메뉴 건너뛰기




Volumn 6, Issue 1, 2013, Pages

The carbohydrate-binding module of xylanase from Nonomuraea flexuosa decreases its non-productive adsorption on lignin

Author keywords

Adsorption; Carbohydrate binding module; Xylan; Xylanase

Indexed keywords

CARBOHYDRATE BINDING MODULES; CORE PROTEINS; FAMILY 11; FAMILY II; FERMENTABLE SUGARS; LIGNOCELLULOSIC MATERIAL; LIMITING STEP; NONSPECIFIC ADSORPTION; WHEAT STRAWS; XYLAN; XYLANASES;

EID: 84873021244     PISSN: 17546834     EISSN: None     Source Type: Journal    
DOI: 10.1186/1754-6834-6-18     Document Type: Article
Times cited : (31)

References (45)
  • 1
    • 0027535915 scopus 로고
    • Synergism of Trichoderma Reesei cellulases while degrading different celluloses
    • Synergism of Trichoderma reesei cellulases while degrading different celluloses. Nidetzky B, Kayn M, Macarron R, Steiner W, Biotechnol Lett 1993 15 71 76 10.1007/BF00131556 (Pubitemid 23075001)
    • (1993) Biotechnology Letters , vol.15 , Issue.1 , pp. 71-76
    • Nidetzky, B.1    Hayn, M.2    Macarron, R.3    Steiner, W.4
  • 2
    • 9244252053 scopus 로고    scopus 로고
    • Helicoidal pattern in secondary cell walls and possible role of xylans in their construction
    • DOI 10.1016/j.crvi.2004.04.008, PII S1631069104002094
    • Helicoidal pattern in secondary cell walls and possible role of xylans in their construction. Reis D, Vian B, Comptes Rendus Biologies 2004 327 785 790 10.1016/j.crvi.2004.04.008 15587069 (Pubitemid 39549861)
    • (2004) Comptes Rendus - Biologies , vol.327 , Issue.9-10 , pp. 785-790
    • Reis, D.1    Vian, B.2
  • 3
    • 1542615147 scopus 로고    scopus 로고
    • Effect of Xylan and Lignin Removal by Batch and Flowthrough Pretreatment on the Enzymatic Digestibility of Corn Stover Cellulose
    • DOI 10.1002/bit.20043
    • Effect of xylan and lignin removal by batch and flowthrough pretreatment on the enzymatic digestibility of corn stover cellulose. Yang B, Wyman CE, Biotechnol Bioeng 2004 86 88 95 10.1002/bit.20043 15007845 (Pubitemid 38339395)
    • (2004) Biotechnology and Bioengineering , vol.86 , Issue.1 , pp. 88-95
    • Yang, B.1    Wyman, C.E.2
  • 4
    • 33947430562 scopus 로고    scopus 로고
    • Effect of hemicellulose and lignin removal on enzymatic hydrolysis of steam pretreated corn stover
    • DOI 10.1016/j.biortech.2006.09.003, PII S0960852406004573
    • Effect of hemicellulose and lignin removal on enzymatic hydrolysis of steam pretreated corn stover. Öhgren K, Bura R, Saddler J, Zacchi G, Bioresour Technol 2007 98 2503 2510 10.1016/j.biortech.2006.09.003 17113771 (Pubitemid 46453471)
    • (2007) Bioresource Technology , vol.98 , Issue.13 , pp. 2503-2510
    • Ohgren, K.1    Bura, R.2    Saddler, J.3    Zacchi, G.4
  • 6
    • 0000992123 scopus 로고
    • Structural chemistry of the hemicelluloses
    • 13794843
    • Structural chemistry of the hemicelluloses. Aspinall GO, Adv Carbohydr Chem 1959 14 429 468 13794843
    • (1959) Adv Carbohydr Chem , vol.14 , pp. 429-468
    • Aspinall, G.O.1
  • 7
    • 0001781446 scopus 로고
    • Linkage of p-coumaroyl and feruloyl groups to cell-wall polysaccharides of barley straw
    • 10.1016/0008-6215(86)80038-6
    • Linkage of p-coumaroyl and feruloyl groups to cell-wall polysaccharides of barley straw. Mueller-Harvey I, Hartley RD, Harris PJ, Curzon EH, Carbohydr Res 1986 148 71 85 10.1016/0008-6215(86)80038-6
    • (1986) Carbohydr Res , vol.148 , pp. 71-85
    • Mueller-Harvey, I.1    Hartley, R.D.2    Harris, P.J.3    Curzon, E.H.4
  • 9
    • 66349091118 scopus 로고    scopus 로고
    • Effect of xylanase supplementation of cellulase on digestion of corn stover solids prepared by leading pretreatment technologies
    • 10.1016/j.biortech.2008.11.057 19386492
    • Effect of xylanase supplementation of cellulase on digestion of corn stover solids prepared by leading pretreatment technologies. Kumar R, Wyman CE, Bioresour Technol 2009 100 4203 4213 10.1016/j.biortech.2008.11.057 19386492
    • (2009) Bioresour Technol , vol.100 , pp. 4203-4213
    • Kumar, R.1    Wyman, C.E.2
  • 10
    • 80052345754 scopus 로고    scopus 로고
    • Comparison of the synergistic action of two thermostable xylanases from GH families 10 and 11 with thermostable cellulases in lignocellulose hydrolysis
    • 10.1016/j.biortech.2011.06.085 21767947
    • Comparison of the synergistic action of two thermostable xylanases from GH families 10 and 11 with thermostable cellulases in lignocellulose hydrolysis. Zhang J, Tuomainen P, Siika-aho M, Viikari L, Bioresour Technol 2011 102 9090 9095 10.1016/j.biortech.2011.06.085 21767947
    • (2011) Bioresour Technol , vol.102 , pp. 9090-9095
    • Zhang, J.1    Tuomainen, P.2    Siika-Aho, M.3    Viikari, L.4
  • 12
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-tuning polysaccharide recognition
    • DOI 10.1042/BJ20040892
    • Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Boraston AB, Bolam DN, Gilbert HJ, Davies GJ, Biochem J 2004 382 769 781 10.1042/BJ20040892 15214846 (Pubitemid 39312891)
    • (2004) Biochemical Journal , vol.382 , Issue.3 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 13
    • 14744278342 scopus 로고
    • A new model for enzymatic hydrolysis of cellulose based on the two-domain structure of cellobiohydrolase i
    • 10.1038/nbt0391-286
    • A new model for enzymatic hydrolysis of cellulose based on the two-domain structure of cellobiohydrolase I. Ståhlberg J, Johansson G, Pettersson G, Biotechnol 1991 9 286 290 10.1038/nbt0391-286
    • (1991) Biotechnol , vol.9 , pp. 286-290
    • Ståhlberg, J.1    Johansson, G.2    Pettersson, G.3
  • 14
    • 0029090730 scopus 로고
    • The non-catalytic cellulose-binding domain of a novel cellulase from Pseudomonas fluorescens subsp. cellulosa is important for the efficient hydrolysis of Avicel
    • 7639689
    • The non-catalytic cellulose-binding domain of a novel cellulase from Pseudomonas fluorescens subsp. cellulosa is important for the efficient hydrolysis of Avicel. Hall J, Black G, Ferreira L, Millward-Saddler S, Ali B, Hazlewood G, Gilbert G, Biochem J 1995 309 749 756 7639689
    • (1995) Biochem J , vol.309 , pp. 749-756
    • Hall, J.1    Black, G.2    Ferreira, L.3    Millward-Saddler, S.4    Ali, B.5    Hazlewood, G.6    Gilbert, G.7
  • 15
    • 33745161547 scopus 로고    scopus 로고
    • Carbohydrate binding modules: Biochemical properties and novel applications
    • DOI 10.1128/MMBR.00028-05
    • Carbohydrate-binding modules: biochemical properties and novel applications. Shoseyov O, Shani Z, Levy I, Microbial Mol Biol Rev 2006 70 283 295 10.1128/MMBR.00028-05 (Pubitemid 43895029)
    • (2006) Microbiology and Molecular Biology Reviews , vol.70 , Issue.2 , pp. 283-295
    • Shoseyov, O.1    Shani, Z.2    Levy, I.3
  • 16
    • 77955691535 scopus 로고    scopus 로고
    • Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis
    • 10.1002/bit.22779 20506147
    • Mechanism of initial rapid rate retardation in cellobiohydrolase catalyzed cellulose hydrolysis. Jalak J, Väljamäe P, Biotechnol Bioeng 2010 106 871 883 10.1002/bit.22779 20506147
    • (2010) Biotechnol Bioeng , vol.106 , pp. 871-883
    • Jalak, J.1    Väljamäe, P.2
  • 17
    • 73649106924 scopus 로고    scopus 로고
    • High speed atomic force microscopy visualizes processive movement of Trichoderma reesei cellobiohydrolase i on crystalline cellulose
    • 10.1074/jbc.M109.034611 19858200
    • High speed atomic force microscopy visualizes processive movement of Trichoderma reesei cellobiohydrolase I on crystalline cellulose. Igarashi K, Koivula A, Wada M, Kimura S, Penttilä M, Samejima M, J Biol Chem 2009 284 36186 36190 10.1074/jbc.M109.034611 19858200
    • (2009) J Biol Chem , vol.284 , pp. 36186-36190
    • Igarashi, K.1    Koivula, A.2    Wada, M.3    Kimura, S.4    Penttilä, M.5    Samejima, M.6
  • 18
    • 0346035834 scopus 로고    scopus 로고
    • A cellulose-binding module of the Trichoderma reesei β-mannanase Man5A increases the mannan-hydrolysis of complex substrates
    • DOI 10.1016/S0168-1656(02)00290-0, PII S0168165602002900
    • A cellulose-binding module of the Trichoderma reesei β-mannanase Man5A increases the mannan-hydrolysis of complex substrates. Hägglund P, Eriksson T, Collén A, Nerinckx W, Claeyssens M, Stålbrand H, J Biotechnol 2003 101 37 48 10.1016/S0168-1656(02)00290-0 12523968 (Pubitemid 36071449)
    • (2003) Journal of Biotechnology , vol.101 , Issue.1 , pp. 37-48
    • Hagglund, P.1    Eriksson, T.2    Collen, A.3    Nerinckx, W.4    Claeyssens, M.5    Stalbrand, H.6
  • 19
    • 77955050826 scopus 로고    scopus 로고
    • Hydrolysis of softwood by Aspergillus mannanase: Role of a carbohydrate-binding module
    • 10.1016/j.jbiotec.2010.05.012 20541570
    • Hydrolysis of softwood by Aspergillus mannanase: role of a carbohydrate-binding module. Pham TA, Berrin JG, Record E, To KA, Sigoillot JC, J Biotechnol 2010 148 163 170 10.1016/j.jbiotec.2010.05.012 20541570
    • (2010) J Biotechnol , vol.148 , pp. 163-170
    • Pham, T.A.1    Berrin, J.G.2    Record, E.3    To, K.A.4    Sigoillot, J.C.5
  • 20
    • 0003149785 scopus 로고    scopus 로고
    • Adsorption of Clostridium stercorarium xylanase A to insoluble xylan and the importance of the CBDs to xylan hydrolysis
    • DOI 10.1016/S0922-338X(97)80355-8
    • Adsorption of Clostridium stercorarium xylanase A to insoluble xylan and the importance of the CBMs to xylan hydrolysis. Sun JL, Sakka K, Karita S, Kimura T, Ohmiya K, J Ferment Bioeng 1998 85 63 68 10.1016/S0922-338X(97)80355-8 (Pubitemid 28128560)
    • (1998) Journal of Fermentation and Bioengineering , vol.85 , Issue.1 , pp. 63-68
    • Sun, J.L.1    Sakka, K.2    Karita, S.3    Kimura, T.4    Ohmiya, K.5
  • 21
  • 22
    • 0037450178 scopus 로고    scopus 로고
    • Fusion of family VI cellulose binding domains to Bacillus halodurans xylanase increases its catalytic activity and substrate-binding capacity to insoluble xylan
    • DOI 10.1016/S1381-1177(02)00226-6, PII S1381117702002266
    • Fusion of family VI cellulose binding domains to Bacillus halodurans xylanase increases its catalytic activity and substrate-binding capacity to insoluble xylan. Mangala SL, Kittur FS, Nishimoto M, Sakka K, Ohmiya K, Kitaoka M, Hayashi K, J Mol Catal B: Enzym 2003 21 221 230 10.1016/S1381-1177(02)00226-6 (Pubitemid 36057139)
    • (2003) Journal of Molecular Catalysis B: Enzymatic , vol.21 , Issue.4-6 , pp. 221-230
    • Mangala, S.L.1    Kittur, F.S.2    Nishimoto, M.3    Sakka, K.4    Ohmiya, K.5    Kitaoka, M.6    Hayashi, K.7
  • 23
    • 33846127494 scopus 로고    scopus 로고
    • Fusion of carbohydrate binding modules from Thermotoga neapolitana with a family 10 xylanase from Bacillus halodurans S7
    • DOI 10.1007/s00792-006-0023-4
    • Fusion of carbohydrate binding modules from Thermotoga neapolitana with a family 10 xylanase from Bacillus halodurans S7. Mamo G, Hatti-Kaul R, Mattiasson B, Extremopiles 2007 11 169 177 10.1007/s00792-006-0023-4 (Pubitemid 46089640)
    • (2007) Extremophiles , vol.11 , Issue.1 , pp. 169-177
    • Mamo, G.1    Hatti-Kaul, R.2    Mattiasson, B.3
  • 24
    • 0000178351 scopus 로고    scopus 로고
    • A family IIb xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity
    • DOI 10.1016/S0969-2126(99)80108-7
    • A family IIb xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity. Simpson PJ, Bolam DN, Cooper A, Ciruela A, Hazlewood GP, Gilbert HJ, Williamson MP, Structure 1999 7 853 864 10.1016/S0969-2126(99)80108-7 10425686 (Pubitemid 29329855)
    • (1999) Structure , vol.7 , Issue.7 , pp. 853-864
    • Simpson, P.J.1    Bolam, D.N.2    Cooper, A.3    Ciruela, A.4    Hazlewood, G.P.5    Gilbert, H.J.6    Williamson, M.P.7
  • 25
    • 0035957081 scopus 로고    scopus 로고
    • Evidence for synergy between family 2b carbohydrate binding modules in Cellulomonas fimi Xylanase 11A
    • DOI 10.1021/bi002564l
    • Evidence for synergy between family 2b carbohydrate binding modules in xylanase 11A. Bolam DN, Xie H, White P, Simpson PJ, Hancock SM, Williamson MP, Gilbert HJ, Biochem 2001 40 2468 2477 10.1021/bi002564l (Pubitemid 32171720)
    • (2001) Biochemistry , vol.40 , Issue.8 , pp. 2468-2477
    • Bolam, D.N.1    Xie, H.2    White, P.3    Simpson, P.J.4    Hancock, S.M.5    Williamson, M.P.6    Gilbert, H.J.7
  • 26
    • 0042063909 scopus 로고    scopus 로고
    • Fusion of family 2b carbohydrate-binding module increases the catalytic activity of a xylanase from Thermotoga maritima to soluble xylan
    • DOI 10.1016/S0014-5793(03)00803-2
    • Fusion of family 2b carbohydrate-binding module increases the catalytic activity of a xylanase from Thermotoga maritime to soluble xylan. Kittur FS, Mangala SL, Rus'd AA, Kitaoka M, Tsujibo H, Hayashi K, FEBS Lett 2003 549 147 151 10.1016/S0014-5793(03)00803-2 12914941 (Pubitemid 36959860)
    • (2003) FEBS Letters , vol.549 , Issue.1-3 , pp. 147-151
    • Kittur, F.S.1    Mangala, S.L.2    Rus'd, A.A.3    Kitaoka, M.4    Tsujibo, H.5    Hayashi, K.6
  • 27
    • 0346363683 scopus 로고    scopus 로고
    • Adsorption of Trichoderma reesei CBH I and EG II and their catalytic domains on steam pretreated softwood and isolated lignin
    • DOI 10.1016/j.jbiotec.2003.09.011
    • Adsorption of Trichoderma reesei CBHI and EGII and their catalytic domains on steam pretreated softwood and isolated lignin. Palonen H, Tjerneld F, Zacchi G, Tenkanen M, J Biotechnol 2004 107 65 72 10.1016/j.jbiotec.2003.09.011 14687972 (Pubitemid 38010270)
    • (2004) Journal of Biotechnology , vol.107 , Issue.1 , pp. 65-72
    • Palonen, H.1    Tjerneld, F.2    Zacchi, G.3    Tenkanen, M.4
  • 28
    • 80054037883 scopus 로고    scopus 로고
    • Inhibition of enzymatic hydrolysis by residual lignins from softwoodstudy of enzyme binding and inactivation on lignin-rich surface
    • 10.1002/bit.23242 21702025
    • Inhibition of enzymatic hydrolysis by residual lignins from softwoodstudy of enzyme binding and inactivation on lignin-rich surface. Rahikainen J, Mkander S, Marjamaa K, Tamminen T, Lappas A, Viikari L, Kruus K, Biotechnol Bioeng 2011 108 2823 2834 10.1002/bit.23242 21702025
    • (2011) Biotechnol Bioeng , vol.108 , pp. 2823-2834
    • Rahikainen, J.1    Mkander, S.2    Marjamaa, K.3    Tamminen, T.4    Lappas, A.5    Viikari, L.6    Kruus, K.7
  • 29
    • 79955975799 scopus 로고    scopus 로고
    • Thermostable recombinant xylanases from Nonomuraea flexuosa and Thermoascus aurantiacus show distinct properties in the hydrolysis of xylans and pretreated wheat straw
    • 10.1186/1754-6834-4-12 21592333
    • Thermostable recombinant xylanases from Nonomuraea flexuosa and Thermoascus aurantiacus show distinct properties in the hydrolysis of xylans and pretreated wheat straw. Zhang J, Siika-aho M, Puranen T, Tang M, Tenkanen M, Viikari L, Biotechnol biofuels 2011 4 12 10.1186/1754-6834-4-12 21592333
    • (2011) Biotechnol Biofuels , vol.4 , pp. 12
    • Zhang, J.1    Siika-Aho, M.2    Puranen, T.3    Tang, M.4    Tenkanen, M.5    Viikari, L.6
  • 30
    • 21344465648 scopus 로고    scopus 로고
    • Thermostable xylanases, Xyn10A and Xyn11A, from the actinomycete Nonomuraea flexuosa: Isolation of the genes and characterization of recombinant Xyn11A polypeptides produced in Trichoderma reesei
    • DOI 10.1007/s00253-004-1797-x
    • Thermostable xylanases, Xyn10A and Xyn11A, from the actinomycete Nonomuraea flexuosa: isolation of the genes and characterization of recombinant Xyn11A polypeptides produced in Trichoderma reesei. Leskinen S, Mäntylä A, Fagerström R, Vehmaanperä J, Lantto R, Paloheimo M, Suominen P, Appl Microbiol Biotechnol 2005 67 495 505 10.1007/s00253-004- 1797-x 15650852 (Pubitemid 40909596)
    • (2005) Applied Microbiology and Biotechnology , vol.67 , Issue.4 , pp. 495-505
    • Leskinen, S.1    Mantyla, A.2    Fagerstrom, R.3    Vehmaanpera, J.4    Lantto, R.5    Paloheimo, M.6    Suominen, P.7
  • 32
    • 66349095817 scopus 로고    scopus 로고
    • Access of cellulase of cellulose and lignin for poplar solids produced by leading pretreatment technologies
    • 10.1002/btpr.153
    • Access of cellulase of cellulose and lignin for poplar solids produced by leading pretreatment technologies. Kumar R, Wyman CE, Biotechnol Pro 2009 25 807 819 10.1002/btpr.153
    • (2009) Biotechnol Pro , vol.25 , pp. 807-819
    • Kumar, R.1    Wyman, C.E.2
  • 33
    • 65549171000 scopus 로고    scopus 로고
    • Cellulase adsorption and relationship to features of corn stover solids produced by leading pretreatments
    • 10.1002/bit.22258
    • Cellulase adsorption and relationship to features of corn stover solids produced by leading pretreatments. Kumar R, Wyman CE, Biotehnol Bioeng 2009 103 252 267 10.1002/bit.22258
    • (2009) Biotehnol Bioeng , vol.103 , pp. 252-267
    • Kumar, R.1    Wyman, C.E.2
  • 34
    • 78751473033 scopus 로고    scopus 로고
    • Enhancing the enzymatic hydrolysis of lignocellulosic biomass by increasing the carboxylic acid content of the associated lignin
    • 10.1002/bit.22981 21246506
    • Enhancing the enzymatic hydrolysis of lignocellulosic biomass by increasing the carboxylic acid content of the associated lignin. Nakagame S, Chandra RP, Kadla JF, Saddler JN, Biotechnol Bioeng 2011 108 538 548 10.1002/bit.22981 21246506
    • (2011) Biotechnol Bioeng , vol.108 , pp. 538-548
    • Nakagame, S.1    Chandra, R.P.2    Kadla, J.F.3    Saddler, J.N.4
  • 35
    • 83055184339 scopus 로고    scopus 로고
    • The laccase-catalyzed modification of lignin for enzymatic hydrolysis
    • 10.1016/j.enzmictec.2011.09.012 22142723
    • The laccase-catalyzed modification of lignin for enzymatic hydrolysis. Moilanen U, Kellock M, Galkin S, Viikari L, Enzyme Microb Technol 2011 49 492 498 10.1016/j.enzmictec.2011.09.012 22142723
    • (2011) Enzyme Microb Technol , vol.49 , pp. 492-498
    • Moilanen, U.1    Kellock, M.2    Galkin, S.3    Viikari, L.4
  • 36
    • 0034629241 scopus 로고    scopus 로고
    • An α-glucuronidase of Schizophyllum commune acting on polymeric xylan
    • DOI 10.1016/S0168-1656(99)00240-0, PII S0168165699002400
    • An α-glucuronidase of Schizophyllum commune acting on polymeric xylan. Tenkanen M, Siika-aho M, J Biotechnol 2000 78 149 161 10.1016/S0168-1656(99)00240-0 10725538 (Pubitemid 30139557)
    • (2000) Journal of Biotechnology , vol.78 , Issue.2 , pp. 149-161
    • Tenkanen, M.1    Siika-Aho, M.2
  • 38
    • 0141782482 scopus 로고    scopus 로고
    • Purification and characterization of a new low molecular weight endoxylanase from Penicillium capsulatum
    • DOI 10.1016/S0141-0229(03)00176-5
    • Purification and characterisation of a new low molecular weight endoxylanase from Penicillium capsulatum. Ryan SE, Nolan K, Thompson R, Gubitz GM, Savage AV, Tuohy MG, Enzyme Microbiol Technol 2003 33 775 785 10.1016/S0141-0229(03)00176-5 (Pubitemid 37123200)
    • (2003) Enzyme and Microbial Technology , vol.33 , Issue.6 , pp. 775-785
    • Ryan, S.E.1    Nolan, K.2    Thompson, R.3    Gubitz, G.M.4    Savage, A.V.5    Tuohy, M.G.6
  • 39
    • 0027131591 scopus 로고
    • High frequency one-step gene replacement in Trichoderma reesei. II. Effects of deletions of individual cellulase genes
    • DOI 10.1007/BF00279894
    • High frequency one-step gene replacement in Trichoderma reesei: effects of deletions of individual genes. Suominen P, Mäntylä A, Karhunen T, Hakola S, Nevalainen H, Mol Gen Genet 1993 241 523 530 10.1007/BF00279894 8264527 (Pubitemid 24003871)
    • (1993) Molecular and General Genetics , vol.241 , Issue.5-6 , pp. 523-530
    • Suominen, P.L.1    Mantyla, A.L.2    Karhunen, T.3    Haokla, S.4    Nevlainen, H.5
  • 40
    • 0026537453 scopus 로고
    • Interlaboratory testing of methods for assay of xylanase activity
    • 10.1016/0168-1656(92)90074-J
    • Interlaboratory testing of methods for assay of xylanase activity. Bailey MJ, Biely P, Poutanen K, J Biotechnol 1992 23 257 270 10.1016/0168-1656(92) 90074-J
    • (1992) J Biotechnol , vol.23 , pp. 257-270
    • Bailey, M.J.1    Biely, P.2    Poutanen, K.3
  • 41
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugars
    • 10.1021/ac60147a030
    • Use of dinitrosalicylic acid reagent for determination of reducing sugars. Miller GL, Anal Chem 1959 31 426 428 10.1021/ac60147a030
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 43
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 10.1038/227680a0 5432063
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Laemmli UK, Nature 1970 227 680 685 10.1038/227680a0 5432063
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 44
    • 0031723458 scopus 로고    scopus 로고
    • Adsorption of a xylanase purified from Pulpzyme HC onto alkali-lignin and crystalline cellulose
    • Adsorption of a xylanase purified from pulpzyme HC onto alkali-lignin and crystalline cellulose. Ryu K, Kim Y, Biotechnol Lett 1998 20 987 990 10.1023/A:1005498703554 (Pubitemid 28522075)
    • (1998) Biotechnology Letters , vol.20 , Issue.10 , pp. 987-990
    • Ryu, K.1    Kim, Y.2
  • 45
    • 0031963064 scopus 로고    scopus 로고
    • Hydrolysis of wheat straw by a thermostable endoxylanase: Adsorption and kinetic studies
    • DOI 10.1016/S0141-0229(97)00105-1, PII S0141022997001051
    • Hydrolysis of wheat straw by a thermostable endoxylanase: adsorption and kinetic studies. Zilliox C, Debeire P, Appl Microbiol Biotechnol 1998 22 58 63 (Pubitemid 28033406)
    • (1998) Enzyme and Microbial Technology , vol.22 , Issue.1 , pp. 58-63
    • Zilliox, C.1    Debeire, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.