Carbohydrate-binding modules (CBMs) revisited: Reduced amount of water counterbalances the need for CBMs

Biotechnology for Biofuels

Volumn 6, Issue 1, 2013, Pages

  Várnai, Anikó ^a   Siika Aho, Matti ^b   Viikari, Liisa ^a  

^a UNIVERSITY OF HELSINKI   (Finland)

^b VTT TECHNICAL RESEARCH CENTRE OF FINLAND   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE-BINDING MODULES; CATALYTIC PERFORMANCE; ENHANCED ADSORPTIONS; ENZYMATIC HYDROLYSIS OF LIGNOCELLULOSE; ENZYME-SUBSTRATE INTERACTIONS; NATURAL ENVIRONMENTS; SECOND GENERATION BIOETHANOL; SUBSTRATE CONCENTRATIONS;

ADSORPTION; BIOLOGY; CARBOHYDRATES; CELLULOSE; ENZYMATIC HYDROLYSIS; LIGNIN; SACCHARIFICATION;

SUBSTRATES;

ADSORPTION; BIOTECHNOLOGY; CARBOHYDRATE; CELLULOSE; ENZYME; ETHANOL; HYDROLYSIS; MOLECULAR ANALYSIS; POLYMER; PROTEIN;

HYPOCREA JECORINA; TRITICUM AESTIVUM;

EID: 84874208200     PISSN: 17546834     EISSN: None     Source Type: Journal    
DOI: 10.1186/1754-6834-6-30     Document Type: Article

References (42)

1. Growing America's fuel: an analysis of corn and cellulosic ethanol feasibility in the United States. Somma D, Lobkowicz H, Deason JP, Clean Techn Environ Policy 2010 12 373 380 10.1007/s10098-009-0234-3
2. Technoeconomic analysis of the dilute sulfuric acid and enzymatic hydrolysis process for the conversion of corn stover to ethanol. Aden A, Foust T, Cellulose 2009 16 535 545 10.1007/s10570-009-9327-8
3. Humbird D, Davis R, Tao L, Kinchin C, Hsu D, Aden A, Schoen P, Lukas J, Olthof B, Worley M, Sexton D, Dudgeon D, Process design and economics for biochemical conversion of lignocellulosic biomass to ethanol. NREL Technical report: 2011 NREL/TP-5100-47764. [ http://www.nrel.gov/biomass/pdfs/47764.pdf
4. Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components. Quinlan RJ, Sweeney MD, Leggio LL, Otten H, Poulsen JCN, Johansen KS, Krogh KBRM, Jørgensen CI, Tovborg M, Anthonsen A, Tryfona T, Walter CP, Dupree P, Xu F, Davies GJ, Walton PH, Proc Natl Acad Sci USA 2011 108 15079 15084 10.1073/pnas.1105776108 21876164
5. The Carbohydrate-Active enZYmes Database: http://www.cazy.org
6. Cellulosomes: microbial nanomachines that display plasticity in quaternary structure. Gilbert HJ, Mol Microbiol 2007 63 1568 1576 10.1111/j.1365-2958.2007.05640.x 17367380 (Pubitemid 46426711)
7. Investigation of the function of mutated cellulose-binding domains of Trichoderma reesei cellobiohydrolase I. Reinikainen T, Ruohonen L, Nevanen T, Laaksonen L, Kraulis P, Jones TA, Knowles JKC, Teeri TT, Proteins Struct Funct Genet 1992 14 475 482 10.1002/prot.340140408 1438185
8. 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)
9. Access to cellulose limits the efficiency of enzymatic hydrolysis: the role of amorphogenesis. Arantes V, Saddler JN, Biotechnol Biofuels 2010 3 4 10.1186/1754-6834-3-4 20178562
10. Limited proteolysis of the cellobioydrolase I from Trichoderma reesei. van Tilbeurgh H, Tomme P, Claeyssens M, Bhikhabhai R, Pettersson G, Separation of functional domains. FEBS Lett 1986 204 223 227
11. Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis. Tomme P, van Tilbeurgh H, Pettersson G, van Damme J, Vandekerckhove J, Knowles J, Teeri T, Claeyssens M, Eur J Biochem 1988 170 575 581 10.1111/j.1432-1033. 1988.tb13736.x 3338453
12. A binding-site-deficient, catalytically active, core protein of endoglucanase III from the culture filtrate of Trichoderma reesei. Ståhlberg J, Johansson G, Pettersson G, Eur J Biochem 1988 173 179 183 10.1111/j.1432-1033.1988.tb13982.x 3356188
13. Updating the sequence-based classification of glycosyl hydrolases. Henrissat B, Bairoch A, Biochem J 1996 316 695 696 8687420 (Pubitemid 26182174)
14. A new model for enzymatic hydrolysis of cellulose based on the two-domain structure of cellobiohydrolase I. Ståhlberg J, Johansson G, Pettersson G, Bio/Technol 1991 9 286 290 10.1038/nbt0391-286
15. Adsorption and activity of Trichoderma reesei cellobiohydrolase I, endoglucanase II and the corresponding core proteins on steam pretreated willow. Kotiranta P, Karlsson J, Siika-Aho M, Medve J, Viikari L, Tjerneld F, Tenkanen M, Appl Biochem Biotechnol 1999 81 81 90 10.1385/ABAB:81:2:81 10581675
16. 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
17. 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
18. The energy landscape for interaction of the family 1 carbohydrate-binding module and the cellulose surface is altered by hydrolyzed glycosidic bonds. Bu L, Beckham GT, Crowley MF, Chang CH, Matthews JF, Bomble YJ, Adney WS, Himmel ME, Nimlos MR, J Phys Chem B 2009 113 10994 11002 19594145
19. Processivity of cellobiohidrolases is limited by the substrate. Kurasin M, Väljamäe P, J Biol Chem 2011 286 169 177 10.1074/jbc.M110.161059 21051539
20. Adsorption of Trichoderma reesei CBH I and EG II 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)
21. Inhibition of enzymatic hydrolysis by residual lignins from softwood-study of enzyme binding and inactivation on lignin-rich surface. Rahikainen J, Mikander S, Marjamaa K, Tamminen T, Lappas A, Viikari L, Kruus K, Biotechnol Bioeng 2011 108 2823 2834 10.1002/bit.23242 21702025
22. Mechanism of surfactant effect in enzymatic hydrolysis of lignocellulose. Eriksson T, Börjesson J, Tjerneld F, Enzyme Microb Technol 2002 31 353 364 10.1016/S0141-0229(02)00134-5 (Pubitemid 34790241)
23. Liquefaction of lignocellulose at high-solids concentrations. Jørgensen H, Vibe-Pedersen J, Larsen J, Felby C, Biotechnol Bioeng 2007 96 862 870 10.1002/bit.21115 16865734 (Pubitemid 46479549)
24. Determining yields in high solids enzymatic hydrolysis of biomass. Kristensen JB, Felby C, Jørgensen H, Appl Biochem Biotechnol 2009 156 127 132 10.1007/s12010-008-8375-0 18836690
25. The Pfam protein families database. Finn RD, Mistry J, Tate J, Coggill P, Heger A, Pollington JE, Gavin OL, Gunasekaran P, Ceric G, Forslund K, Holm L, Sonnhammer ELL, Eddy SR, Bateman A, Nucl Acids Res 2010 38 suppl 1 211 D222 19920124
26. Genome analyses highlight the different biological roles of cellulases. Medie FM, Davies GJ, Drancourt M, Henrissat B, Nat Rev Microbiol 2012 10 227 234 10.1038/nrmicro2729 22266780
27. The plant cell wall-decomposing machinery underlies the functional diversity of forest fungi. Eastwood DC, Floudas D, Binder M, Majcherczyk A, Schneider P, Aerts A, Asiegbu FO, Baker SE, Barry K, Bendiksby M, Blumentritt M, Coutinho PM, Cullen D, de Vries RP, Gathman A, Goodell B, Henrissat B, Ihrmark K, Kauserud H, Kohler A, LaButti K, Lapidus A, Lavin JL, Lee YH, Lindquist E, Lilly W, Lucas S, Morin E, Murat C, Oguiza JA, Science 2011 333 762 765 10.1126/science.1205411 21764756
28. UniProtKB Protein Knowledgebase: http://www.uniprot.org
29. Cellulose hydrolysis by the cellulases from Trichoderma reesei: a new model for synergistic interaction. Nidetzky B, Steiner W, Hayn M, Claeyssens M, Biochem J 1994 298 705 710 8141786 (Pubitemid 24085199)
30. Restriction of enzymatic hydrolysis of pretreated spruce by lignin. Várnai A, Siika-aho M, Viikari L, Enzyme Microb Technol 2010 46 185 193 10.1016/j.enzmictec.2009.12.013
31. Two structurally discrete GH7-cellobiohydrolases compete for the same cellulosic substrate fiber. Segato F, Damasio AR, Gonçalves TA, Murakami MT, Squina FM, Polizeli M, Mort AJ, Prade RA, Biotechnol. Biofuels 2012 5 21 10.1186/1754-6834-5-21 22494694
32. Microbial diversity of cellulose hydrolysis. Wilson DB, Curr Opin Microbiol 2011 14 259 263 10.1016/j.mib.2011.04.004 21531609
33. Ruiz R, Ehrman T, Determination of carbohydrates in biomass by high performance liquid chromatography. NREL Chemical Analysis and Testing Task, Laboratory Analytical Procedure 002: https://engineering.purdue.edu/LORRE/ research/LAP-002.pdf
34. An α-glucuronidase of Schizophyllum commune acting on polymeric xylan. Tenkanen M, Siika-aho M, J Biotechnol 2000 75 149 161 (Pubitemid 30139557)
35. Trichoderma reesei cellulases and their core domains in the hydrolysis and modification of chemical pulp. Suurnäkki A, Cellulose 2000 7 189 209 10.1023/A:1009280109519
36. Two major xylanases of Trichoderma reesei. Tenkanen M, Puls J, Poutanen K, Enzyme Microb Technol 1992 14 566 574 10.1016/0141-0229(92)90128-B
37. Purification and characterization of two β-mannanases from Trichoderma reesei. Stålbrand H, Siika-aho M, Tenkanen M, Viikari L, J Biotechnol 1993 29 229 242 10.1016/0168-1656(93)90055-R
38. Characterisation of specific activities and hydrolytic properties of cell-wall degrading enzymes produced by Trichoderma reesei Rut C30 on different carbon sources. Sipos B, Appl Biochem Biotechnol 2009 161 347 364 19898963
39. Protein measurement with the Folin phenol reagent. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ, J Biol Chem 1951 193 265 275 14907713
40. Adsorption of monocomponent enzymes in enzyme mixture analyzed quantitatively during hydrolysis of lignocellulose substrates. Várnai A, Viikari L, Marjamaa K, Siika-aho M, Bioresour Technol 2011 102 1220 1227 10.1016/j.biortech.2010.07.120 20736135
41. Fluorogenic and chromogenic glycosides as substrates and ligands of carbohydrases. van Tilbeurgh H, Loontiens FG, de Bruyne CK, Claeyssens M, Methods Enzymol 1988 160 45 59
42. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Miller GL, Anal Chem 1959 31 426 428 10.1021/ac60147a030