메뉴 건너뛰기




Volumn 123, Issue 1, 2006, Pages 33-42

Purification and characterization of a novel pectinase from Acrophialophora nainiana with emphasis on its physicochemical properties

Author keywords

Acrophialophora nainiana; Pectin; Pectinase; Thermostability

Indexed keywords

CHARACTERIZATION; FILTRATION; FUNGI; GELS; MASS SPECTROMETRY; PURIFICATION;

EID: 33646028781     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2005.10.024     Document Type: Article
Times cited : (59)

References (33)
  • 1
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrilamide gels
    • Blum H., Beier H., and Gross B. Improved silver staining of plant proteins, RNA and DNA in polyacrilamide gels. Electrophoresis 8 (1987) 93-99
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, B.3
  • 2
    • 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
  • 3
    • 0038095190 scopus 로고    scopus 로고
    • Purification and characterization of a novel cellulase-free xylanase from Acrophialophora nainiana
    • Cardoso O.A., and Filho E.X.F. Purification and characterization of a novel cellulase-free xylanase from Acrophialophora nainiana. FEMS Microbiol. Lett. 223 (2003) 309-314
    • (2003) FEMS Microbiol. Lett. , vol.223 , pp. 309-314
    • Cardoso, O.A.1    Filho, E.X.F.2
  • 4
    • 0027190626 scopus 로고    scopus 로고
    • An interactive graphic program for calculating the secondary structures content of proteins from circular dichroism spectrum
    • Deléage G., and Geourjon C. An interactive graphic program for calculating the secondary structures content of proteins from circular dichroism spectrum. Comp. Appl. Biosc. 9 (1999) 197-199
    • (1999) Comp. Appl. Biosc. , vol.9 , pp. 197-199
    • Deléage, G.1    Geourjon, C.2
  • 5
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substrates
    • Dubois M., Gilles K., Hamilton J.K., Rebers P.A., and Smith F. Colorimetric method for determination of sugars and related substrates. Anal. Chem. 28 (1956) 350-356
    • (1956) Anal. Chem. , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 6
    • 1942424126 scopus 로고    scopus 로고
    • Purification and partial characterisation of an acidic polygalacturonase from Aspergillus kawachii
    • Esquivel J.C., and Vogel C.E. Purification and partial characterisation of an acidic polygalacturonase from Aspergillus kawachii. J. Biotechnol. 110 (2004) 21-28
    • (2004) J. Biotechnol. , vol.110 , pp. 21-28
    • Esquivel, J.C.1    Vogel, C.E.2
  • 7
    • 3142741043 scopus 로고    scopus 로고
    • Purification and characterization of a β-mannanase from Trichoderma harzianum strain T4
    • Ferreira H.M., and Filho E.X.F. Purification and characterization of a β-mannanase from Trichoderma harzianum strain T4. Carbohydr. Polym. 57 (2004) 23-29
    • (2004) Carbohydr. Polym. , vol.57 , pp. 23-29
    • Ferreira, H.M.1    Filho, E.X.F.2
  • 8
    • 0027595156 scopus 로고
    • Biochemical characterisitics of two endo-β-1,4-xylanases produced by Penicillium capsulatum
    • Filho E.X.F., Puls J., and Coughlan M.P. Biochemical characterisitics of two endo-β-1,4-xylanases produced by Penicillium capsulatum. J. Ind. Microbiol. 11 (1993) 171-180
    • (1993) J. Ind. Microbiol. , vol.11 , pp. 171-180
    • Filho, E.X.F.1    Puls, J.2    Coughlan, M.P.3
  • 9
    • 0032079528 scopus 로고    scopus 로고
    • Improving the recovery of lysine in automated protein sequencing
    • Fontes W., Cunha R.B., Sousa M.V., and Morhy L. Improving the recovery of lysine in automated protein sequencing. Anal. Biochem. 258 (1998) 259-267
    • (1998) Anal. Biochem. , vol.258 , pp. 259-267
    • Fontes, W.1    Cunha, R.B.2    Sousa, M.V.3    Morhy, L.4
  • 10
    • 0347297442 scopus 로고    scopus 로고
    • Purification, characterisation and mode of action of an endopolygalacturonase from the psychrophilic fungus Mucor flavus
    • Gadre R.V., Driessche G.V., Beeumen J.V., and Bhat M.K. Purification, characterisation and mode of action of an endopolygalacturonase from the psychrophilic fungus Mucor flavus. Enzyme Microb. Technol. 32 (2003) 321-330
    • (2003) Enzyme Microb. Technol. , vol.32 , pp. 321-330
    • Gadre, R.V.1    Driessche, G.V.2    Beeumen, J.V.3    Bhat, M.K.4
  • 11
    • 0037899941 scopus 로고    scopus 로고
    • Purification and biochemical properties of microbial pectinases-a review
    • Gummadi S.N., and Panda T. Purification and biochemical properties of microbial pectinases-a review. Process Biochem. 38 (2003) 987-996
    • (2003) Process Biochem. , vol.38 , pp. 987-996
    • Gummadi, S.N.1    Panda, T.2
  • 12
    • 0033927724 scopus 로고    scopus 로고
    • Production, purification and characterization of pectinase from a Bacillus sp. DT7
    • Kashyap D.R., Chandra S., Kaul A., and Tewari R. Production, purification and characterization of pectinase from a Bacillus sp. DT7. World J. Microbiol. Biotechnol. 16 (2000) 277-282
    • (2000) World J. Microbiol. Biotechnol. , vol.16 , pp. 277-282
    • Kashyap, D.R.1    Chandra, S.2    Kaul, A.3    Tewari, R.4
  • 13
    • 0035191237 scopus 로고    scopus 로고
    • Applications of pectinases in the commercial sector: a review
    • Kashyap D.R., Vohra P.K., Chopra S., and Tewari R. Applications of pectinases in the commercial sector: a review. Biores. Technol. 77 (2001) 215-227
    • (2001) Biores. Technol. , vol.77 , pp. 215-227
    • Kashyap, D.R.1    Vohra, P.K.2    Chopra, S.3    Tewari, R.4
  • 14
    • 2942615497 scopus 로고    scopus 로고
    • Production, characterization and application of a thermostable polygalacturonase of a thermophilic mould Sporotrichum thermophile Apinis
    • Kaur G., Kumar S., and Satyanarayana T. Production, characterization and application of a thermostable polygalacturonase of a thermophilic mould Sporotrichum thermophile Apinis. Biores. Technol. 94 (2004) 239-243
    • (2004) Biores. Technol. , vol.94 , pp. 239-243
    • Kaur, G.1    Kumar, S.2    Satyanarayana, T.3
  • 15
    • 0035811977 scopus 로고    scopus 로고
    • Purification and properties of a high molecular-weight, alkaline exopolygalacturonase from a strain of Bacillus
    • Kobayashi T., Higaki N., Suzumatsu A., Sawada K., Hagihara H., Kawai S., and Ito S. Purification and properties of a high molecular-weight, alkaline exopolygalacturonase from a strain of Bacillus. Enzyme Microb. Technol. 29 (2001) 70-75
    • (2001) Enzyme Microb. Technol. , vol.29 , pp. 70-75
    • Kobayashi, T.1    Higaki, N.2    Suzumatsu, A.3    Sawada, K.4    Hagihara, H.5    Kawai, S.6    Ito, S.7
  • 16
    • 0038333434 scopus 로고    scopus 로고
    • Maximal stabilities of reversible two-state proteins
    • Kumar S., Tsai C.J., and Nussinov R. Maximal stabilities of reversible two-state proteins. Biochemistry 42 (2003) 4864-4873
    • (2003) Biochemistry , vol.42 , pp. 4864-4873
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly ot he head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly ot he head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 33747333106 scopus 로고
    • Use of dinitrosalycilic acid reagent for determination of reducing sugar
    • Miller G.L. Use of dinitrosalycilic acid reagent for determination of reducing sugar. Anal. Chem. 31 (1959) 426-428
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 21
    • 2042505067 scopus 로고    scopus 로고
    • Isolation and characterization of psychrophilic yeasts producing cold-adapted pectinolytic enzymes
    • Nakagawa T., Nagaoka T., Taniguchi S., Miyaji T., and Tomizuka N. Isolation and characterization of psychrophilic yeasts producing cold-adapted pectinolytic enzymes. Lett. Appl. Microbiol. 38 (2004) 383-387
    • (2004) Lett. Appl. Microbiol. , vol.38 , pp. 383-387
    • Nakagawa, T.1    Nagaoka, T.2    Taniguchi, S.3    Miyaji, T.4    Tomizuka, N.5
  • 22
    • 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 Palmqvist E.A. Influence of the carbon source on production of cellulases, hemicellulases and pectinases by Trichoderma reesei Rut C-30. Enzyme Microb. Technol. 33 (2003) 612-619
    • (2003) Enzyme Microb. Technol. , vol.33 , pp. 612-619
    • Olsson, L.1    Christensen, T.M.I.E.2    Hansen, K.P.3    Palmqvist, E.A.4
  • 23
    • 0025019350 scopus 로고
    • Conformational stability of globular proteins
    • Pace C.N. Conformational stability of globular proteins. Trends Biochem Sci. 15 (1990) 14-17
    • (1990) Trends Biochem Sci. , vol.15 , pp. 14-17
    • Pace, C.N.1
  • 24
    • 0038021209 scopus 로고    scopus 로고
    • Cloning expression and characterisation of a thermostable exopolygalacturonase from Thermotoga maritima
    • Parisot J., Langlois V., Sakanyan V., and Rabiller C. Cloning expression and characterisation of a thermostable exopolygalacturonase from Thermotoga maritima. Carbohydr. Res. 338 (2003) 1333-1337
    • (2003) Carbohydr. Res. , vol.338 , pp. 1333-1337
    • Parisot, J.1    Langlois, V.2    Sakanyan, V.3    Rabiller, C.4
  • 25
    • 0034717177 scopus 로고    scopus 로고
    • Purification and characterization of polygalacturonase from banana fruit
    • Pathak N., Mishra S., and Sanwal G.G. Purification and characterization of polygalacturonase from banana fruit. Phytochemistry 54 (2000) 147-152
    • (2000) Phytochemistry , vol.54 , pp. 147-152
    • Pathak, N.1    Mishra, S.2    Sanwal, G.G.3
  • 26
    • 9144273061 scopus 로고    scopus 로고
    • Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species
    • Rey M.W., Ramaiya P., Nelson B.A., et al. Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species. Genome Biol. 5 10 (2004) R77
    • (2004) Genome Biol. , vol.5 , Issue.10
    • Rey, M.W.1    Ramaiya, P.2    Nelson, B.A.3
  • 27
    • 0034714124 scopus 로고    scopus 로고
    • Purification and characterization of a new xylanase from Acrophialophora nainiana
    • Salles B.C., Cunha R.B., Fontes W., Sousa M.V., and Filho E.X.F. Purification and characterization of a new xylanase from Acrophialophora nainiana. J. Biotechnol. 81 (2000) 199-204
    • (2000) J. Biotechnol. , vol.81 , pp. 199-204
    • Salles, B.C.1    Cunha, R.B.2    Fontes, W.3    Sousa, M.V.4    Filho, E.X.F.5
  • 28
    • 4444325886 scopus 로고    scopus 로고
    • Effect of cellulase-free xylanases from Acrophialophora nainiana and Humicola grisea var. thermoidea on eucalyptus kraft pulp
    • Salles B.C., Medeiros R.G., Báo S.N., Silva Jr. F.G., and Filho E.X.F. Effect of cellulase-free xylanases from Acrophialophora nainiana and Humicola grisea var. thermoidea on eucalyptus kraft pulp. Process Biochem. 40 (2005) 343-349
    • (2005) Process Biochem. , vol.40 , pp. 343-349
    • Salles, B.C.1    Medeiros, R.G.2    Báo, S.N.3    Silva Jr., F.G.4    Filho, E.X.F.5
  • 29
    • 0032988009 scopus 로고    scopus 로고
    • The exopolygalacturonase lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937
    • Shevchik V.E., Condemine G., Robert-Baudoy J., and Hugouvieux-Cotte-Pattat N. The exopolygalacturonase lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937. J. Bacteriol. 181 (1999) 3912-3919
    • (1999) J. Bacteriol. , vol.181 , pp. 3912-3919
    • Shevchik, V.E.1    Condemine, G.2    Robert-Baudoy, J.3    Hugouvieux-Cotte-Pattat, N.4
  • 30
    • 0037161811 scopus 로고    scopus 로고
    • Comparison of the genomes of two Xanthomonas pathogens with differing host specificities
    • Silva A.C.R., Ferro J.A., Reinach F.C., et al. Comparison of the genomes of two Xanthomonas pathogens with differing host specificities. Nature 417 6887 (2002) 459-463
    • (2002) Nature , vol.417 , Issue.6887 , pp. 459-463
    • Silva, A.C.R.1    Ferro, J.A.2    Reinach, F.C.3
  • 31
    • 0035014021 scopus 로고    scopus 로고
    • Pectinolytic enzyme production by Bacillus species and their potential application on juice extraction
    • Soares M.M.C.N., Da Silva R., Carmona E.C., and Gomes E. Pectinolytic enzyme production by Bacillus species and their potential application on juice extraction. World J. Microbiol. Biotechnol. 17 (2001) 79-82
    • (2001) World J. Microbiol. Biotechnol. , vol.17 , pp. 79-82
    • Soares, M.M.C.N.1    Da Silva, R.2    Carmona, E.C.3    Gomes, E.4
  • 32
    • 0037413382 scopus 로고    scopus 로고
    • A specific method for determination of pectin esterase in blood oranges
    • Spagna G., Barbagallo R.N., and Ingallinera B. A specific method for determination of pectin esterase in blood oranges. Enzyme Microb. Technol. 32 (2003) 174-177
    • (2003) Enzyme Microb. Technol. , vol.32 , pp. 174-177
    • Spagna, G.1    Barbagallo, R.N.2    Ingallinera, B.3
  • 33
    • 0142043937 scopus 로고    scopus 로고
    • Cloning and expression of a pectate lyase gene from Bacillus alcalophillus NTT33
    • Zhai C., Cao J., and Wang Y. Cloning and expression of a pectate lyase gene from Bacillus alcalophillus NTT33. Enzyme Microb. Technol. 33 (2003) 173-178
    • (2003) Enzyme Microb. Technol. , vol.33 , pp. 173-178
    • Zhai, C.1    Cao, J.2    Wang, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.