002), Blackwell Publishing Ltd., Oxford 174-221
    • (2002) Pectins and their manipulation , pp. 174-221
    • Bene, J.A.E.1    Vincken, J.P.2    Van Alebeek, G.J.W.M.3
  • 3
    • 0024575448 scopus 로고
    • Enzymatic degradation of cell wall and related plant polysaccharides
    • Ward O.P., and Moo-Young M. Enzymatic degradation of cell wall and related plant polysaccharides. CRC Crit Rev Biotechnol 8 (1989) 237-274
    • (1989) CRC Crit Rev Biotechnol , vol.8 , pp. 237-274
    • Ward, O.P.1    Moo-Young, M.2
  • 4
    • 15744372800 scopus 로고    scopus 로고
    • Pectinase production from Penicillium viridicatum RFC3 by solid-state fermentation using agricultural residues and agro-industrial by-product
    • Silva D., Martins E.S., Da Silva R., and Gomes E. Pectinase production from Penicillium viridicatum RFC3 by solid-state fermentation using agricultural residues and agro-industrial by-product. Braz J Microbiol 33 (2002) 318-324
    • (2002) Braz J Microbiol , vol.33 , pp. 318-324
    • Silva, D.1    Martins, E.S.2    Da Silva, R.3    Gomes, E.4
  • 5
    • 0028810288 scopus 로고
    • Production and properties of three pectinolytic activities produced by Aspergillus niger in submerged and solid-state fermentation
    • Acuña-Argüelles M.E., Gutiérrez-Rojas M., Viniegra-González G., and Favela-Torres E. Production and properties of three pectinolytic activities produced by Aspergillus niger in submerged and solid-state fermentation. Appl Microbiol Biotechnol 43 (1995) 808-814
    • (1995) Appl Microbiol Biotechnol , vol.43 , pp. 808-814
    • Acuña-Argüelles, M.E.1    Gutiérrez-Rojas, M.2    Viniegra-González, G.3    Favela-Torres, E.4
  • 6
    • 4143141031 scopus 로고    scopus 로고
    • Purification and biochemical characterization of polygalacturonase II produced in semi-solid medium by a strain of Fusarium moniliforme
    • Niture S.K., and Pant A. Purification and biochemical characterization of polygalacturonase II produced in semi-solid medium by a strain of Fusarium moniliforme. Microbiol Res 154 (2004) 305-314
    • (2004) Microbiol Res , vol.154 , pp. 305-314
    • Niture, S.K.1    Pant, A.2
  • 7
    • 2442446299 scopus 로고    scopus 로고
    • Purification of the extracellular pectinolytic enzyme from the fungus Rhizopus oryzae NBRC 4707
    • Saito K., Takakuwa N., and Oda Y. Purification of the extracellular pectinolytic enzyme from the fungus Rhizopus oryzae NBRC 4707. Microbiol Res 159 (2004) 83-86
    • (2004) Microbiol Res , vol.159 , pp. 83-86
    • Saito, K.1    Takakuwa, N.2    Oda, Y.3
  • 8
    • 0036171217 scopus 로고    scopus 로고
    • Solid-state production of thermostable pectinases from thermophilic Thermoascus aurantiacus
    • Martins E.S., Silva D., Da Silva R., and Gomes E. Solid-state production of thermostable pectinases from thermophilic Thermoascus aurantiacus. Process Biochem 37 (2002) 949-954
    • (2002) Process Biochem , vol.37 , pp. 949-954
    • Martins, E.S.1    Silva, D.2    Da Silva, R.3    Gomes, E.4
  • 9
    • 0042733746 scopus 로고    scopus 로고
    • Influence of the carbon source on production of cellulases, hemicellulases and pectinases by Trichoderma reesei Rut C-30
    • Olsson L., Christensen T.M.I.E., Hansen K.P., and Palmovist E.A. Influence of the carbon source on production of cellulases, hemicellulases and pectinases by Trichoderma reesei Rut C-30. Enzyme Microbiol Technol 33 (2003) 612-619
    • (2003) Enzyme Microbiol Technol , vol.33 , pp. 612-619
    • Olsson, L.1    Christensen, T.M.I.E.2    Hansen, K.P.3    Palmovist, E.A.4
  • 10
    • 22544467018 scopus 로고    scopus 로고
    • Microbial pectinolytic enzymes: a review
    • Jayani R.S., Saxena S., and Gupta R. Microbial pectinolytic enzymes: a review. Process Biochem 40 (2005) 2931-2944
    • (2005) Process Biochem , vol.40 , pp. 2931-2944
    • Jayani, R.S.1    Saxena, S.2    Gupta, R.3
  • 11
    • 15744384627 scopus 로고    scopus 로고
    • Production of pectinase by solid-state fermentation with Penicillium viridicatum RFC3
    • Silva D., Tokuioshi K., Martins E.S., Da Silva R., and Gomes E. Production of pectinase by solid-state fermentation with Penicillium viridicatum RFC3. Process Biochem 40 (2005) 2885-2889
    • (2005) Process Biochem , vol.40 , pp. 2885-2889
    • Silva, D.1    Tokuioshi, K.2    Martins, E.S.3    Da Silva, R.4    Gomes, E.5
  • 12
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugars
    • Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugars. Anal Chem 31 (1959) 426-428
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 14
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 33748769291 scopus 로고    scopus 로고
    • Why solid-state fermentation seems to be resistant to catabolite repression?
    • Viniegra-González G., and Favela-Torres E. Why solid-state fermentation seems to be resistant to catabolite repression?. Food Tecnol Biotechnol 44 (2006) 397-406
    • (2006) Food Tecnol Biotechnol , vol.44 , pp. 397-406
    • Viniegra-González, G.1    Favela-Torres, E.2
  • 17
    • 0142226991 scopus 로고    scopus 로고
    • Ambient pH controls the expression of endopolygalacturonase genes in the necrotrophic fungus Sclerotinia sclerotium
    • Cotton P., Kasza Z., Bruel C., Rascle C., and Févre M. Ambient pH controls the expression of endopolygalacturonase genes in the necrotrophic fungus Sclerotinia sclerotium. FEMS Microbiol Lett 227 (2003) 163-169
    • (2003) FEMS Microbiol Lett , vol.227 , pp. 163-169
    • Cotton, P.1    Kasza, Z.2    Bruel, C.3    Rascle, C.4    Févre, M.5
  • 18
    • 0029110882 scopus 로고
    • Sequential production of pectinases by Penicillium frequentans
    • Fonseca M.J.V., and Said S. Sequential production of pectinases by Penicillium frequentans. World J Microbiol Biotechnol 11 (1995) 174-177
    • (1995) World J Microbiol Biotechnol , vol.11 , pp. 174-177
    • Fonseca, M.J.V.1    Said, S.2
  • 19
    • 0036221202 scopus 로고    scopus 로고
    • Production, purification and characterization of a polygalacturonase from a new strain of Kluyveromyces marxianus isolated from coffee wet-processing wastewater
    • Serrat M., Bermudez R.C., and Villa T.G. Production, purification and characterization of a polygalacturonase from a new strain of Kluyveromyces marxianus isolated from coffee wet-processing wastewater. Appl Biochem Biotechnol 97 (2002) 193-208
    • (2002) Appl Biochem Biotechnol , vol.97 , pp. 193-208
    • Serrat, M.1    Bermudez, R.C.2    Villa, T.G.3
  • 20
    • 0036196525 scopus 로고    scopus 로고
    • Purification and partial characterization of exopolygalacturonase I from Penicillium frequentans
    • Chellegatti M.A.S.C., Fonseca M.J.V., and Said S. Purification and partial characterization of exopolygalacturonase I from Penicillium frequentans. Microbiol Res 157 (2002) 19-24
    • (2002) Microbiol Res , vol.157 , pp. 19-24
    • Chellegatti, M.A.S.C.1    Fonseca, M.J.V.2    Said, S.3
  • 21
    • 0034011112 scopus 로고    scopus 로고
    • Perspectives in the biological function and the technological application of polygalacturonases
    • Lang C., and Dörnenburg H. Perspectives in the biological function and the technological application of polygalacturonases. Appl Microbiol Biotechnol 53 (2000) 366-375
    • (2000) Appl Microbiol Biotechnol , vol.53 , pp. 366-375
    • Lang, C.1    Dörnenburg, H.2
  • 22
    • 0037899941 scopus 로고    scopus 로고
    • Purification and biochemical properties of microbial pectinases- a review
    • Panda T., and Gummadi N. Purification and biochemical properties of microbial pectinases- a review. Process Biochem 38 (2003) 987-996
    • (2003) Process Biochem , vol.38 , pp. 987-996
    • Panda, T.1    Gummadi, N.2
  • 23
    • 0025514206 scopus 로고
    • Endopolygalacturonase production from Kluyveromyces marxianus. I. Resolution, purification and partial characterization of the enzyme
    • Barnby F.M., Morpeth F.F., and Pyle D.L. Endopolygalacturonase production from Kluyveromyces marxianus. I. Resolution, purification and partial characterization of the enzyme. Enzyme Microbiol Technol 12 (1990) 891-897
    • (1990) Enzyme Microbiol Technol , vol.12 , pp. 891-897
    • Barnby, F.M.1    Morpeth, F.F.2    Pyle, D.L.3
  • 24
    • 0030561473 scopus 로고    scopus 로고
    • Purification and characterization of an exo-polygalacturonase from the tomato vascular wilt pathogen Fusarium oxysporum f.sp. lycopersici
    • Pietro A.D., and Roncero M.I.G. Purification and characterization of an exo-polygalacturonase from the tomato vascular wilt pathogen Fusarium oxysporum f.sp. lycopersici. FEMS Microbiol Lett 145 (1996) 295-298
    • (1996) FEMS Microbiol Lett , vol.145 , pp. 295-298
    • Pietro, A.D.1    Roncero, M.I.G.2
  • 25
    • 0000907195 scopus 로고
    • Partial purification of polygalacturonase produced by solid-state cultures of Aspergillus niger 3T5B
    • Coelho M.A.Z., Medronho R.A., Leite S.G.F., and Couri S. Partial purification of polygalacturonase produced by solid-state cultures of Aspergillus niger 3T5B. Rev Microbiol 26 (1995) 318-322
    • (1995) Rev Microbiol , vol.26 , pp. 318-322
    • Coelho, M.A.Z.1    Medronho, R.A.2    Leite, S.G.F.3    Couri, S.4
  • 26
    • 24144469142 scopus 로고    scopus 로고
    • The contribution of ionic interactions to the conformational stability and function of polygalacturonase from A. niger
    • Jyothi T.C., Singh S.A., and Rao A.G.A. The contribution of ionic interactions to the conformational stability and function of polygalacturonase from A. niger. Intern J Biol Macromol 36 (2005) 310-317
    • (2005) Intern J Biol Macromol , vol.36 , pp. 310-317
    • Jyothi, T.C.1    Singh, S.A.2    Rao, A.G.A.3
  • 27
    • 33947263665 scopus 로고    scopus 로고
    • Purification and characterization of polygalacturonase produced by thermophilic Thermoascus aurantiacus CBMAI-756 in submerged fermentation
    • Martins E.S., Leite R.S., Silva D., Da Silva R., and Gomes E. Purification and characterization of polygalacturonase produced by thermophilic Thermoascus aurantiacus CBMAI-756 in submerged fermentation. Antonie Leew 91 (2007) 291-299
    • (2007) Antonie Leew , vol.91 , pp. 291-299
    • Martins, E.S.1    Leite, R.S.2    Silva, D.3    Da Silva, R.4    Gomes, E.5
  • 29
    • 0030044882 scopus 로고    scopus 로고
    • Fractionation, purification, and preliminary characterization of polygalacturonases produced by Aspergillus carbonarius
    • Devi N.A., and Rao A.G.A. Fractionation, purification, and preliminary characterization of polygalacturonases produced by Aspergillus carbonarius. Enzyme Microbiol Technol 18 (1996) 59-65
    • (1996) Enzyme Microbiol Technol , vol.18 , pp. 59-65
    • Devi, N.A.1    Rao, A.G.A.2
  • 31
    • 12844268316 scopus 로고    scopus 로고
    • Effect of chemical modification of histidines on the copper-induced oligomerization of jack bean urease (EC 3.5.1.5)
    • Follmer C., and Carlini C.R. Effect of chemical modification of histidines on the copper-induced oligomerization of jack bean urease (EC 3.5.1.5). Arch Biochem Biophys 435 (2005) 15-20
    • (2005) Arch Biochem Biophys , vol.435 , pp. 15-20
    • Follmer, C.1    Carlini, C.R.2
  • 32
    • 14744297808 scopus 로고    scopus 로고
    • The influence of salts and temperature on enzymatic activity of microbial trensglutaminase
    • Kütemeyer C., Froeck M., Werlein H.D., and Watkinson B.M. The influence of salts and temperature on enzymatic activity of microbial trensglutaminase. Food Control 16 (2005) 735-737
    • (2005) Food Control , vol.16 , pp. 735-737
    • Kütemeyer, C.1    Froeck, M.2    Werlein, H.D.3    Watkinson, B.M.4
  • 33
    • 13844271823 scopus 로고    scopus 로고
    • A thermodynamic study of mesophilic, thermophilic, and hyperthermophilic l-arabinose isomerases: The effects of divalent metal ions on protein stability at alevated temperature
    • Lee D.-W., Hong Y-OH, Choe E.-A., Lee S.-J., Kim S-b, Lee H.-S., et al. A thermodynamic study of mesophilic, thermophilic, and hyperthermophilic l-arabinose isomerases: The effects of divalent metal ions on protein stability at alevated temperature. FEBS Lett 579 (2005) 1261-1266
    • (2005) FEBS Lett , vol.579 , pp. 1261-1266
    • Lee, D.-W.1    Hong Y-OH2    Choe, E.-A.3    Lee, S.-J.4    Kim S-b5    Lee, H.-S.6
  • 34
    • 27944487490 scopus 로고    scopus 로고
    • Effect of ions and other compatible solutes on enzyme activity, and its implication for biocatalysis using ionic liquids
    • Zhao H. Effect of ions and other compatible solutes on enzyme activity, and its implication for biocatalysis using ionic liquids. J Mol Catal B: Enzyme 37 (2005) 16-25
    • (2005) J Mol Catal B: Enzyme , vol.37 , pp. 16-25
    • Zhao, H.1
  • 35
    • 27644565163 scopus 로고    scopus 로고
    • Hofmeister specific-ion effects on enzyme activity and buffer pH: horseradish peroxidase in citrate buffer
    • Bauduim P., Nohmie F., Touraud D., Neueder R., Kunz W., and Ninham B.W. Hofmeister specific-ion effects on enzyme activity and buffer pH: horseradish peroxidase in citrate buffer. J Mol Liq 123 (2006) 14-19
    • (2006) J Mol Liq , vol.123 , pp. 14-19
    • Bauduim, P.1    Nohmie, F.2    Touraud, D.3    Neueder, R.4    Kunz, W.5    Ninham, B.W.6
  • 36
    • 0036208545 scopus 로고    scopus 로고
    • A simple fractionation protocol for, and a comprehensive study of the molecular properties of two major endopolygalacturonases from Aspergillus niger
    • Singh S.A., and Rao A.G.A. A simple fractionation protocol for, and a comprehensive study of the molecular properties of two major endopolygalacturonases from Aspergillus niger. Biotechnol Appl Biochem 35 (2002) 115-123
    • (2002) Biotechnol Appl Biochem , vol.35 , pp. 115-123
    • Singh, S.A.1    Rao, A.G.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.