메뉴 건너뛰기




Volumn 69, Issue 9, 2003, Pages 5622-5626

Purification and properties of a feruloyl esterase involved in lignocellulose degradation by Aureobasidium pullulans

Author keywords

[No Author keywords available]

Indexed keywords

HYDROPHOBIC INTERACTION;

EID: 0141481200     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.69.9.5622-5626.2003     Document Type: Article
Times cited : (59)

References (40)
  • 1
    • 0036901753 scopus 로고    scopus 로고
    • Differentiation of feruloyl esterases on synthetic substrates in α-arabinofuranosidase-coupled and UV-spectrophotometric assays
    • Biely, P., M. Mastihubová, W. H. van Zyl, and B. A. Prior. 2002. Differentiation of feruloyl esterases on synthetic substrates in α-arabinofuranosidase-coupled and UV-spectrophotometric assays. Anal. Biochem. 311:68-75.
    • (2002) Anal. Biochem. , vol.311 , pp. 68-75
    • Biely, P.1    Mastihubová, M.2    Van Zyl, W.H.3    Prior, B.A.4
  • 2
    • 0033983751 scopus 로고    scopus 로고
    • Feruloyl esterase activity of the Clostridium thermocellum cellulosome can be attributed to previously unknown domains of XynY and XynZ
    • Blum, D. L., I. A. Kataeva, X. L. Li, and L. G. Ljungdahl. 2000. Feruloyl esterase activity of the Clostridium thermocellum cellulosome can be attributed to previously unknown domains of XynY and XynZ. J. Bacteriol. 182:1346-1351.
    • (2000) J. Bacteriol. , vol.182 , pp. 1346-1351
    • Blum, D.L.1    Kataeva, I.A.2    Li, X.L.3    Ljungdahl, L.G.4
  • 3
    • 0026448264 scopus 로고
    • Purification and partial characterization of two feruloyl esterases from the anaerobic fungus Neocallimastix strain MC-2
    • Borneman, W. S., L. G. Ljungdahl, R. D. Hartley, and D. E. Akin. 1992. Purification and partial characterization of two feruloyl esterases from the anaerobic fungus Neocallimastix strain MC-2. Appl. Environ. Microbiol. 58:3762-3766.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3762-3766
    • Borneman, W.S.1    Ljungdahl, L.G.2    Hartley, R.D.3    Akin, D.E.4
  • 4
    • 0034028789 scopus 로고    scopus 로고
    • Lignins and lignification: Selected issues
    • Boudet, A. M. 2000. Lignins and lignification: selected issues. Plant Physiol. Biochem. 38:81-96.
    • (2000) Plant Physiol. Biochem. , vol.38 , pp. 81-96
    • Boudet, A.M.1
  • 5
    • 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. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0026955801 scopus 로고
    • Purification and properties of a feruloyl/p-coumaroyl esterase from the fungus Penicillium pinophilum
    • Castanares, A., S. I. McCrae, and T. M. Wood. 1992. Purification and properties of a feruloyl/p-coumaroyl esterase from the fungus Penicillium pinophilum. Enzyme Microb. Technol. 14:875-884.
    • (1992) Enzyme Microb. Technol. , vol.14 , pp. 875-884
    • Castanares, A.1    McCrae, S.I.2    Wood, T.M.3
  • 7
    • 0030111186 scopus 로고    scopus 로고
    • Repeated treatments with Aureobasidium pullulans hemicellulases and alkali enhance biobleaching of sulphite pulps
    • Christov, L. P., and B. A. Prior. 1996. Repeated treatments with Aureobasidium pullulans hemicellulases and alkali enhance biobleaching of sulphite pulps. Enzyme Microb. Technol. 18:244-250.
    • (1996) Enzyme Microb. Technol. , vol.18 , pp. 244-250
    • Christov, L.P.1    Prior, B.A.2
  • 8
    • 0028712259 scopus 로고
    • Lignin-carbohydrate complexes in forages: Structure and consequences in the ruminal degradation of cell-wall carbohydrates
    • Cornu, A., J. M. Besle, P. Mosoni, and G. G. Gross. 1994. Lignin-carbohydrate complexes in forages: structure and consequences in the ruminal degradation of cell-wall carbohydrates. Reprod. Nutr. 34:385-389.
    • (1994) Reprod. Nutr. , vol.34 , pp. 385-389
    • Cornu, A.1    Besle, J.M.2    Mosoni, P.3    Gross, G.G.4
  • 9
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: An integrated database approach
    • H. J. Gilbert, G. Davies, B. Henrissat, and B. Svensson (ed.). The Royal Society of Chemistry, Cambridge, United Kingdom
    • Coutinho, P. M., and B. Henrissat. 1999. Carbohydrate-active enzymes: an integrated database approach, p. 3-12. In H. J. Gilbert, G. Davies, B. Henrissat, and B. Svensson (ed.), Recent advances in carbohydrate bioengineering. The Royal Society of Chemistry, Cambridge, United Kingdom.
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 3-12
    • Coutinho, P.M.1    Henrissat, B.2
  • 10
    • 0030272514 scopus 로고    scopus 로고
    • Cloning of a gene encoding cinnamoyl ester hydrolase from the ruminal bacterium Butyrivibrio fibrisolvens E14 by a novel method
    • Dalrymple, B. P., Y. Swadling, D. H. Cybinski, and G. P. Xue. 1996. Cloning of a gene encoding cinnamoyl ester hydrolase from the ruminal bacterium Butyrivibrio fibrisolvens E14 by a novel method. FEMS Microbiol. Lett. 143:115-120.
    • (1996) FEMS Microbiol. Lett. , vol.143 , pp. 115-120
    • Dalrymple, B.P.1    Swadling, Y.2    Cybinski, D.H.3    Xue, G.P.4
  • 11
    • 0026899847 scopus 로고
    • Aureobasidium pullulans in applied microbiology: A status report
    • Deshpande, M. S., V. B. Rale, and J. M. Lynch. 1992. Aureobasidium pullulans in applied microbiology: a status report. Enzyme Microb. Technol. 14:514-527.
    • (1992) Enzyme Microb. Technol. , vol.14 , pp. 514-527
    • Deshpande, M.S.1    Rale, V.B.2    Lynch, J.M.3
  • 13
    • 0031457584 scopus 로고    scopus 로고
    • Purification and characterization of a feruloyl esterase from the fungus Penicillium expansum
    • Donaghy, J., and A. M. McKay. 1997. Purification and characterization of a feruloyl esterase from the fungus Penicillium expansum. J. Appl. Microbiol. 83:718-726.
    • (1997) J. Appl. Microbiol. , vol.83 , pp. 718-726
    • Donaghy, J.1    McKay, A.M.2
  • 14
    • 0025954878 scopus 로고
    • The purification and characterization of 4-hydroxy-3-methoxycinnamic (ferulic) acid esterase from Streptomyces olivochromogenes
    • Faulds, C. B., and G. Williamson. 1991. The purification and characterization of 4-hydroxy-3-methoxycinnamic (ferulic) acid esterase from Streptomyces olivochromogenes. J. Gen. Microbiol. 137:2339-2345.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2339-2345
    • Faulds, C.B.1    Williamson, G.2
  • 15
    • 0028218853 scopus 로고
    • Purification and characterization of a ferulic acid esterase (FAE-III) from Aspergillus niger: Specificity of the phenolic moiety and binding to microcrystalline cellulose
    • Faulds, C. B., and G. Williamson. 1994. Purification and characterization of a ferulic acid esterase (FAE-III) from Aspergillus niger: specificity of the phenolic moiety and binding to microcrystalline cellulose. Microbiology 140:779-787.
    • (1994) Microbiology , vol.140 , pp. 779-787
    • Faulds, C.B.1    Williamson, G.2
  • 16
    • 0033214507 scopus 로고    scopus 로고
    • A modular cinnamoyl ester hydrolase from the anaerobic fungus Piromyces equi acts synergistically with xylanase and is part of a multiprotein cellulose-binding cellulase-hemicellulase complex
    • Fillingham, I. J., P. A. Kroon, G. Williamson, H. J. Gilbert, and G. P. Hazlewood. 1999. A modular cinnamoyl ester hydrolase from the anaerobic fungus Piromyces equi acts synergistically with xylanase and is part of a multiprotein cellulose-binding cellulase-hemicellulase complex. Biochem. J. 343:215-224.
    • (1999) Biochem. J. , vol.343 , pp. 215-224
    • Fillingham, I.J.1    Kroon, P.A.2    Williamson, G.3    Gilbert, H.J.4    Hazlewood, G.P.5
  • 17
    • 0000506710 scopus 로고
    • Cross-linking of matrix polymers in the growing cell walls of angiosperms
    • Fry, S. C. 1986. Cross-linking of matrix polymers in the growing cell walls of angiosperms. Annu. Rev. Plant. Physiol. 37:165-186.
    • (1986) Annu. Rev. Plant. Physiol. , vol.37 , pp. 165-186
    • Fry, S.C.1
  • 18
    • 0031717205 scopus 로고    scopus 로고
    • Lignin-hemicellulose complexes restrict enzymatic solubilization of mannan and xylan from dissolving pulp
    • Gübitz, G. M., D. W. Stebbing, C. I. Johansson, and J. N. Saddler. 1998. Lignin-hemicellulose complexes restrict enzymatic solubilization of mannan and xylan from dissolving pulp. Appl. Microbiol. Biotechnol. 50:390-395.
    • (1998) Appl. Microbiol. Biotechnol. , vol.50 , pp. 390-395
    • Gübitz, G.M.1    Stebbing, D.W.2    Johansson, C.I.3    Saddler, J.N.4
  • 20
    • 0000206036 scopus 로고
    • Phenolic bridges between polysaccharides and lignin in wheat internodes
    • Iiyama, K., T. B. T. Lam, and B. A. Stone. 1990. Phenolic bridges between polysaccharides and lignin in wheat internodes. Phytochemistry 29:733-737.
    • (1990) Phytochemistry , vol.29 , pp. 733-737
    • Iiyama, K.1    Lam, T.B.T.2    Stone, B.A.3
  • 21
    • 0025068644 scopus 로고
    • Feruloylated xyloglucan and p-coumaryl arabinoxylan oligosaccharides from bamboo shoot cell walls
    • Ishii, T., T. Hiroi, and J. R. Thomas. 1990. Feruloylated xyloglucan and p-coumaryl arabinoxylan oligosaccharides from bamboo shoot cell walls. Phytochemistry 29:1999-2003.
    • (1990) Phytochemistry , vol.29 , pp. 1999-2003
    • Ishii, T.1    Hiroi, T.2    Thomas, J.R.3
  • 22
    • 0000990069 scopus 로고
    • Biodegradation of lignin-carbohydrate complexes
    • Jeffries, T. W. 1990. Biodegradation of lignin-carbohydrate complexes. Biodegradation 1:163-176.
    • (1990) Biodegradation , vol.1 , pp. 163-176
    • Jeffries, T.W.1
  • 23
    • 0029888799 scopus 로고    scopus 로고
    • Purification and characterization of a novel esterase induced by growth of Aspergillus niger on sugar-beet pulp
    • Kroon, P. A., C. B. Faulds, and G. Williamson. 1996. Purification and characterization of a novel esterase induced by growth of Aspergillus niger on sugar-beet pulp. Biotechnol. Appl. Biochem. 23:255-262.
    • (1996) Biotechnol. Appl. Biochem. , vol.23 , pp. 255-262
    • Kroon, P.A.1    Faulds, C.B.2    Williamson, G.3
  • 24
    • 0033679102 scopus 로고    scopus 로고
    • A modular esterase from Penicillium funiculosum which releases ferulic acid from plant cell walls and binds crystalline cellulose contains a carbohydrate binding module
    • Kroon, P. A., G. Williamson, N. M. Fish, D. B. Archer, and N. J. Belshaw. 2000. A modular esterase from Penicillium funiculosum which releases ferulic acid from plant cell walls and binds crystalline cellulose contains a carbohydrate binding module. Eur. J. Biochem. 267:6740-6752.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6740-6752
    • Kroon, P.A.1    Williamson, G.2    Fish, N.M.3    Archer, D.B.4    Belshaw, N.J.5
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0035800179 scopus 로고    scopus 로고
    • Bonding of hydroxycinnamic acids to lignin: Ferulic and p-coumaric acids are predominantly linked at the benzyl position of lignin, not the β-position, in grass cell walls
    • Lam, T. B. T., K. Kadoya, and K. Iiyama. 2001. Bonding of hydroxycinnamic acids to lignin: ferulic and p-coumaric acids are predominantly linked at the benzyl position of lignin, not the β-position, in grass cell walls. Phytochemistry 57:987-992.
    • (2001) Phytochemistry , vol.57 , pp. 987-992
    • Lam, T.B.T.1    Kadoya, K.2    Iiyama, K.3
  • 27
    • 0022998285 scopus 로고
    • Color variants of aureobasidium pullulans overproduce xylanase with extremely high specific activity
    • Leathers, T. D. 1986. Color variants of aureobasidium pullulans overproduce xylanase with extremely high specific activity. Appl. Environ. Microbiol. 52:1026-1030.
    • (1986) Appl. Environ. Microbiol. , vol.52 , pp. 1026-1030
    • Leathers, T.D.1
  • 28
    • 0028518490 scopus 로고
    • Xylandegrading enzyme system produced by the fungus Aspergillus awamori: Isolation and characterization of a feruloyl esterase and ap-coumaroyl esterase
    • McCrae, S. I., K. M. Leith, A. H. Gordon, and T. M. Wood. 1994. Xylandegrading enzyme system produced by the fungus Aspergillus awamori: isolation and characterization of a feruloyl esterase and ap-coumaroyl esterase. Enzyme Microb. Technol. 16:826-834.
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 826-834
    • McCrae, S.I.1    Leith, K.M.2    Gordon, A.H.3    Wood, T.M.4
  • 29
    • 0035666321 scopus 로고    scopus 로고
    • The structure of the feruloyl esterase module of xylanase 10B from Clostridium thermocellum provides insights into substrate recognition
    • Prates, J. A. M., N. Tarbouriech, S. J. Charnock, C. M. G. A. Fontes, L. M. A. Ferreira, and G. J. Davies. 2001. The structure of the feruloyl esterase module of xylanase 10B from Clostridium thermocellum provides insights into substrate recognition. Structure 9:1183-1190.
    • (2001) Structure , vol.9 , pp. 1183-1190
    • Prates, J.A.M.1    Tarbouriech, N.2    Charnock, S.J.3    Fontes, C.M.G.A.4    Ferreira, L.M.A.5    Davies, G.J.6
  • 30
    • 37049067514 scopus 로고
    • Lignin-feruloyl ester cross links in grasses. Part 1. Incorporation of feruloyl esters into coniferyl alcohol dehydrogenation polymers
    • Ralph, J., R. F. Helm, S. Quideau, and R. D. Hatfield. 1992. Lignin-feruloyl ester cross links in grasses. Part 1. Incorporation of feruloyl esters into coniferyl alcohol dehydrogenation polymers. J. Chem. Soc. Perkin Trans. I 21:2961-2969.
    • (1992) J. Chem. Soc. Perkin Trans. I , vol.21 , pp. 2961-2969
    • Ralph, J.1    Helm, R.F.2    Quideau, S.3    Hatfield, R.D.4
  • 31
    • 0034441830 scopus 로고    scopus 로고
    • Cementing the wall: Cell wall polysaccharide synthesising enzymes
    • Reid, J. G. 2000. Cementing the wall: cell wall polysaccharide synthesising enzymes. Curr. Opin. Plant Biol. 3:512-516.
    • (2000) Curr. Opin. Plant Biol. , vol.3 , pp. 512-516
    • Reid, J.G.1
  • 32
    • 84870304657 scopus 로고    scopus 로고
    • Influence of growth substrate and free ferulic acid on the production of feruloyl esterase by Aureobasidium pullulans
    • S. D. Mansfield and J. N. Saddler (ed.). American Chemical Society, Washington, D.C.
    • Rumbold, K., G. M. Gübitz, K.-H. Robra, and B. A. Prior. 2002. Influence of growth substrate and free ferulic acid on the production of feruloyl esterase by Aureobasidium pullulans, p. 151-160. In S. D. Mansfield and J. N. Saddler (ed.), Enzymes in lignocellulose degradation. American Chemical Society, Washington, D.C.
    • (2002) Enzymes in Lignocellulose Degradation , pp. 151-160
    • Rumbold, K.1    Gübitz, G.M.2    Robra, K.-H.3    Prior, B.A.4
  • 33
    • 0037198886 scopus 로고    scopus 로고
    • Monitoring on-line desalted lignocellulosic hydrolysates by microdialysis sampling micro-high performance anion exchange chromatography with integrated pulsed electrochemical detection/mass spectrometry
    • DOI: 10.1002/bit.10264
    • Rumbold K, Okatch H, Torto N, Siika-Aho M, Gubitz G, Robra KH,Prior B (2002). Monitoring on-line desalted lignocellulosic hydrolysates by microdialysis sampling micro-high performance anion exchange chromatography with integrated pulsed electrochemical detection/mass spectrometry. J. Biotech. Bioeng. 78(7):822-828, DOI: 10.1002/bit.10264.
    • (2002) Biotechnology and Bioengineering , vol.78 , Issue.7 , pp. 822-828
    • Rumbold, K.1    Okatch, H.2    Torto, N.3    Siika-Aho, M.4    Gübitz, G.M.5    Robra, K.-H.6    Prior, B.A.7
  • 34
    • 0031975343 scopus 로고    scopus 로고
    • Purification and characterization of a novel thermostable α-L-arabinofuranosidase from a color-variant strain of Aureobasidium pullulans
    • Saha, B. C., and R. J. Bothast. 1998. Purification and characterization of a novel thermostable α-L-arabinofuranosidase from a color-variant strain of Aureobasidium pullulans. Appl. Environ. Microbiol. 64:216-220.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 216-220
    • Saha, B.C.1    Bothast, R.J.2
  • 35
    • 0028136713 scopus 로고
    • Production, purification and properties of a thermostable β-glucosidase from a color-variant strain of Aureobasidium pullulans
    • Saha, B. C., S. N. Freer, and R. J. Bothast. 1994. Production, purification and properties of a thermostable β-glucosidase from a color-variant strain of Aureobasidium pullulans. Appl. Environ. Microbiol. 60:3774-3780.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3774-3780
    • Saha, B.C.1    Freer, S.N.2    Bothast, R.J.3
  • 37
    • 0033059228 scopus 로고    scopus 로고
    • Ferulic acid and diferulic acids as components of sugar-beet pectins and maize bran heteroxylans
    • Saulnier, L., and J. F. Thibault. 1999. Ferulic acid and diferulic acids as components of sugar-beet pectins and maize bran heteroxylans. J. Sci. Food Agric. 79:396-402.
    • (1999) J. Sci. Food Agric. , vol.79 , pp. 396-402
    • Saulnier, L.1    Thibault, J.F.2
  • 38
    • 0026031235 scopus 로고
    • Production, purification and characterization of an esterase liberating phenolic acids from lignocellulosics
    • Tenkanen, M., J. Schuseil, J. Puls, and K. Poutanen. 1991. Production, purification and characterization of an esterase liberating phenolic acids from lignocellulosics. J. Biotechnol. 1:69-84.
    • (1991) J. Biotechnol. , vol.1 , pp. 69-84
    • Tenkanen, M.1    Schuseil, J.2    Puls, J.3    Poutanen, K.4
  • 39
  • 40
    • 0031662992 scopus 로고    scopus 로고
    • Hairy plant polysaccharides: A close shave with microbial esterases
    • Williamson, G., P. A. Kroon, and C. B. Faulds. 1998. Hairy plant polysaccharides: a close shave with microbial esterases. Microbiology 144:2011-2023.
    • (1998) Microbiology , vol.144 , pp. 2011-2023
    • Williamson, G.1    Kroon, P.A.2    Faulds, C.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.