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Volumn 98, Issue 16, 2014, Pages 7051-7060

A thermophilic endo-1,4-β-glucanase from Talaromyces emersonii CBS394.64 with broad substrate specificity and great application potentials

Author keywords

Broad substrate specificity; Endo 1,4 glucanase; Talaromyces emersonii; Thermophilic

Indexed keywords

ENZYME ACTIVITY; METAL IONS; SODIUM DODECYL SULFATE; TEXTILE INDUSTRY;

EID: 84905966683     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-014-5680-0     Document Type: Article
Times cited : (42)

References (34)
  • 1
    • 0028946812 scopus 로고
    • Purification and characterization of a protease-resistant cellulase from Aspergillus niger
    • Akiba S, Kimura Y, Yamamoto K, Kumagai H (1995) Purification and characterization of a protease-resistant cellulase from Aspergillus niger. J Ferment Bioeng 79:125-130
    • (1995) J Ferment Bioeng , vol.79 , pp. 125-130
    • Akiba, S.1    Kimura, Y.2    Yamamoto, K.3    Kumagai, H.4
  • 2
    • 76449100768 scopus 로고    scopus 로고
    • Extremely acidic β-1, 4-glucanase, CelA4, from thermoacidophilic Alicyclobacillus sp. A4 with high protease resistance and potential as a pig feed additive
    • Bai Y, Wang J, Zhang Z, Shi P, Luo H, Huang H, Feng Y, Yao B (2010a) Extremely acidic β-1, 4-glucanase, CelA4, from thermoacidophilic Alicyclobacillus sp. A4 with high protease resistance and potential as a pig feed additive. J Agric Food Chem 58:1970-1975
    • (2010) J Agric Food Chem , vol.58 , pp. 1970-1975
    • Bai, Y.1    Wang, J.2    Zhang, Z.3    Shi, P.4    Luo, H.5    Huang, H.6    Feng, Y.7    Yao, B.8
  • 3
    • 77952890103 scopus 로고    scopus 로고
    • A novel family 9 β-1,3 (4)-glucanase from thermoacidophilic Alicyclobacillus sp. A4 with potential applications in the brewing industry
    • Bai Y, Wang J, Zhang Z, Shi P, Luo H, Huang H, Luo C, Yao B (2010b) A novel family 9 β-1,3 (4)-glucanase from thermoacidophilic Alicyclobacillus sp. A4 with potential applications in the brewing industry. Appl Microbiol Biotechnol 87:251-259
    • (2010) Appl Microbiol Biotechnol , vol.87 , pp. 251-259
    • Bai, Y.1    Wang, J.2    Zhang, Z.3    Shi, P.4    Luo, H.5    Huang, H.6    Luo, C.7    Yao, B.8
  • 4
    • 0032590072 scopus 로고    scopus 로고
    • An endoglucanase, eg1A, from the hyperthermophilic archaeon Pyrococcus furiosus hydrolyzes β-1,4 bonds in mixed-linkage (1→3),(1→4)- β-D- glucans and cellulose
    • Bauer MW, Driskill LE, Callen W, Snead MA, Mathur EJ, Kelly RM (1999) An endoglucanase, EglA, from the hyperthermophilic Archaeon Pyrococcus furiosus hydrolyzes β-1,4 bonds in mixed-linkage (1→3), (1→4)-β-d- glucans and cellulose. J Bacteriol 181:284-290 (Pubitemid 29013682)
    • (1999) Journal of Bacteriology , vol.181 , Issue.1 , pp. 284-290
    • Bauer, M.W.1    Driskill, L.E.2    Callen, W.3    Snead, M.A.4    Mathur, E.J.5    Kelly, R.M.6
  • 5
    • 0032403607 scopus 로고    scopus 로고
    • Purification, characterization, and molecular analysis of thermostable cellulases CelA and CelB from Thermotoga neapolitana
    • Bok J-D, Yernool DA, Eveleigh DE (1998) Purification, characterization, and molecular analysis of thermostable cellulases CelA and CelB from Thermotoga neapolitana. Appl Environ Microbiol 64:4774-4781 (Pubitemid 28557838)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.12 , pp. 4774-4781
    • Bok, J.-D.1    Yernool, D.A.2    Eveleigh, D.E.3
  • 6
    • 33845688815 scopus 로고    scopus 로고
    • Characterization of a β-glucanase produced by Rhizopus microsporus var. microsporus, and its potential for application in the brewing industry
    • Celestino K, Cunha R, Felix C (2006) Characterization of a β-glucanase produced by Rhizopus microsporus var. microsporus, and its potential for application in the brewing industry. BMC Biochem 7:23
    • (2006) BMC Biochem , vol.7 , pp. 23
    • Celestino, K.1    Cunha, R.2    Felix, C.3
  • 7
    • 0034107851 scopus 로고    scopus 로고
    • Simultaneous production of high activities of thermostable endoglucanase and β-glucosidase by the wild thermophilic fungus Thermoascus aurantiacus
    • Gomes I, Gomes J, Gomes D, Steiner W (2000) Simultaneous production of high activities of thermostable endoglucanase and β-glucosidase by the wild thermophilic fungus Thermoascus aurantiacus. Appl Microbiol Biotechnol 53:461-468 (Pubitemid 30236121)
    • (2000) Applied Microbiology and Biotechnology , vol.53 , Issue.4 , pp. 461-468
    • Gomes, I.1    Gomes, J.2    Gomes, D.J.3    Steiner, W.4
  • 8
    • 9744263969 scopus 로고    scopus 로고
    • Three-dimensional structure of a thermostable native cellobiohydrolase, CBH IB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii
    • DOI 10.1111/j.1432-1033.2004.04409.x
    • Grassick A, Murray PG, Thompson R, Collins CM, Byrnes L, Birrane G, Higgins TM, Tuohy MG (2004) Three-dimensional structure of a thermostable native cellobiohydrolase, CBH IB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii. Eur J Biochem 271:4495-4506 (Pubitemid 39585212)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.22 , pp. 4495-4506
    • Grassick, A.1    Murray, P.G.2    Thompson, R.3    Collins, C.M.4    Byrnes, L.5    Birrane, G.6    Higgins, T.M.7    Tuohy, M.G.8
  • 10
    • 33846125000 scopus 로고    scopus 로고
    • Cloning and functional expression of thermostable β-glucosidase gene from Thermoascus aurantiacus
    • DOI 10.1007/s00253-006-0618-9
    • Hong J, Tamaki H, Kumagai H (2007) Cloning and functional expression of thermostable β-glucosidase gene from Thermoascus aurantiacus. Appl Microbiol Biotechnol 73:1331-1339 (Pubitemid 46089506)
    • (2007) Applied Microbiology and Biotechnology , vol.73 , Issue.6 , pp. 1331-1339
    • Hong, J.1    Tamaki, H.2    Kumagai, H.3
  • 11
    • 1642521928 scopus 로고    scopus 로고
    • Cloning of a gene encoding thermostable cellobiohydrolase from Thermoascus aurantiacus and its expression in yeast
    • DOI 10.1007/s00253-003-1379-3
    • Hong J, Tamaki H, Yamamoto K, Kumagai H (2003a) Cloning of a gene encoding thermostable cellobiohydrolase from Thermoascus aurantiacus and its expression in yeast. Appl Microbiol Biotechnol 63:42-50 (Pubitemid 38130260)
    • (2003) Applied Microbiology and Biotechnology , vol.63 , Issue.1 , pp. 42-50
    • Hong, J.1    Tamaki, H.2    Yamamoto, K.3    Kumagai, H.4
  • 12
    • 0038373628 scopus 로고    scopus 로고
    • Cloning of a gene encoding a thermo-stable endo-β-1,4-glucanase from Thermoascus aurantiacus and its expression in yeast
    • DOI 10.1023/A:1023072311980
    • Hong J, Tamaki H, Yamamoto K, Kumagai H (2003b) Cloning of a gene encoding a thermo-stable endo-β-1,4-glucanase from Thermoascus aurantiacus and its expression in yeast. Biotechnol Lett 25:657-661 (Pubitemid 36536571)
    • (2003) Biotechnology Letters , vol.25 , Issue.8 , pp. 657-661
    • Hong, J.1    Tamaki, H.2    Yamamoto, K.3    Kumagai, H.4
  • 13
    • 77449087500 scopus 로고    scopus 로고
    • Structure of hyperthermophilic endocellulase from Pyrococcus horikoshii
    • Kim HW, Ishikawa K (2010) Structure of hyperthermophilic endocellulase from Pyrococcus horikoshii. Proteins 78:496-500
    • (2010) Proteins , vol.78 , pp. 496-500
    • Kim, H.W.1    Ishikawa, K.2
  • 14
    • 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
  • 15
    • 36148939054 scopus 로고    scopus 로고
    • Lignocellulose conversion: An introduction to chemistry, process and economics
    • Lange JP (2007) Lignocellulose conversion: an introduction to chemistry, process and economics. Biofuel Bioprod Bior 1:39-48
    • (2007) Biofuel Bioprod Bior , vol.1 , pp. 39-48
    • Lange, J.P.1
  • 16
    • 84867788061 scopus 로고    scopus 로고
    • Cellulases from thermophilic fungi: Recent insights and biotechnological potential
    • Li D-C, Li A-N, Papageorgiou AC (2011) Cellulases from thermophilic fungi: recent insights and biotechnological potential. Enzyme Res 2011:308730
    • (2011) Enzyme Res , vol.2011 , pp. 308730
    • Li, D.-C.1    Li, A.-N.2    Papageorgiou, A.C.3
  • 17
    • 80051593748 scopus 로고    scopus 로고
    • Expression, purification and characterization of two thermostable endoglucanases cloned from a lignocellulosic decomposing fungi Aspergillus fumigatus Z5 isolated from compost
    • Liu D, Zhang R, Yang X, Xu Y, Tang Z, Tian W, Shen Q (2011) Expression, purification and characterization of two thermostable endoglucanases cloned from a lignocellulosic decomposing fungi Aspergillus fumigatus Z5 isolated from compost. Protein Expr Purif 79:176-186
    • (2011) Protein Expr Purif , vol.79 , pp. 176-186
    • Liu, D.1    Zhang, R.2    Yang, X.3    Xu, Y.4    Tang, Z.5    Tian, W.6    Shen, Q.7
  • 18
    • 0028949381 scopus 로고
    • Thermal asymmetric interlaced PCR: Automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking
    • Liu Y-G, 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
  • 19
    • 0037125126 scopus 로고    scopus 로고
    • The 1.62 Å structure of Thermoascus aurantiacus endoglucanase: Completing the structural picture of subfamilies in glycoside hydrolase family 5
    • DOI 10.1016/S0014-5793(02)02954-X, PII S001457930202954X
    • Lo Leggio L, Larsen S (2002) The 1.62 A structure of Thermoascus aurantiacus endoglucanase: completing the structural picture of subfamilies in glycoside hydrolase family 5. FEBS Lett 523:103-108 (Pubitemid 34786067)
    • (2002) FEBS Letters , vol.523 , Issue.1-3 , pp. 103-108
    • Lo, L.L.1    Larsen, S.2
  • 20
  • 21
    • 0022626555 scopus 로고
    • Optimization of fermentation conditions for thermostable cellulase production by Thielavia terrestris
    • Margaritis A, Merchant RF (1986) Optimization of fermentation conditions for thermostable cellulase production by Thielavia terrestris. J Ind Microbiol 1:149-156 (Pubitemid 16096146)
    • (1986) Journal of Industrial Microbiology , vol.1 , Issue.3 , pp. 149-156
    • Margaritis, A.1    Merchant, R.F.2
  • 22
    • 0347700479 scopus 로고    scopus 로고
    • Effects of xylanase and β-glucanase addition on performance, nutrient digestibility, and physico-chemical conditions in the small intestine contents and caecal microflora of broiler chickens fed a wheat and barley-based diet
    • Mathlouthi N, Mallet S, Saulnier L, Quemener B, Larbier M (2002) Effects of xylanase and β-glucanase addition on performance, nutrient digestibility, and physico-chemical conditions in the small intestine contents and caecal microflora of broiler chickens fed a wheat and barley-based diet. Anim Res 51:395-406 (Pubitemid 135712125)
    • (2002) Animal Research , vol.51 , Issue.5 , pp. 395-406
    • Mathlouthi, N.1    Mallet, S.2    Saulnier, L.3    Ouemener, B.4    Larbier, M.5
  • 23
    • 0025729215 scopus 로고
    • Subsite structure of Saccharomycopsis α-amylase secreted from Saccharomyces cerevisiae
    • Matsui I, Ishikawa K, Matsui E, Miyairi S, Fukui S, Honda K (1991) Subsite structure of Saccharomycopsis α-amylase secreted from Saccharomyces cerevisiae. J Biochem 109:566-569
    • (1991) J Biochem , vol.109 , pp. 566-569
    • Matsui, I.1    Ishikawa, K.2    Matsui, E.3    Miyairi, S.4    Fukui, S.5    Honda, K.6
  • 24
    • 0242383940 scopus 로고    scopus 로고
    • Catalytic properties and mode of action of three endo-β-glucanases from Talaromyces emersonii on soluble β-1,4- and β-1,3;1,4-linked glucans
    • DOI 10.1016/S0141-8130(03)00080-1
    • McCarthy T, Hanniffy O, Savage AV, Tuohy MG (2003) Catalytic properties and mode of action of three endo-β-glucanases from Talaromyces emersonii on soluble β-1, 4-and β-1, 3; 1, 4-linked glucans. Int J Biol Macromol 33:141-148 (Pubitemid 37346369)
    • (2003) International Journal of Biological Macromolecules , vol.33 , Issue.1-3 , pp. 141-148
    • McCarthy, T.1    Hanniffy, O.2    Savage, A.V.3    Tuohy, M.G.4
  • 25
    • 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
  • 26
    • 0021911424 scopus 로고
    • Isolation and characterization of the 1,4-β-D-glucan glucanohydrolases of Talaromyces emersonii
    • Moloney A, McCrae S, Wood T, Coughlan M (1985) Isolation and characterization of the 1, 4-β-D-glucan glucanohydrolases of Talaromyces emersonii. Biochem J 225:365-374 (Pubitemid 15162182)
    • (1985) Biochemical Journal , vol.225 , Issue.2 , pp. 365-374
    • Moloney, A.P.1    McCrae, S.I.2    Wood, M.3    Coughlan, M.P.4
  • 28
    • 0025913198 scopus 로고
    • Thermostable cellobiohydrolase from the thermophilic eubacterium Thermotoga sp. strain FjSS3-B. 1. Purification and properties
    • Ruttersmith LD, Daniel RM (1991) Thermostable cellobiohydrolase from the thermophilic eubacterium Thermotoga sp. strain FjSS3-B. 1. Purification and properties. Biochem J 277:887-890
    • (1991) Biochem J , vol.277 , pp. 887-890
    • Ruttersmith, L.D.1    Daniel, R.M.2
  • 29
    • 0029740205 scopus 로고    scopus 로고
    • Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose
    • DOI 10.1021/bi9604439
    • Sakon J, Adney WS, Himmel ME, Thomas SR, Karplus PA (1996) Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose. Biochemistry 35:10648-10660 (Pubitemid 26279644)
    • (1996) Biochemistry , vol.35 , Issue.33 , pp. 10648-10660
    • Sakon, J.1    Adney, W.S.2    Himmel, M.E.3    Thomas, S.R.4    Andrew, K.P.5
  • 30
    • 0032212169 scopus 로고    scopus 로고
    • The use of capillary viscometry, reducing end-group analysis, and size exclusion chromatography combined with multi-angle laser light scattering to characterize endo-1,4-β-d-glucanases on carboxymethylcellulose: A comparative evaluation of the three methods
    • DOI 10.1016/S0141-0229(98)00052-0, PII S0141022998000520
    • Vlasenko EY, Ryan AI, Shoemaker CF, Shoemaker SP (1998) The use of capillary viscometry, reducing end-group analysis, and size exclusion chromatography combined with multi-angle laser light scattering to characterize endo-1, 4-β-D-glucanases on carboxymethylcellulose: a comparative evaluation of the three methods. Enzym Microb Technol 23:350-359 (Pubitemid 28479849)
    • (1998) Enzyme and Microbial Technology , vol.23 , Issue.6 , pp. 350-359
    • Vlasenko, E.Y.1    Ryan, A.I.2    Shoemaker, C.F.3    Shoemaker, S.P.4
  • 31
    • 36349023786 scopus 로고    scopus 로고
    • Characterization of a thermostable and acidic-tolerable β-Glucanase from aerobic fungi Trichoderma koningii ZJU-T
    • DOI 10.1111/j.1750-3841.2007.00549.x
    • Wang JL, Ruan H, Zhang HF, Zhang Q, Zhang HB, He GQ, Shen SR (2007) Characterization of a thermostable and acidic-tolerable β-glucanase from aerobic fungi Trichoderma koningii ZJU-T. J Food Sci 72:C452-C456 (Pubitemid 350150707)
    • (2007) Journal of Food Science , vol.72 , Issue.9
    • Wang, J.-L.1    Ruan, H.2    Zhang, H.-F.3    Zhang, Q.4    Zhang, H.-B.5    He, G.-Q.6    Shen, S.-R.7
  • 32
    • 67649815010 scopus 로고    scopus 로고
    • Cellulases and biofuels
    • Wilson DB (2009) Cellulases and biofuels. Curr Opin Biotechnol 20:295-299
    • (2009) Curr Opin Biotechnol , vol.20 , pp. 295-299
    • Wilson, D.B.1
  • 34
    • 85004235287 scopus 로고
    • Purification and properties of a new endo-cellulase from Robillarda sp. Y-20
    • Yoshigi N, Taniguchi H, Sasaki T (1988) Purification and properties of a new endo-cellulase from Robillarda sp. Y-20. Agric Biol Chem 52:1389-1396
    • (1988) Agric Biol Chem , vol.52 , pp. 1389-1396
    • Yoshigi, N.1    Taniguchi, H.2    Sasaki, T.3


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