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Volumn 49, Issue 3, 2011, Pages 312-320

Characterization and mode of action of two acetyl xylan esterases from Chrysosporium lucknowense C1 active towards acetylated xylans

Author keywords

Acetyl xylan esterase; Acetylated xylooligosaccharides; Chrysosporium lucknowense; Eucalyptus; Xylan

Indexed keywords

ACETYL XYLAN ESTERASE; CHRYSOSPORIUM LUCKNOWENSE; EUCALYPTUS; XYLAN; XYLOOLIGOSACCHARIDES;

EID: 79960590224     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2011.05.010     Document Type: Article
Times cited : (34)

References (49)
  • 1
    • 0036616389 scopus 로고    scopus 로고
    • Biodegradation and biological treatments of cellulose, hemicellulose and lignin: an overview
    • Pérez J., Muñoz-Dorado J., de la Rubia T., Martínez J. Biodegradation and biological treatments of cellulose, hemicellulose and lignin: an overview. Int Microbiol 2002, 5:53-63.
    • (2002) Int Microbiol , vol.5 , pp. 53-63
    • Pérez, J.1    Muñoz-Dorado, J.2    de la Rubia, T.3    Martínez, J.4
  • 2
    • 0034922896 scopus 로고    scopus 로고
    • Fuel ethanol production from lignocellulose: a challenge for metabolic engineering and process integration
    • Zaldivar J., Nielsen J., Olsson L. Fuel ethanol production from lignocellulose: a challenge for metabolic engineering and process integration. Appl Microbiol Biotechnol 2001, 56:17-34.
    • (2001) Appl Microbiol Biotechnol , vol.56 , pp. 17-34
    • Zaldivar, J.1    Nielsen, J.2    Olsson, L.3
  • 3
    • 34250512499 scopus 로고
    • Recent progress in the chemistry of wood hemicellulose
    • Timell T.E. Recent progress in the chemistry of wood hemicellulose. Wood Sci Technol 1967, 1:45-70.
    • (1967) Wood Sci Technol , vol.1 , pp. 45-70
    • Timell, T.E.1
  • 4
    • 0028899381 scopus 로고
    • Conversion of cellulosic materials to ethanol
    • Ingram L.O., Doran J.B. Conversion of cellulosic materials to ethanol. FEMS Microbiol Rev 1995, 16:235-241.
    • (1995) FEMS Microbiol Rev , vol.16 , pp. 235-241
    • Ingram, L.O.1    Doran, J.B.2
  • 5
    • 0031909985 scopus 로고    scopus 로고
    • AguA, the gene encoding an extracellular alpha-glucuronidase from Aspergillus tubingensis, is specifically induced on xylose and not on glucuronic acid
    • de Vries R.P., Poulsen C.H., Madrid S., Visser J. aguA, the gene encoding an extracellular alpha-glucuronidase from Aspergillus tubingensis, is specifically induced on xylose and not on glucuronic acid. J Bacteriol 1998, 180:243-249.
    • (1998) J Bacteriol , vol.180 , pp. 243-249
    • de Vries, R.P.1    Poulsen, C.H.2    Madrid, S.3    Visser, J.4
  • 6
    • 0037623814 scopus 로고    scopus 로고
    • Hemicellulose bioconversion
    • Saha B. Hemicellulose bioconversion. J Ind Microbiol Biotechnol 2003, 30:279-291.
    • (2003) J Ind Microbiol Biotechnol , vol.30 , pp. 279-291
    • Saha, B.1
  • 7
    • 0001909043 scopus 로고    scopus 로고
    • Structural features of (glucurono)arabinoxylans extracted from wheat bran by barium hydroxide
    • Schoonveld-Bergmans M.E.F., Beldman G., Voragen A.G.J. Structural features of (glucurono)arabinoxylans extracted from wheat bran by barium hydroxide. J Cereal Sci 1999, 29:63-75.
    • (1999) J Cereal Sci , vol.29 , pp. 63-75
    • Schoonveld-Bergmans, M.E.F.1    Beldman, G.2    Voragen, A.G.J.3
  • 8
    • 85013724288 scopus 로고
    • Structural features of rice bran hemicellulose
    • Shibuya N., Iwasaki T. Structural features of rice bran hemicellulose. Phytochemistry 1985, 30:488-494.
    • (1985) Phytochemistry , vol.30 , pp. 488-494
    • Shibuya, N.1    Iwasaki, T.2
  • 9
    • 79960580203 scopus 로고
    • O-ferulated, O-acteylated oligosaccharides as side chains of grass xylans
    • Wende G., Fry S.C. O-ferulated, O-acteylated oligosaccharides as side chains of grass xylans. Phytochemistry 1991, 44:1019-1030.
    • (1991) Phytochemistry , vol.44 , pp. 1019-1030
    • Wende, G.1    Fry, S.C.2
  • 10
    • 1842492272 scopus 로고    scopus 로고
    • The functions of cell wall polysaccharides in composition and architecture revealed through mutations
    • Carpita N., McCann M. The functions of cell wall polysaccharides in composition and architecture revealed through mutations. Plant Soil 2002, 247:71-80.
    • (2002) Plant Soil , vol.247 , pp. 71-80
    • Carpita, N.1    McCann, M.2
  • 11
    • 0000599512 scopus 로고
    • On the ester linkage between lignin and 4-O-methyl-d-glucurono-d-xylan in jute fiber (Corchorus capsularis)
    • Das N.N., Das S.C., Mukherjee A.K. On the ester linkage between lignin and 4-O-methyl-d-glucurono-d-xylan in jute fiber (Corchorus capsularis). Carbohydr Res 1984, 127:345-348.
    • (1984) Carbohydr Res , vol.127 , pp. 345-348
    • Das, N.N.1    Das, S.C.2    Mukherjee, A.K.3
  • 12
    • 0000199142 scopus 로고
    • Ester linkages between lignin and glucuronoxylan in lignin-carbohydrate complex from beech (Fagus crenata) wood
    • Tabahashi N., Koshijima T. Ester linkages between lignin and glucuronoxylan in lignin-carbohydrate complex from beech (Fagus crenata) wood. Wood Sci Technol 1988, 22:231-241.
    • (1988) Wood Sci Technol , vol.22 , pp. 231-241
    • Tabahashi, N.1    Koshijima, T.2
  • 14
    • 0027907989 scopus 로고
    • Mode of action of (1→4)-beta-d-arabinoxylan arabinofuranohydrolase (AXH) and alpha-l-arabinofuranosidases on alkali-extractable wheat-flour arabinoxylan
    • Kormelink F.J.M., Gruppen H., Voragen A.G.J. Mode of action of (1→4)-beta-d-arabinoxylan arabinofuranohydrolase (AXH) and alpha-l-arabinofuranosidases on alkali-extractable wheat-flour arabinoxylan. Carbohydr Res 1993, 249:345-353.
    • (1993) Carbohydr Res , vol.249 , pp. 345-353
    • Kormelink, F.J.M.1    Gruppen, H.2    Voragen, A.G.J.3
  • 15
    • 33751542736 scopus 로고    scopus 로고
    • A novel GH43 α-l-arabinofuranosidase from Humicola insolens: mode of action and synergy with GH51 α-l-arabinofuranosidases on wheat arabinoxylan
    • Sørensen H.R., Jørgensen C.T., Hansen C.H., Jørgensen C.I., Pedersen S., Meyer A.S. A novel GH43 α-l-arabinofuranosidase from Humicola insolens: mode of action and synergy with GH51 α-l-arabinofuranosidases on wheat arabinoxylan. Appl Microbiol Biotechnol 2006, 73:850-861.
    • (2006) Appl Microbiol Biotechnol , vol.73 , pp. 850-861
    • Sørensen, H.R.1    Jørgensen, C.T.2    Hansen, C.H.3    Jørgensen, C.I.4    Pedersen, S.5    Meyer, A.S.6
  • 16
  • 17
    • 34548463377 scopus 로고    scopus 로고
    • Cloning, characterisation and expression analysis of α-glucuronidase from the thermophilic fungus Talaromyces emersonii
    • Heneghan M.N., McLoughlin L., Murray P.G., Tuohy M.G. Cloning, characterisation and expression analysis of α-glucuronidase from the thermophilic fungus Talaromyces emersonii. Enzyme Microb Technol 2007, 41:677-682.
    • (2007) Enzyme Microb Technol , vol.41 , pp. 677-682
    • Heneghan, M.N.1    McLoughlin, L.2    Murray, P.G.3    Tuohy, M.G.4
  • 18
    • 0034629241 scopus 로고    scopus 로고
    • An α-glucuronidase of Schizophyllum commune acting on polymeric xylan
    • Tenkanen M., Siika-aho M. An α-glucuronidase of Schizophyllum commune acting on polymeric xylan. J Biotechnol 2000, 78:149-161.
    • (2000) J Biotechnol , vol.78 , pp. 149-161
    • Tenkanen, M.1    Siika-aho, M.2
  • 20
    • 33846152664 scopus 로고    scopus 로고
    • A type B feruloyl esterase from Aspergillus nidulans with broad pH applicability
    • Shin H.D., Chen R. A type B feruloyl esterase from Aspergillus nidulans with broad pH applicability. Appl Microbiol Biotechnol 2007, 73:1323-1330.
    • (2007) Appl Microbiol Biotechnol , vol.73 , pp. 1323-1330
    • Shin, H.D.1    Chen, R.2
  • 21
    • 0037090961 scopus 로고    scopus 로고
    • The Aspergillus niger faeB gene encodes a second feruloyl esterase involved in pectin and xylan degradation and is specifically induced in the presence of aromatic compounds
    • de Vries R.P., van Kuyk P.A., Kester H.C.M., Visser J. The Aspergillus niger faeB gene encodes a second feruloyl esterase involved in pectin and xylan degradation and is specifically induced in the presence of aromatic compounds. Biochem J 2002, 363:377-386.
    • (2002) Biochem J , vol.363 , pp. 377-386
    • de Vries, R.P.1    van Kuyk, P.A.2    Kester, H.C.M.3    Visser, J.4
  • 22
    • 0028892406 scopus 로고
    • Release of ferulic acid from wheat bran by a ferulic acid esterase (FAE-III) from Aspergillus niger
    • Faulds C.B., Williamson G. Release of ferulic acid from wheat bran by a ferulic acid esterase (FAE-III) from Aspergillus niger. Appl Microbiol Biotechnol 1995, 43:1082-1087.
    • (1995) Appl Microbiol Biotechnol , vol.43 , pp. 1082-1087
    • Faulds, C.B.1    Williamson, G.2
  • 23
  • 24
    • 57449109714 scopus 로고    scopus 로고
    • Novel family of carbohydrate esterases, based on identification of the Hypocrea jecorina acetyl esterase gene
    • Li X.-L., Skory C.D., Cotta M.A., Puchart V., Biely P. Novel family of carbohydrate esterases, based on identification of the Hypocrea jecorina acetyl esterase gene. Appl Environ Microbiol 2008, 74:7482-7489.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 7482-7489
    • Li, X.-L.1    Skory, C.D.2    Cotta, M.A.3    Puchart, V.4    Biely, P.5
  • 25
    • 0027415217 scopus 로고
    • Purification and characterization of three endo-(1,4)-β-xylanases and β-xylosidase from Aspergillus awamori
    • Kormelink F.J.M., Searle-van Leeuwen M.J.F., Wood T.M., Voragen A.G.J. Purification and characterization of three endo-(1,4)-β-xylanases and β-xylosidase from Aspergillus awamori. J Biotechnol 1993, 27:249-265.
    • (1993) J Biotechnol , vol.27 , pp. 249-265
    • Kormelink, F.J.M.1    Searle-van Leeuwen, M.J.F.2    Wood, T.M.3    Voragen, A.G.J.4
  • 26
    • 67650786749 scopus 로고    scopus 로고
    • Enzymatically derived aldouronic acids from Eucalyptus globulus glucuronoxylan
    • Togashi H., Kato A., Shimizu K. Enzymatically derived aldouronic acids from Eucalyptus globulus glucuronoxylan. Carbohydr Polym 2009, 78:247-252.
    • (2009) Carbohydr Polym , vol.78 , pp. 247-252
    • Togashi, H.1    Kato, A.2    Shimizu, K.3
  • 27
    • 0037470846 scopus 로고    scopus 로고
    • Characterization of an acetylated heteroxylan from Eucalyptus globulus Labill
    • Evtuguin D.V., Tomás J.L., Silva A.M.S., Neto C.P. Characterization of an acetylated heteroxylan from Eucalyptus globulus Labill. Carbohydr Res 2003, 338:597-604.
    • (2003) Carbohydr Res , vol.338 , pp. 597-604
    • Evtuguin, D.V.1    Tomás, J.L.2    Silva, A.M.S.3    Neto, C.P.4
  • 28
  • 30
    • 33750017102 scopus 로고    scopus 로고
    • Penicillium purpurogenum produces a family 1 acetyl xylan esterase containing a carbohydrate-binding module: characterization of the protein and its gene
    • Gordillo F., Caputo V., Peirano A., Chávez R., Van Beeumen J., Vandenberghe I., et al. Penicillium purpurogenum produces a family 1 acetyl xylan esterase containing a carbohydrate-binding module: characterization of the protein and its gene. Mycol Res 2006, 110:1129-1139.
    • (2006) Mycol Res , vol.110 , pp. 1129-1139
    • Gordillo, F.1    Caputo, V.2    Peirano, A.3    Chávez, R.4    Van Beeumen, J.5    Vandenberghe, I.6
  • 31
    • 33747412234 scopus 로고    scopus 로고
    • Recent progress in the assays of xylanolytic enzymes
    • Biely P., Puchart V. Recent progress in the assays of xylanolytic enzymes. J Sci Food Agric 2006, 86:1636-1647.
    • (2006) J Sci Food Agric , vol.86 , pp. 1636-1647
    • Biely, P.1    Puchart, V.2
  • 32
    • 58649117988 scopus 로고    scopus 로고
    • Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp. lactis AD011
    • Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., et al. Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp. lactis AD011. J Bacteriol 2009, 191:678-679.
    • (2009) J Bacteriol , vol.191 , pp. 678-679
    • Kim, J.F.1    Jeong, H.2    Yu, D.S.3    Choi, S.-H.4    Hur, C.-G.5    Park, M.-S.6
  • 34
    • 0034465722 scopus 로고    scopus 로고
    • Three-dimensional structure of the catalytic core of acetylxylan esterase from Trichoderma reesei: insights into the deacetylation mechanism
    • Hakulinen N., Tenkanen M., Rouvinen J. Three-dimensional structure of the catalytic core of acetylxylan esterase from Trichoderma reesei: insights into the deacetylation mechanism. J Struct Biol 2000, 132:180-190.
    • (2000) J Struct Biol , vol.132 , pp. 180-190
    • Hakulinen, N.1    Tenkanen, M.2    Rouvinen, J.3
  • 35
    • 78650710670 scopus 로고    scopus 로고
    • Action of xylan deacetylating enzymes on monoacetyl derivatives of 4-nitrophenyl glycosides of β-d-xylopyranose and α-l-arabinofuranose
    • Biely P., Mastihubova M., Tenkanen M., Eyzaguirre J., Li X.-L., Vrŝanská M. Action of xylan deacetylating enzymes on monoacetyl derivatives of 4-nitrophenyl glycosides of β-d-xylopyranose and α-l-arabinofuranose. J Biotechnol 2011, 151:137-142.
    • (2011) J Biotechnol , vol.151 , pp. 137-142
    • Biely, P.1    Mastihubova, M.2    Tenkanen, M.3    Eyzaguirre, J.4    Li, X.-L.5    Vrŝanská, M.6
  • 37
    • 34047238347 scopus 로고    scopus 로고
    • A dedicated vector for efficient library construction and high throughput screening in the hyphal fungus Chrysosporium lucknowense
    • Verdoes J.C., Punt P.J., Burlingame R., Bartels J., Van Dijk R., Slump E., et al. A dedicated vector for efficient library construction and high throughput screening in the hyphal fungus Chrysosporium lucknowense. Ind. Biotechnol. 2007, 3:48-57.
    • (2007) Ind. Biotechnol. , vol.3 , pp. 48-57
    • Verdoes, J.C.1    Punt, P.J.2    Burlingame, R.3    Bartels, J.4    Van Dijk, R.5    Slump, E.6
  • 38
    • 0347367045 scopus 로고    scopus 로고
    • Location of O-acetyl substituents in xylo-oligosaccharides obtained from hydrothermally treated Eucalyptus wood
    • Kabel M.A., de Waard P., Schols H.A., Voragen A.G.J. Location of O-acetyl substituents in xylo-oligosaccharides obtained from hydrothermally treated Eucalyptus wood. Carbohydr Res 2003, 338:69-77.
    • (2003) Carbohydr Res , vol.338 , pp. 69-77
    • Kabel, M.A.1    de Waard, P.2    Schols, H.A.3    Voragen, A.G.J.4
  • 40
    • 0025320429 scopus 로고
    • Essential probelms in quantification of proteins following colloidal staining with coomassie brilliant blue dyes in polyacrylamide gels, and their solution
    • Neuhoff V., Stamm R., Pardowitz I., Arold N., Ehrhardt W., Taube D. Essential probelms in quantification of proteins following colloidal staining with coomassie brilliant blue dyes in polyacrylamide gels, and their solution. Electrophoresis 1990, 11:101-117.
    • (1990) Electrophoresis , vol.11 , pp. 101-117
    • Neuhoff, V.1    Stamm, R.2    Pardowitz, I.3    Arold, N.4    Ehrhardt, W.5    Taube, D.6
  • 41
    • 66149085766 scopus 로고    scopus 로고
    • Introducing capillary electrophoresis with laser-induced fluorescence detection (CE-LIF) for the characterization of konjac glucomannan oligosaccharides and their in vitro fermentation behavior
    • Albrecht S., Van Muiswinkel G.C.J., Schols H.A., Voragen A.G.J., Gruppen H. Introducing capillary electrophoresis with laser-induced fluorescence detection (CE-LIF) for the characterization of konjac glucomannan oligosaccharides and their in vitro fermentation behavior. J Agric Food Chem 2009, 57:3867-3876.
    • (2009) J Agric Food Chem , vol.57 , pp. 3867-3876
    • Albrecht, S.1    Van Muiswinkel, G.C.J.2    Schols, H.A.3    Voragen, A.G.J.4    Gruppen, H.5
  • 45
    • 33646521703 scopus 로고    scopus 로고
    • The xylanolytic enzyme system from the genus Penicillium
    • Chávez R., Bull P., Eyzaguirre J. The xylanolytic enzyme system from the genus Penicillium. J Biotechnol 2006, 123:413-433.
    • (2006) J Biotechnol , vol.123 , pp. 413-433
    • Chávez, R.1    Bull, P.2    Eyzaguirre, J.3
  • 46
    • 0141842967 scopus 로고    scopus 로고
    • Comparison of catalytic properties of acetyl xylan esterases from three carbohydrate esterase families
    • Tenkanen M., Eyzaguirre J., Isoniemi R., Faulds C.B., Biely P. Comparison of catalytic properties of acetyl xylan esterases from three carbohydrate esterase families. ACS Symp Ser 2003, 855:211-229.
    • (2003) ACS Symp Ser , vol.855 , pp. 211-229
    • Tenkanen, M.1    Eyzaguirre, J.2    Isoniemi, R.3    Faulds, C.B.4    Biely, P.5
  • 47
    • 0023029475 scopus 로고
    • Cooperativity of esterases and xylanases in the enzymatic degradation of acetyl xylan
    • Biely P., MacKenzie C.R., Puls J., Schneider H. Cooperativity of esterases and xylanases in the enzymatic degradation of acetyl xylan. Biotechnology 1986, 4:731-733.
    • (1986) Biotechnology , vol.4 , pp. 731-733
    • Biely, P.1    MacKenzie, C.R.2    Puls, J.3    Schneider, H.4
  • 49
    • 2142715897 scopus 로고    scopus 로고
    • Lipase-catalysed preparation of acetates of 4-nitrophenyl β-d-xylopyranoside and their use in kinetic studies of acetyl migration
    • Mastihubová M., Biely P. Lipase-catalysed preparation of acetates of 4-nitrophenyl β-d-xylopyranoside and their use in kinetic studies of acetyl migration. Carbohydr Res 2004, 339:1353-1360.
    • (2004) Carbohydr Res , vol.339 , pp. 1353-1360
    • Mastihubová, M.1    Biely, P.2


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