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Volumn 79, Issue 6, 2013, Pages 1990-1995

Distinct actions by Paenibacillus sp. strain E18 α-larabinofuranosidases and xylanase in xylan degradation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ARABINANS; COMBINED EFFECT; FAMILY 10 XYLANASE; GENE CLUSTERS; OPEN READING FRAME; PAENIBACILLUS SP; SIDE-CHAINS; STERIC HINDRANCES; SUBSTRATE SPECIFICITY; SYNERGISTIC EFFECT; WHEAT ARABINOXYLAN; XYLAN DEGRADATIONS; XYLANASES; XYLOBIOSES; XYLOOLIGOSACCHARIDES;

EID: 84874806579     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.03276-12     Document Type: Article
Times cited : (29)

References (35)
  • 1
    • 0001719868 scopus 로고
    • Xylan structure, microbial xylanases, and their mode of action
    • Bastawde KB. 1992. Xylan structure, microbial xylanases, and their mode of action. World J. Microbiol. Biotechnol. 8:353-368.
    • (1992) World J. Microbiol. Biotechnol. , vol.8 , pp. 353-368
    • Bastawde, K.B.1
  • 3
    • 0036159062 scopus 로고    scopus 로고
    • Hydrolysis of lignocellulosic materials for ethanol production: a review
    • Sun Y, Cheng J. 2002. Hydrolysis of lignocellulosic materials for ethanol production: a review. Bioresour. Technol. 83:1-11.
    • (2002) Bioresour. Technol. , vol.83 , pp. 1-11
    • Sun, Y.1    Cheng, J.2
  • 4
    • 0022386956 scopus 로고
    • Microbial xylanolytic systems
    • Biely P. 1985. Microbial xylanolytic systems. Trends Biotechnol. 3:286- 290.
    • (1985) Trends Biotechnol. , vol.3
    • Biely, P.1
  • 6
    • 0000136305 scopus 로고
    • Chemistry of cell wall polysaccharides
    • Preiss J (ed), Carbohydrates structure and function Academic Press, New York, NY
    • Aspinall GO. 1980. Chemistry of cell wall polysaccharides, p 473-500. In Preiss J (ed), The biochemistry of plants (a comprehensive treatise), vol 3. Carbohydrates: structure and function. Academic Press, New York, NY.
    • (1980) The biochemistry of plants (a comprehensive treatise) , vol.3 , pp. 473-500
    • Aspinall, G.O.1
  • 7
    • 0037207032 scopus 로고    scopus 로고
    • Optimization of xylanase production by Bacillus circulans D1 in submerged fermentation using response surface methodology
    • Bocchini DA, Alves-Prado HF, Baida LC, Roberto IC, Gomes E, Da- Silva R. 2002. Optimization of xylanase production by Bacillus circulans D1 in submerged fermentation using response surface methodology. Process Biochem. 38:727-731.
    • (2002) Process Biochem. , vol.38 , pp. 727-731
    • Bocchini, D.A.1    Alves-Prado, H.F.2    Baida, L.C.3    Roberto, I.C.4    Gomes, E.5    Da-Silva, R.6
  • 8
    • 77955569621 scopus 로고    scopus 로고
    • Novel bifunctional α-Larabinofuranosidase/ xylobiohydrolase (ABF3) from Penicillium purpurogenum
    • Ravanal MC, Callegari E, Eyzaguirre J. 2010. Novel bifunctional α-Larabinofuranosidase/ xylobiohydrolase (ABF3) from Penicillium purpurogenum. Appl. Environ. Microbiol. 76:5247-5253.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 5247-5253
    • Ravanal, M.C.1    Callegari, E.2    Eyzaguirre, J.3
  • 10
    • 79551681003 scopus 로고    scopus 로고
    • Effect of endoxylanase and α-L-arabinofuranosidase supplementation on the enzymatic hydrolysis of steam exploded wheat straw
    • Alvira P, Negro MJ, Ballesteros M. 2011. Effect of endoxylanase and α-L-arabinofuranosidase supplementation on the enzymatic hydrolysis of steam exploded wheat straw. Bioresour. Technol. 102:4552- 4558.
    • (2011) Bioresour. Technol. , vol.102
    • Alvira, P.1    Negro, M.J.2    Ballesteros, M.3
  • 11
    • 78650517371 scopus 로고    scopus 로고
    • Catalytic properties of Talaromyces thermophilus α-L-arabinofuranosidase and its synergistic action with immobilized endo-β-1,4-xylanase
    • Guerfali M, Gargouri A, Belghith H. 2011. Catalytic properties of Talaromyces thermophilus α-L-arabinofuranosidase and its synergistic action with immobilized endo-β-1,4-xylanase. J. Mol. Catal. B Enzym. 68:192- 199.
    • (2011) J. Mol. Catal. B Enzym. , vol.68
    • Guerfali, M.1    Gargouri, A.2    Belghith, H.3
  • 12
    • 33644789042 scopus 로고    scopus 로고
    • α-L-Arabinofuranosidases: the potential applications in biotechnology
    • Numan MT, Bhosle NB. 2006. α-L-Arabinofuranosidases: the potential applications in biotechnology. J. Ind. Microbiol. Biotechnol. 33:247-260.
    • (2006) J. Ind. Microbiol. Biotechnol. , vol.33 , pp. 247-260
    • Numan, M.T.1    Bhosle, N.B.2
  • 13
    • 50349083934 scopus 로고    scopus 로고
    • α-LArabinofuranosidase from Streptomyces sp. PC22: purification, characterization and its synergistic action with xylanolytic enzymes in the degradation of xylan and agricultural residues Bioresour
    • Raweesri P, Riangrungrojana P, Pinphanichakarn P. 2008. α-LArabinofuranosidase from Streptomyces sp. PC22: purification, characterization and its synergistic action with xylanolytic enzymes in the degradation of xylan and agricultural residues. Bioresour. Technol. 99:8981-8986.
    • (2008) Technol. , vol.99 , pp. 8981-8986
    • Raweesri, P.1    Riangrungrojana, P.2    Pinphanichakarn, P.3
  • 14
    • 0037457313 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of water-soluble wheat arabinoxylan. 1. Synergy between α-L-arabinofuranosidases, endo-1,4-β-xylanases, and β-xylosidase activities
    • Sørensen HR, Meyer AS, Pedersen S. 2003. Enzymatic hydrolysis of water-soluble wheat arabinoxylan. 1. Synergy between α-L-arabinofuranosidases, endo-1,4-β-xylanases, and β-xylosidase activities. Biotechnol. Bioeng. 81:726 -731.
    • (2003) Biotechnol. Bioeng. , vol.81
    • Sørensen, H.R.1    Meyer, A.S.2    Pedersen, S.3
  • 16
    • 0028949381 scopus 로고
    • Thermal asymmetric interlaced PCR: automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking
    • Liu YG, Whittier RF. 1995. Thermal asymmetric interlaced PCR: automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking. Genomics 25:674-681.
    • (1995) Genomics , vol.25 , pp. 674-681
    • Liu, Y.G.1    Whittier, R.F.2
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 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
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 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
    • Bradford, M.M.1
  • 19
    • 0028170281 scopus 로고
    • Purification and characterization of an α-L-arabinofuranosidase from Streptomyces lividan 66 and DNA sequence of the gene (abfA)
    • Manin C, Shareek F, Morosoli R, Kluepfel D. 1994. Purification and characterization of an α-L-arabinofuranosidase from Streptomyces lividan 66 and DNA sequence of the gene (abfA). Biochem. J. 302:443- 449.
    • (1994) Biochem. J. , vol.302
    • Manin, C.1    Shareek, F.2    Morosoli, R.3    Kluepfel, D.4
  • 20
    • 77954887963 scopus 로고    scopus 로고
    • Gene cloning, expression, and characterization of a family 51 α-l-arabinofuranosidase from Streptomyces sp
    • Shi P, Li N, Yang P, Wang Y, Luo H, Bai Y, Yao B. 2010. Gene cloning, expression, and characterization of a family 51 α-l-arabinofuranosidase from Streptomyces sp. S9. Appl. Biochem. Biotechnol. 162:707-718.
    • (2010) S9. Appl. Biochem. Biotechnol. , vol.162 , pp. 707-718
    • Shi, P.1    Li, N.2    Yang, P.3    Wang, Y.4    Luo, H.5    Bai, Y.6    Yao, B.7
  • 21
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller GL. 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31:426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 22
    • 79551476044 scopus 로고    scopus 로고
    • Characterization of a novel β-xylosidase, XylC, from Thermoanaerobacterium saccharolyticum JW/SL-YS485
    • Shao W, Xue Y, Wu A, Kataeva I, Pei J, Wu H, Wiegel J. 2011. Characterization of a novel β-xylosidase, XylC, from Thermoanaerobacterium saccharolyticum JW/SL-YS485. Appl. Environ. Microbiol. 77:719-726.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 719-726
    • Shao, W.1    Xue, Y.2    Wu, A.3    Kataeva, I.4    Pei, J.5    Wu, H.6    Wiegel, J.7
  • 23
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H, Burk D. 1934. The determination of enzyme dissociation constants. J. Am. Chem. Soc. 56:658-666.
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 24
    • 33846860196 scopus 로고    scopus 로고
    • Cloning and overexpression of a Paenibacillus β-glucanase in Pichia pastoris: purification and characterization of the recombinant enzyme
    • Yang P, Shi P, Wang Y, Bai Y, Meng K, Luo H, Yuan T, Yao B. 2007. Cloning and overexpression of a Paenibacillus β-glucanase in Pichia pastoris: purification and characterization of the recombinant enzyme. J. Microbiol. Biotechnol. 17:58-66.
    • (2007) J. Microbiol. Biotechnol. , vol.17 , pp. 58-66
    • Yang, P.1    Shi, P.2    Wang, Y.3    Bai, Y.4    Meng, K.5    Luo, H.6    Yuan, T.7    Yao, B.8
  • 25
    • 0034652374 scopus 로고    scopus 로고
    • Purification, characterization and gene cloning of two α-L-arabinofuranosidases from Streptomyces chartreusis GS901
    • Matsuo N, Kaneko S, Kuno A, Kobayashi H, Kusakabe I. 2000. Purification, characterization and gene cloning of two α-L-arabinofuranosidases from Streptomyces chartreusis GS901. Biochem. J. 346:9 -15.
    • (2000) Biochem. J. , vol.346
    • Matsuo, N.1    Kaneko, S.2    Kuno, A.3    Kobayashi, H.4    Kusakabe, I.5
  • 26
    • 4344653896 scopus 로고    scopus 로고
    • Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan: reconstitution of the in vivo system from recombinant enzymes
    • Adelsberger H, Hertel C, Glawischnig E, Zverlov VV, Schwarz WH. 2004. Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan: reconstitution of the in vivo system from recombinant enzymes. Microbiology 150:2257-2266.
    • (2004) Microbiology , vol.150 , pp. 2257-2266
    • Adelsberger, H.1    Hertel, C.2    Glawischnig, E.3    Zverlov, V.V.4    Schwarz, W.H.5
  • 27
    • 78650820845 scopus 로고    scopus 로고
    • Characterization of a Paenibacillus woosongensis β-xylosidase/α-arabinofuranosidase produced by recombinant Escherichia coli
    • Kim YA, Yoon KH. 2010. Characterization of a Paenibacillus woosongensis β-xylosidase/α-arabinofuranosidase produced by recombinant Escherichia coli. J. Microbiol. Biotechnol. 20:1711-1716.
    • (2010) J. Microbiol. Biotechnol. , vol.20 , pp. 1711-1716
    • Kim, Y.A.1    Yoon, K.H.2
  • 28
    • 0025818617 scopus 로고
    • Sequencing and expression of the Butyrivibrio fibrisolvens xylB gene encoding a novel bifunctional protein with β-D-xylosidase and α-L-arabinofuranosidase activities
    • Utt EA, Eddy CK, Keshav KF, Ingram LO. 1991. Sequencing and expression of the Butyrivibrio fibrisolvens xylB gene encoding a novel bifunctional protein with β-D-xylosidase and α-L-arabinofuranosidase activities. Appl. Environ. Microbiol. 57:1227-1234.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 1227-1234
    • Utt, E.A.1    Eddy, C.K.2    Keshav, K.F.3    Ingram, L.O.4
  • 30
    • 78649442942 scopus 로고    scopus 로고
    • Substrate specificity of three recombinant α-L-arabinofuranosidases from Bifidobacterium adolescentis and their divergent action on arabinoxylan and arabinoxylan oligosaccharides
    • Lagaert S, Pollet A, Delcour JA, Lavigne R, Courtin CM, Volckaert G. 2010. Substrate specificity of three recombinant α-L-arabinofuranosidases from Bifidobacterium adolescentis and their divergent action on arabinoxylan and arabinoxylan oligosaccharides. Biochem. Biophys. Res. Commun. 402:644-650.
    • (2010) Biochem. Biophys. Res. Commun. , vol.402 , pp. 644-650
    • Lagaert, S.1    Pollet, A.2    Delcour, J.A.3    Lavigne, R.4    Courtin, C.M.5    Volckaert, G.6
  • 31
    • 50249172181 scopus 로고    scopus 로고
    • Characterization of a modular enzyme of exo-1,5-α-L-arabinofuranosidase and arabinan binding module from Streptomyces avermitilis NBRC14893
    • Ichinose H, Yoshida M, Fujimoto Z, Kaneko S. 2008. Characterization of a modular enzyme of exo-1,5-α-L-arabinofuranosidase and arabinan binding module from Streptomyces avermitilis NBRC14893. Appl. Microbiol. Biotechnol. 80:399-408.
    • (2008) Appl. Microbiol. Biotechnol. , vol.80 , pp. 399-408
    • Ichinose, H.1    Yoshida, M.2    Fujimoto, Z.3    Kaneko, S.4
  • 32
    • 84857626431 scopus 로고    scopus 로고
    • Biochemical and kinetic characterization of GH43 β-D-xylosidase/α-L-arabinofuranosidase and GH30 α-L-arabinofuranosidase/β-D-xylosidase from rumen metagenome
    • Zhou J, Bao L, Chang L, Zhou Y, Lu H. 2012. Biochemical and kinetic characterization of GH43 β-D-xylosidase/α-L-arabinofuranosidase and GH30 α-L-arabinofuranosidase/β-D-xylosidase from rumen metagenome. J. Ind. Microbiol. Biotechnol. 39:143-152.
    • (2012) J. Ind. Microbiol. Biotechnol. , vol.39 , pp. 143-152
    • Zhou, J.1    Bao, L.2    Chang, L.3    Zhou, Y.4    Lu, H.5
  • 33
    • 0037249430 scopus 로고    scopus 로고
    • A role of xylanase, α-L-arabinofuranosidase, and xylosidase in xylan degradation
    • Rahman AKMS, Sugitani N, Hatsu M, Takamizawa K. 2003. A role of xylanase, α-L-arabinofuranosidase, and xylosidase in xylan degradation. Can. J. Microbiol. 49:58-64.
    • (2003) Can. J. Microbiol. , vol.49 , pp. 58-64
    • Rahman, A.K.M.S.1    Sugitani, N.2    Hatsu, M.3    Takamizawa, K.4
  • 34
    • 66349118920 scopus 로고    scopus 로고
    • Purification and characterization of a glycoside hydrolase family 43 β-xylosidase from Geobacillus thermoleovorans IT-08
    • Wagschal K, Heng C, Lee CC, Robertson GH, Orts WJ, Wong DW. 2009. Purification and characterization of a glycoside hydrolase family 43 β-xylosidase from Geobacillus thermoleovorans IT-08. Appl. Biochem. Biotechnol. 155:304 -313.
    • (2009) Appl. Biochem. Biotechnol. , vol.155
    • Wagschal, K.1    Heng, C.2    Lee, C.C.3    Robertson, G.H.4    Orts, W.J.5    Wong, D.W.6
  • 35
    • 0027497465 scopus 로고
    • Degradation of different [(glucurono) arabino] xylans by a combination of purified xylan-degrading enzymes
    • Kormelink FJM, Voragen AGJ. 1993. Degradation of different [(glucurono) arabino] xylans by a combination of purified xylan-degrading enzymes. Appl. Microbiol. Biotechnol. 38:688-695.
    • (1993) Appl. Microbiol. Biotechnol. , vol.38 , pp. 688-695
    • Kormelink, F.J.M.1    Voragen, A.G.J.2


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