메뉴 건너뛰기




Volumn 45, Issue 12, 2008, Pages 1616-1624

Identification, biochemical characterization, and evolution of the Rhizopus oryzae 99-880 polygalacturonase gene family

Author keywords

Family 28 glycosyl hydrolase; Pichia pastoris; Polygalacturonase; Recombinant protein expression; Rhizopus oryzae

Indexed keywords

COMPLEMENTARY DNA;

EID: 56249140422     PISSN: 10871845     EISSN: 10960937     Source Type: Journal    
DOI: 10.1016/j.fgb.2008.09.009     Document Type: Article
Times cited : (21)

References (50)
  • 1
    • 34247253077 scopus 로고    scopus 로고
    • The structural basis for exopolygalacturonase activity in a family 28 glycoside hydrolase
    • Abbott D.W., and Boraston A.B. The structural basis for exopolygalacturonase activity in a family 28 glycoside hydrolase. J. Mol. Biol. 268 (2007) 1215-1222
    • (2007) J. Mol. Biol. , vol.268 , pp. 1215-1222
    • Abbott, D.W.1    Boraston, A.B.2
  • 2
    • 2442593127 scopus 로고    scopus 로고
    • rDNA ITS sequence of Rhizopus oryzae: its application to classification and identification of lactic acid producers
    • Abe A., Sone T., Sujaya I.N., Saito K., Asano K., and Tomita F. rDNA ITS sequence of Rhizopus oryzae: its application to classification and identification of lactic acid producers. Biosci. Biotechnol. Biochem. 67 (2003) 1725-1731
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 1725-1731
    • Abe, A.1    Sone, T.2    Sujaya, I.N.3    Saito, K.4    Asano, K.5    Tomita, F.6
  • 4
    • 0025018051 scopus 로고
    • Molecular cloning, nucleotide sequence and expression of the gene encoding prepro-polygalacturonaseII of Aspergillus niger
    • Bussink H.J., Kester H.C., and Visser J. Molecular cloning, nucleotide sequence and expression of the gene encoding prepro-polygalacturonaseII of Aspergillus niger. FEBS Lett. 273 (1990) 127-130
    • (1990) FEBS Lett. , vol.273 , pp. 127-130
    • Bussink, H.J.1    Kester, H.C.2    Visser, J.3
  • 5
    • 0025908645 scopus 로고
    • Identification and characterization of a second polygalacturonase gene of Aspergillus niger
    • Bussink H.J.D., Brouwer K.B., de Graaff L.H., Kester H.C.M., and Visser J. Identification and characterization of a second polygalacturonase gene of Aspergillus niger. Curr. Genet. 20 (1991) 301-307
    • (1991) Curr. Genet. , vol.20 , pp. 301-307
    • Bussink, H.J.D.1    Brouwer, K.B.2    de Graaff, L.H.3    Kester, H.C.M.4    Visser, J.5
  • 6
    • 0026646374 scopus 로고
    • The polygalacturonases of Aspergillus niger are encoded by a family of diverged genes
    • Bussink H.J.D., Buxton F.P., Fraaye B.A., de Graaff L.H., and Visser J. The polygalacturonases of Aspergillus niger are encoded by a family of diverged genes. Eur. J. Biochem. 208 (1992) 83-90
    • (1992) Eur. J. Biochem. , vol.208 , pp. 83-90
    • Bussink, H.J.D.1    Buxton, F.P.2    Fraaye, B.A.3    de Graaff, L.H.4    Visser, J.5
  • 7
    • 56249142361 scopus 로고    scopus 로고
    • Purification and characterization of two isozymes of polygalacturonase from Botrytis cinerea
    • Cabanne C., and Doneche B. Purification and characterization of two isozymes of polygalacturonase from Botrytis cinerea. Microbiol. Res. 16 (2002) 1183-1195
    • (2002) Microbiol. Res. , vol.16 , pp. 1183-1195
    • Cabanne, C.1    Doneche, B.2
  • 8
    • 0035943418 scopus 로고    scopus 로고
    • The X-ray structure of Aspergillus aculeatus polygalacturonase and a modeled structure of the polygalacturonase-octagalacturonate complex
    • Cho S.W., Lee S., and Shin W. The X-ray structure of Aspergillus aculeatus polygalacturonase and a modeled structure of the polygalacturonase-octagalacturonate complex. J. Mol. Biol. 314 (2001) 863-878
    • (2001) J. Mol. Biol. , vol.314 , pp. 863-878
    • Cho, S.W.1    Lee, S.2    Shin, W.3
  • 9
    • 0035199524 scopus 로고    scopus 로고
    • Aspergillus enzymes involved in degradation of plant cell wall polysaccharides. Microbiol
    • de Vries R.P., and Visser J. Aspergillus enzymes involved in degradation of plant cell wall polysaccharides. Microbiol. Mol. Biol. Rev. 65 (2001) 497-522
    • (2001) Mol. Biol. Rev. , vol.65 , pp. 497-522
    • de Vries, R.P.1    Visser, J.2
  • 10
    • 0030734575 scopus 로고    scopus 로고
    • A simple method for estimating the parameter of substitution rate variation among sites
    • Gu X., and Zhang J. A simple method for estimating the parameter of substitution rate variation among sites. Mol. Biol. Evol. 14 (1997) 1106-1113
    • (1997) Mol. Biol. Evol. , vol.14 , pp. 1106-1113
    • Gu, X.1    Zhang, J.2
  • 11
    • 0015108154 scopus 로고
    • Improved solid medium for the detection and enumeration of pectinolytic bacteria
    • Hankin L., Zucker M., and Sands D.C. Improved solid medium for the detection and enumeration of pectinolytic bacteria. Appl. Microbiol. 22 (1971) 205-209
    • (1971) Appl. Microbiol. , vol.22 , pp. 205-209
    • Hankin, L.1    Zucker, M.2    Sands, D.C.3
  • 12
    • 0032995005 scopus 로고    scopus 로고
    • Production of highly efficient enzymes for flax retting by Rhizomucor pusillus
    • Henriksson G., Akin D.E., Slomczynski D., and Eriksson K.-E.L. Production of highly efficient enzymes for flax retting by Rhizomucor pusillus. J. Biotechnol. 68 (1999) 115-123
    • (1999) J. Biotechnol. , vol.68 , pp. 115-123
    • Henriksson, G.1    Akin, D.E.2    Slomczynski, D.3    Eriksson, K.-E.L.4
  • 13
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycosyl hydrolases
    • Henrissat B., and Davies G. Structural and sequence-based classification of glycosyl hydrolases. Curr. Opin. Struct. Biol. 7 (1997) 637-644
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 14
    • 0025367467 scopus 로고
    • DNA sequence analysis of pglA and mechanism of export of its polygalacturonase product from Pseudomonas solanacearum
    • Huang J.H., and Schell M.A. DNA sequence analysis of pglA and mechanism of export of its polygalacturonase product from Pseudomonas solanacearum. J. Bacteriol. 172 (1990) 3879-3887
    • (1990) J. Bacteriol. , vol.172 , pp. 3879-3887
    • Huang, J.H.1    Schell, M.A.2
  • 15
    • 0030725162 scopus 로고    scopus 로고
    • An exo-poly-α-d-galacturonosidase, PehB, is required for wild-type virulence of Ralstonia solanacearum
    • Huang Q., and Allen C. An exo-poly-α-d-galacturonosidase, PehB, is required for wild-type virulence of Ralstonia solanacearum. J. Bacteriol. 179 (1997) 7369-7378
    • (1997) J. Bacteriol. , vol.179 , pp. 7369-7378
    • Huang, Q.1    Allen, C.2
  • 16
    • 0034849408 scopus 로고    scopus 로고
    • MRBAYES: Bayesian inference of phylogenetic trees
    • Huelsenbeck J.P., and Ronquist F. MRBAYES: Bayesian inference of phylogenetic trees. Bioinformatics 17 (2001) 754-755
    • (2001) Bioinformatics , vol.17 , pp. 754-755
    • Huelsenbeck, J.P.1    Ronquist, F.2
  • 17
    • 0031710490 scopus 로고    scopus 로고
    • Regulation of the glucoamylase-encoding gene (glaB), expressed in solid-state culture (Koji) of Aspergillus oryzae
    • Ishida H., Hata Y., Ichikawa E., Kawato A., Suginami K., and Imayasu S. Regulation of the glucoamylase-encoding gene (glaB), expressed in solid-state culture (Koji) of Aspergillus oryzae. J. Ferm. Bioeng. 86 (1998) 301-307
    • (1998) J. Ferm. Bioeng. , vol.86 , pp. 301-307
    • Ishida, H.1    Hata, Y.2    Ichikawa, E.3    Kawato, A.4    Suginami, K.5    Imayasu, S.6
  • 18
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones D.T., Taylor W.R., and Thornton J.M. The rapid generation of mutation data matrices from protein sequences. Comput. Appl. Biosci. 8 (1992) 275-282
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 19
    • 22544465583 scopus 로고    scopus 로고
    • Necrotizing activity of five Botrytis cinerea endopolygalacturonases produced in Pichia pastoris
    • Kars I., Krooshof G.H., Wagemakers L., Joosten R., Benen J.A.E., and van Kan J.A.L. Necrotizing activity of five Botrytis cinerea endopolygalacturonases produced in Pichia pastoris. Plant J. 43 (2005) 213-225
    • (2005) Plant J. , vol.43 , pp. 213-225
    • Kars, I.1    Krooshof, G.H.2    Wagemakers, L.3    Joosten, R.4    Benen, J.A.E.5    van Kan, J.A.L.6
  • 20
    • 0025361857 scopus 로고
    • Purification and characterization of polygalacturonases produced by the hyphal fungus Aspergillus niger
    • Kester H.C.M., and Visser J. Purification and characterization of polygalacturonases produced by the hyphal fungus Aspergillus niger. Biotechnol. Appl. Biochem. 12 (1990) 150-160
    • (1990) Biotechnol. Appl. Biochem. , vol.12 , pp. 150-160
    • Kester, H.C.M.1    Visser, J.2
  • 21
    • 0029778186 scopus 로고    scopus 로고
    • Primary structure and characterization of an exopolygalacturonase from Aspergillus tubingensis
    • Kester H.C.M., Kusters-van Someren M.A., Muller Y., and Visser J. Primary structure and characterization of an exopolygalacturonase from Aspergillus tubingensis. Eur. J. Biochem. 240 (1996) 738-746
    • (1996) Eur. J. Biochem. , vol.240 , pp. 738-746
    • Kester, H.C.M.1    Kusters-van Someren, M.A.2    Muller, Y.3    Visser, J.4
  • 22
    • 0021919480 scopus 로고
    • Rapid and sensitive protein similarity searches
    • Lipman D.J., and Pearson W.R. Rapid and sensitive protein similarity searches. Science 227 (1985) 1435-1441
    • (1985) Science , vol.227 , pp. 1435-1441
    • Lipman, D.J.1    Pearson, W.R.2
  • 24
    • 0035188524 scopus 로고    scopus 로고
    • Pectin degrading glycoside hydrolases of family 28: sequence-structural features specificities and evolution
    • Markovič O., and Janaček S. Pectin degrading glycoside hydrolases of family 28: sequence-structural features specificities and evolution. Prot. Eng. 14 (2001) 615-631
    • (2001) Prot. Eng. , vol.14 , pp. 615-631
    • Markovič, O.1    Janaček, S.2
  • 25
    • 33745824211 scopus 로고    scopus 로고
    • Plasmids for expression of heterologous proteins in Rhizopus oryzae
    • Mertens J.A., Skory C.D., and Ibraham A.S. Plasmids for expression of heterologous proteins in Rhizopus oryzae. Arch. Microbiol. 186 (2006) 41-50
    • (2006) Arch. Microbiol. , vol.186 , pp. 41-50
    • Mertens, J.A.1    Skory, C.D.2    Ibraham, A.S.3
  • 26
    • 33847287213 scopus 로고    scopus 로고
    • Isolation and characterization of a second glucoamylase gene without a starch binding domain from Rhizopus oryzae
    • Mertens J.A., and Skory C.D. Isolation and characterization of a second glucoamylase gene without a starch binding domain from Rhizopus oryzae. Enzyme Microbiol. Technol. 40 (2007) 874-880
    • (2007) Enzyme Microbiol. Technol. , vol.40 , pp. 874-880
    • Mertens, J.A.1    Skory, C.D.2
  • 27
    • 38349084993 scopus 로고    scopus 로고
    • Comparitive biochemical and structural characterizations of fungal polygalacturonases
    • Niture S.K. Comparitive biochemical and structural characterizations of fungal polygalacturonases. Biologia 63 (2008) 1-19
    • (2008) Biologia , vol.63 , pp. 1-19
    • Niture, S.K.1
  • 28
    • 0034703098 scopus 로고    scopus 로고
    • Subsite mapping of Aspergillus niger endopolygalacturonase II by site-directed mutagenesis
    • Pagès S., Heijne W.H.M., Kester H.C.M., Visser J., and Benen J.A.E. Subsite mapping of Aspergillus niger endopolygalacturonase II by site-directed mutagenesis. J. Biol. Chem. 275 (2000) 29348-29353
    • (2000) J. Biol. Chem. , vol.275 , pp. 29348-29353
    • Pagès, S.1    Heijne, W.H.M.2    Kester, H.C.M.3    Visser, J.4    Benen, J.A.E.5
  • 29
    • 0034142291 scopus 로고    scopus 로고
    • pgaA and pgaB encode two constitutively expressed endopolygalacturonases of Aspergillus niger
    • Parenicová L., Benen J.A.E., Kester H.C.M., and Visser J. pgaA and pgaB encode two constitutively expressed endopolygalacturonases of Aspergillus niger. Biochem. J. 345 (2000) 637-644
    • (2000) Biochem. J. , vol.345 , pp. 637-644
    • Parenicová, L.1    Benen, J.A.E.2    Kester, H.C.M.3    Visser, J.4
  • 30
    • 0343114331 scopus 로고    scopus 로고
    • Characterization of a novel endopolygalacturonase from Aspergillus niger with unique kinetic properties
    • Parenicová L., Kester H.C.M., Benen J.A., and Visser J. Characterization of a novel endopolygalacturonase from Aspergillus niger with unique kinetic properties. FEBS Lett. 467 (2000) 333-336
    • (2000) FEBS Lett. , vol.467 , pp. 333-336
    • Parenicová, L.1    Kester, H.C.M.2    Benen, J.A.3    Visser, J.4
  • 31
    • 33846861493 scopus 로고    scopus 로고
    • Pel, H.J., de Winde, J.H., Archer, D.B., Dyer, P.S., Hofmann, G., Schaap, P.J., Turner, G., De Vries, R.P., Albang, R., Albermann, K., Andersen, M.R., Bendtsen, J.D., Benen, J.A., van den Berg, M., Breestraat, S., Caddick, M.X., Contreras, R., Cornell, M., Coutinho, P.M., Danchin, E.G., Debets, A.J., Dekker, P., van Dijck, P.W., van Dijk, A., Dijkhuizen, L., Driessen, A.J., d'Enfert, C., Geysens, S., Goosen, C., Groot, G.S., De Groot, P.W., Guillemette, T., Henrissat, B., Herweijer, M., van den Hombergh, J.P., van den Hondel, C.A., van der Heijden, R.T., van der Kaaij, R.M., Klis, F.M., Kools, H.J., Kubicek, C.P., van Kuyk, P.A., Lauber, J., Lu, X., van der Maarel, M.J., Meulenberg, R., Menke, H., Mortimer, M.A., Nielsen, J., Oliver, S.G., Olsthoorn, M., Pal, K., van Peij, N.N., Ram, A.F., Rinas, U., Roubos, J.A., Sagt, C.M., Schmoll, M., Sun, J., Ussery, D., Varga, J.
    • Pel, H.J., de Winde, J.H., Archer, D.B., Dyer, P.S., Hofmann, G., Schaap, P.J., Turner, G., De Vries, R.P., Albang, R., Albermann, K., Andersen, M.R., Bendtsen, J.D., Benen, J.A., van den Berg, M., Breestraat, S., Caddick, M.X., Contreras, R., Cornell, M., Coutinho, P.M., Danchin, E.G., Debets, A.J., Dekker, P., van Dijck, P.W., van Dijk, A., Dijkhuizen, L., Driessen, A.J., d'Enfert, C., Geysens, S., Goosen, C., Groot, G.S., De Groot, P.W., Guillemette, T., Henrissat, B., Herweijer, M., van den Hombergh, J.P., van den Hondel, C.A., van der Heijden, R.T., van der Kaaij, R.M., Klis, F.M., Kools, H.J., Kubicek, C.P., van Kuyk, P.A., Lauber, J., Lu, X., van der Maarel, M.J., Meulenberg, R., Menke, H., Mortimer, M.A., Nielsen, J., Oliver, S.G., Olsthoorn, M., Pal, K., van Peij, N.N., Ram, A.F., Rinas, U., Roubos, J.A., Sagt, C.M., Schmoll, M., Sun, J., Ussery, D., Varga, J., Vervecken, W., van de Vondervoort, P.J., Wedler, H., Wosten, HA., Zeng, A.P., van Ooyen, A.J., Visser, J., Stam, H., 2007. Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88. Nat. Biotechnol. 25, 221-231.
  • 32
    • 56249100136 scopus 로고    scopus 로고
    • Rhizopus oryzae Sequencing Project. Broad Institute of Harvard and MIT. http://www.broad.mit.edu (accessed December 2006).
    • Rhizopus oryzae Sequencing Project. Broad Institute of Harvard and MIT. http://www.broad.mit.edu (accessed December 2006).
  • 33
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • Ronquist F., and Huelsenbeck J.P. MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19 (2003) 1572-1574
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 34
    • 17044401340 scopus 로고    scopus 로고
    • Evolution of a large ribosomal RNA multigene family in filamentous fungi: birth-and-death of a concerted evolution paradigm
    • Rooney A.P., and Ward T.J. Evolution of a large ribosomal RNA multigene family in filamentous fungi: birth-and-death of a concerted evolution paradigm. Proc. Natl. Acad. Sci. USA 102 (2005) 5084-5089
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5084-5089
    • Rooney, A.P.1    Ward, T.J.2
  • 35
    • 0025356515 scopus 로고
    • Structural analysis of the pehA gene and characterization of its protein product, endopolygalacturonase, of Erwinia carotovora subspecies carotovora
    • Saarilahti H.T., Heino P., Pakkanen R., Kalkkinen N., Palva I., and Palva E.T. Structural analysis of the pehA gene and characterization of its protein product, endopolygalacturonase, of Erwinia carotovora subspecies carotovora. Mol. Microbiol. 4 (1990) 1037-1044
    • (1990) Mol. Microbiol. , vol.4 , pp. 1037-1044
    • Saarilahti, H.T.1    Heino, P.2    Pakkanen, R.3    Kalkkinen, N.4    Palva, I.5    Palva, E.T.6
  • 36
    • 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
  • 37
    • 4544225675 scopus 로고    scopus 로고
    • Genetic diversity in Rhizopus oryzae strains as revealed by the sequence of lactate dehydrogenase genes
    • Saito K., Saito A., Ohnishi M., and Oda Y. Genetic diversity in Rhizopus oryzae strains as revealed by the sequence of lactate dehydrogenase genes. Arch Microbiol. 182 (2004) 30-36
    • (2004) Arch Microbiol. , vol.182 , pp. 30-36
    • Saito, K.1    Saito, A.2    Ohnishi, M.3    Oda, Y.4
  • 39
    • 0036434440 scopus 로고    scopus 로고
    • Homologous recombination and double strand break repair in the transformation of Rhizopus oryzae
    • Skory C.D. Homologous recombination and double strand break repair in the transformation of Rhizopus oryzae. Mol. Genet. Genomics 268 (2002) 397-406
    • (2002) Mol. Genet. Genomics , vol.268 , pp. 397-406
    • Skory, C.D.1
  • 40
    • 33750423631 scopus 로고
    • Notes on sugar determination
    • Somogyi M. Notes on sugar determination. J. Biol. Chem. 195 (1952) 19-23
    • (1952) J. Biol. Chem. , vol.195 , pp. 19-23
    • Somogyi, M.1
  • 42
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4.0
    • Tamura K., Dudley J., Nei M., and Kumar S. MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24 (2007) 1596-1599
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 43
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25 (1997) 4876-4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 44
    • 0242457394 scopus 로고    scopus 로고
    • Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger
    • van Pouderoyen G., Snijder H.J., Benen A.E., and Dijkstra B.W. Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger. FEBS Lett. 554 (2003) 462-466
    • (2003) FEBS Lett. , vol.554 , pp. 462-466
    • van Pouderoyen, G.1    Snijder, H.J.2    Benen, A.E.3    Dijkstra, B.W.4
  • 45
    • 0032589464 scopus 로고    scopus 로고
    • 1.68-Å crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis
    • van Santen Y., Benen J.A.E., Schröter K., Kalk K.H., Armand S., Visser J., and Dijkkstra B.W. 1.68-Å crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis. J. Biol. Chem. 274 (1999) 30474-30480
    • (1999) J. Biol. Chem. , vol.274 , pp. 30474-30480
    • van Santen, Y.1    Benen, J.A.E.2    Schröter, K.3    Kalk, K.H.4    Armand, S.5    Visser, J.6    Dijkkstra, B.W.7
  • 46
    • 0035031966 scopus 로고    scopus 로고
    • A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach
    • Whelan S., and Goldman N. A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach. Mol. Biol. Evol. 18 (2001) 691-699
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 691-699
    • Whelan, S.1    Goldman, N.2
  • 47
    • 0036349189 scopus 로고    scopus 로고
    • Endopolygalacturonase is encoded by a multigene family in the basidomycete Chondrostereum purpuream
    • Williams H.L., Tang Y., and Hintz W.E. Endopolygalacturonase is encoded by a multigene family in the basidomycete Chondrostereum purpuream. Fungal Genet. Biol. 36 (2002) 71-83
    • (2002) Fungal Genet. Biol. , vol.36 , pp. 71-83
    • Williams, H.L.1    Tang, Y.2    Hintz, W.E.3
  • 48
    • 0032949792 scopus 로고    scopus 로고
    • Cloning and partial characterization of endopolygalacturonase genes from Botrytis cinerea
    • Wubben J.P., Mulder W., ten Have A., van kan J.A.L., and Visser J. Cloning and partial characterization of endopolygalacturonase genes from Botrytis cinerea. Appl. Environ. Microbiol. 65 (1999) 1596-1602
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1596-1602
    • Wubben, J.P.1    Mulder, W.2    ten Have, A.3    van kan, J.A.L.4    Visser, J.5
  • 49
    • 13444273599 scopus 로고    scopus 로고
    • Cloning and characterization of a gene rpg1 encoding polygalacturonase of Rhizopus oryzae
    • Yoshida S., Suzuki F., Tsukiboshi T., and Shinohara H. Cloning and characterization of a gene rpg1 encoding polygalacturonase of Rhizopus oryzae. Mycol. Res. 108 (2004) 1407-1414
    • (2004) Mycol. Res. , vol.108 , pp. 1407-1414
    • Yoshida, S.1    Suzuki, F.2    Tsukiboshi, T.3    Shinohara, H.4
  • 50
    • 27444435985 scopus 로고    scopus 로고
    • The active component in the flax-retting system of the zygomycete Rhizopus oryzae sb is a family 28 polygalacturonase
    • Zhang J., Henriksson H., Szabo I.J., Henriksson G., and Johansson G. The active component in the flax-retting system of the zygomycete Rhizopus oryzae sb is a family 28 polygalacturonase. J. Ind. Microbiol. Biotechnol. 32 (2005) 431-438
    • (2005) J. Ind. Microbiol. Biotechnol. , vol.32 , pp. 431-438
    • Zhang, J.1    Henriksson, H.2    Szabo, I.J.3    Henriksson, G.4    Johansson, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.