Access to cellulose limits the efficiency of enzymatic hydrolysis: The role of amorphogenesis

Biotechnology for Biofuels

Volumn 3, Issue 1, 2010, Pages 1-11

  Arantes, Valdeir ^a   Saddler, Jack N ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 77950356429     PISSN: 17546834     EISSN: None     Source Type: Journal    
DOI: 10.1186/1754-6834-3-1     Document Type: Review

References (81)

1. Walker LP, Wilson DB: Enzymatic hydrolysis of cellulose: An Overview. Biores Technol 1991, 36:3-14.
2. Xia L, Len P: Cellulose production by solid-state fermentation on lignocellulosic waste from the xylose industry. Process Biochem 1999, 34:909-912.
3. Berlin A, Maximenko V, Gilkes N, Saddler J: Optimization of enzyme complexes for lignocellulose hydrolysis. Biotechnol Bioeng 2007, 97:287-296.
4. Zhang X, Qin W, Paice M, Saddler JN: High consistency enzymatic hydrolysis of hardwood substrates. Biores Technol 2009, 100:5890-5897.
5. Mansfield SD, Mooney C, Saddler JN: Substrate and enzyme characteristics that limit cellulose hydrolysis. Biotechnol Prog 1999, 15:804-816.
6. Coughlan MP: The properties of fungal and bacterial cellulases with comment on their production and application. Biotechnology and genetic engineering reviews Newcastle-upon-Tyne: InterscienceRussell GE 1985, 3:37-109.
7. Din N, Gilkes NR, Tekant B, Miller RC Jr, Warren RA, Kilburn DG: Nonhydrolytic disruption of cellulose fibres by the binding domain of a bacterial cellulase. Bio/Technology 1991, 9:1096-1099.
8. Teeri TT, Reinikainen T, Ruohonen L, Alwyn Jones T, Knowles JKC: Domain function in Trichoderma reesei cellobiohydrolases. J Biotechnol 1992, 21:169-176.
9. Walker LP, Wilson DB, Irwin DC: Measuring fragmentation of cellulose by Thermomonospora fusca cellulase. Enzyme Microb Technol 1990, 12:378-386.
10. Reese ET, Sui RGH, Levinson HS: The biological degradation of soluble cellulose derivatives and its relationship to the mechanisms of cellulose hydrolysis. J Bacteriol 1950, 59:485-497.
11. Mandels M, Reese ET: Fungal cellulases and the microbial decomposition of cellulosic fabric. Development in Industrial Mycology Washington: American Institute of Biological Sciences 1964, 5:5-20.
12. Baker JO, King MR, Adney WS, Decker SR, Vinzant TB, Lantz SE, Nieves RE, Thomas SR, Li LC, Cosgrove DJ, Himmel ME: Investigation of the cell-wall loosening protein expansin as a possible additive in the enzymatic saccharification of lignocellulosic biomass. Appl Biochem Biotechnol 2000, 84:217-223.
13. Kim ES, Lee HJ, Bang WG, Choi IG, Kim KH: Functional characterization of a bacterial expansin from Bacillus subtilis for enhanced enzymatic hydrolysis of cellulose. Biotechnol Bioeng 2009, 102:1342-1353.
14. Krässing HA: Effect of structure and morphology on accessibility and reactivity. Cellulose: Structure, Accessibility, and Reactivity Gordon and Breach Science PublishersKrässing HA 1993, 11:167-324.
15. Somerville C, Bauer S, Brininstool G, Facette M, Hamann T, Milne J, Osborne E, Paredez A, Person S, Raab T, Vormerk S, Youngs H: Toward a systems approach to understanding plant cell walls. Science 2004, 306:2206-2211.
16. Ding S-Y, Himmel ME: The maize primary cell wall microfibril: a new model derived from direct visualization. J Agric Food Chem 2006, 54:597-606.
17. Wood TM, McCrae SI, Bhat KM: The mechanism of fungal cellulase action. Synergism between enzyme components of Penicillium pinophilum cellulase in solubilizing hydrogen-bond ordered cellulose. Biochem J 1989, 260:37-43.
18. Laureano-Perez L, Teymouri F, Alizadeh H, Dale BE: Understanding factors that limit enzymatic hydrolysis of biomass. Appl Biochem Biotechnol 2005, 121:1081-1099.
19. Gilkes NR, Henrissat B, Kilburn DG, Miller RC Jr, Warren RAJ: Domains in microbial b-1,4-glycanases: sequence conservation, function, and enzyme families. Microbiol Rev 1991, 55:303-315.
20. Boraston AB, Bolam DN, Gilbert HJ, Davies GJ: Carbohydrate-binding modules: fine tuning polysaccharide recognition. Biochem J 2004, 382:769-782.
21. Lynd LR, Weimer PJ, van Zyl WH, Pretorius IS: Microbial cellulose utilization: fundamentals and biotechnology. Microbiol Mol Biol R 2002, 66:506-577.
22. Raghothama S, Simpson PJ, Szabo L, Nagy T, Gilbert H, Williamson MP: Solution structure of the CBM10 cellulose binding module from Pseudomonas xylanase A. Biochem 2000, 39:978-984.
23. Irwin DC, Spezio M, Walker LP, Wilson DB: Activity studies of eight purified cellulases: specificity, synergism, and binding domain effects. Biotechnol Bioeng 1993, 42:1002-1013.
24. Wang LS, Zhang YZ, Gao PJ: A novel function for the cellulose binding module of cellobiohydro late I. Sci China Ser C-Life Sci 2008, 51:620-629.
25. Gao PJ, Chen GJ, Wang TH, Zhang YS, Liu J: Non-hydrolytic disruption of crystalline structure of cellulose by cellulose binding domain and liker sequence of cellobiohy drolase I from Penicillium janthinellum. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 2001, 33:13-18.
26. Pinto R, Moreira S, Mota M, Gama M: Studies on the cellulose-binding domains adsorption to cellulose. Langmuir 2004, 20:1409-1413.
27. Lee L, Evans BR, Woodward J: The mechanism of cellulose action on cotton fibers: evidence from atomic force microscopy. Ultramicroscopy 2000, 82:213-221.
28. Zeltins A, Schrempf H: Visualization of a-chitin-binding protein (CHB1) from Streptomyces olivaceoviridis. Anal Biochem 1995, 231:287-294.
29. Vaaje-Kolstad G, Horn SJ, van Aalten DMF, Synstad B, Eijsink VGH: The noncatalytic chiting-binding proteinCBP21 from Serratia marcescens is essential for chiting degradation. J Biol Chem 2005, 280:28492-28497.
30. Southall SM, Simpson PJ, Gilbert HJ, Williamson G, Williamson MP: The starch-binding domain from glucoamylase disrupts the structure of starch. FEBS Lett 1999, 447:58-60.
31. Sorimachi K, Le Gal-Coeffet MF, Williamson G, Archer DB, Williamson MP: Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to β-cyclodextrin. Structure 1997, 5:647-661.
32. Klyosov AA: Trends in biochemistry and enzymology of cellulose degradation. Biochem 1990, 29:10577-10585.
33. Rabinovich ML, Nguen VV, Klyosov AA: Adsorption of cellulolytic enzymes on cellulose and kinetics of the adsorbed enzymes. Two types of interactions of the enzymes with the insoluble substrate. Biokhimiya 1982, 48:369-377, (in Russian).
34. Rabinovich ML: Mechanisms of enzymatic degradation of cellulose. Microbiology and Biochemistry of Degradation of Plant Raw Materials Skryabin GK, Golovlev EL, Klyosov A Nauka 1988, 70-108, (in Russian).
35. Klyosov AA, Rabinovich ML: Enzymatic conversion of cellulose to glucose: present state of the art and potential. Enzyme Engineering: Future Directions New York: Plenum PressWingard LB, Berezin IV, Klyosov AA 1980, 83-165.
36. Esteghalian AR, Srivastava V, Gilkes N, Gregg DJ, Saddler JN: An overview of factors influencing the enzymatic hydrolysis of lignocellulosic feedstocks. Glycosyl Hydrolases for Biomass Conversion Washington DC: Americal Chemical SocietyHimmel ME, Baker JO, Saddler JN 2000, 100-111.
37. Mattews J, Skopec CE, Mason PE, Zuccato P, Torget RW, Sugiyama J, Himmel ME, Brady JW: Computer simulation studies of microcrystalline cellulose Iβ. Carbohyd Res 2006, 324:138-152.
38. Zhong L, Matthews JF, Crowley MF, Rignall T, Talón C, Cleary JM, Walker RC, Chukkapall G, McCabe C, Nimlos MR, Brooks CL III, Himmel ME, Brady JW: Interactions of the complete cellobiohydrolase I from Trichodera reesei with microcrystalline cellulose. Cellulose 2008, 15:261-273.
39. Zhong L, Matthews JF, Hansen PI, Crowley MF, Cleary JM, Walker RC, Nimlos MR, Books CL III, Adney WS, Himmel ME, Brady JW: Computational simulations of the Trichoderma reesei cellobiohydrolase I acting on microcrystalline cellulose Ib: the enzyme-substrate complex. Carbohyd Res 2009, 344:1984-1992.
40. Levy I, Shoseyov O: Cellulose-binding domains - Biotechnological applications. Biotechnol Adv 2002, 20:191-213.
41. Li ZC, Durachko DM, Cosgrove DJ: An oat coleoptile wall protein that induces wall extension in vitro and that is antigenically related to a similar protein from cucumber hypocotyls. Planta 1993, 191:349-356.
42. McQueen-Mason S, Durachko DM, Cosgrove DJ: Two endogenous proteins that induce cell wall expansion in plants. Plant Cell 1992, 4:1425-1433.
43. Cosgrove DJ: Growth of the plant cell wall. Nat Rev Mol Cell Biol 2005, 6:850-861.
44. Yennawar NH, Li LC, Dudzinski DM, Tabuchi A, Cosgrove DJ: Crystal structure and activities of EXP1 (Zea m 1), a β-expansin and group-1 pollen allergen from maize. Proc Natl Acad Sci 2006, 103:14664-114671.
45. Cosgrove DJ: New genes and new biological roles for expansins. Curr Opin Plant Biol 2000, 3:73-78.
46. Cosgrove DJ: Relaxation in a high-stress environment: the molecular bases of extensible cell walls and cell enlargement. Plant Cell 1997, 9:1031-1041.
47. Saloheimo A, Henrissat B, Hoffren AM, Teleman O, Penttilä M: A novel, small endoglucanase gene, egl5, from Trichoderma reesei isolated by expression in yeast. Mol Microbiol 1994, 13:219-228.
48. Tatusova TA, Madden TL: Blast 2 sequences - a new tool for comparing protein and nucleotide sequences. FEMS Microbiol Lett 1999, 174:247-250.
49. Cosgrove DJ, Durachko DM, Li LC: Expansins may have cryptic endoglucanase activity and can synergize the breakdown of cellulose by fungal cellulases. Annu Meeting Am Soc Plant Physiol Abstr 1998, 171.
50. Sampedro J, Cosgrove DJ: The expansin superfamily. Genome Biol 2005, 6:242.1-242.11.
51. Cosgrove DJ: Enhancement of accessibility of cellulose by expansins. United States Patent. Patent No. US 6,326,470 B1 2001.
52. Kerff F, Amoroso A, Herman R, Sauvage E, Petrella S, Filée P, Charlier P, Joris B, Tabuchi A, Nikolaidis N, Cosgrove DJ: Crystal structure and activity of Bacillus subtilis YoaJ (EXLX1), a bacterial expansin that promotes root colonization. Proc Natl Acad Sci USA 2008, 105:16876-81.
53. Saloheimo M, Paloheimo M, Hakola S, Pere J, Swanson B, Nyyssönen E, Bhatia A, Ward M, Penttilä M: Swollenin, a Trichoderma reesei protein with sequence similarity to the plant expansins, exhibits disruption activity on cellulosic materials. Eur J Biochem 2002, 269:4202-11.
54. Laine MJ, Haapalainen M, Wahlroos T, Kankare K, Nissinen R, Kassuwi S, Metzler MC: The cellulase encoded by the native plasmid of Clavibacter michiganensis ssp. sepedonicus plays a role in virulence and contains an expansin-like domain. Physiol Mol Plant P 2000, 57:221-233.
55. Yao Q, Sun TT, Liu WF, Chen GJ: Gene Cloning and heterologous Expression of a novel endoglucanase, swollenin, from Trichoderma pseudokoningii S38. Biosci Biotech Bioch 2008, 72:2799-2805.
56. Brotman Y, Briff E, Viterbo A, Chet I: Role of swollenin, an expansin-Like protein from Trichoderma, in plant root colonization. Plant Physiol 2008, 147:779-789.
57. Yang B, Wyman CE: BSA treatment to enhance enzymatic hydrolysis of cellulose in lignin containing substrates. Biotechnol Bioeng 2006, 94:611-617.
58. Bommarius AS, Katona A, Cheben SE, Patel AS, Ragauskas AJ, Knudson K, Pu Y: Cellulase kinetics as a function of cellulose pretreatment. Metab Eng 2008, 10:371-381.
59. Xu F, Ding H: A new kinetic model for heterogeneous (or spatially confined) enzymatic catalysis: contributions from the fractal and jamming (overcrowding) effects. Appl Catal A-Gen 2007, 317:70-81.
60. Levasseur A, Saloheimo M, Navarro D, Andberg M, Monot F, Nakari-Setala T, Asther M, Record E: Production of a chimeric enzyme tool associating the Trichoderma reesei swollenin with the Aspergillus niger feruloyl esterase A for release of ferulic acid. Appl Microbiol Biotechnol 2006, 73:872-880.
61. Ljungdahl LG, Petersson B, Eriksson KE, Wiegel J: A yellow affinity substance involved in the cellulolytic system of Clostridium thermocellum. Curr Microbiol 1983, 9:195-200.
62. Kopecny J, Simunek J, Hodrova B: Production and properties of yellow affinity substances by Ruminococcus flavefaciens. Ann Zootech 1996, 45(SUPPL):299-299.
63. Kopecny J, Hodrova B: The effect of yellow affinity substance on cellulases of Ruminococcus flavefaciens. Lett Appl Microbiol 1997, 25:191-196.
64. Lamed R, Kenig R, Setter E, Bayer EA: Major characteristics of the cellulolytic system of Clostridium thermocellum coincide with those of the purified cellulosome. Enzyme Microbial Technol 1985, 7:37-41.
65. Han Y, Chen HZ: Synergism between corn stover protein and cellulase. Enzyme Microbial Technol 2007, 41:638-645.
66. De Leon AL, Ding H, Brown K: Polypeptides having cellulolytic enhancing activity and nucleic acids encoding same. US 2009/0019608 A1 2009.
67. Merino ST, Cherry J: Progress and challenges in enzyme development for biomass utilization. Adv Biochem Engin/Biotechnol 2007, 108:95-120.
68. Cosgrove DJ: Loosening of plant cell walls by expansins. Nature 2000, 407:321-326.
69. Foreman PK, Brown D, Dankmeyer L, Dean R, Diener S, Dunn-Coleman NS, Goedegebuur F, Houfek TD, England GJ, Kelley AS, Meerman HJ, Mitchell T, Mitchinson C, Olivares HA, Teunissen PJM, Yao J, Ward M: Transcriptional regulation of biomass-degrading enzymes in the filamentous fungus Trichoderma reesei. J Biol Chem 2003, 278:31988-31997.
70. Karkehadabi S, Hansson H, Kim S, Piens K, Mitchinson C, Sandgren M: The first structure of a glycoside hydrolase family 61 member, Cel61B from Hypocrea jecorina, at 1.6 Å resolution. J Mol Biol 2008, 383:144-154.
71. Goodell B, Jellison J, Liu J, Daniel G, Paszczynski A, Fekete F, Krishnamurthy S, Jun L, Xu G: Low molecular weight chelators and phenolic compounds isolated from wood decay fungi and their role in the fungal biodegradation of wood. J Biotechnol 1997, 53:133-162.
72. Enoki A, Itajura S, Tanaka H: The involvement of extracelullar substances for reducing molecular oxygen to hydroxyl radical and ferric ion to ferrous iron in wood degradation by wood decay fungi. J Biotechnol 1997, 53:265-272.
73. Arantes V, Milagres AMF: The relevance of low molecular weight compounds in wood biodegradation by fungi. Quim Nova 2009, 32:1586-1595.
74. Fluornoy DS, Kirk TK, Highley TL: Wood decay by brown-rot fungi: changes in pore structure and cell wall volume. Holzforschung 1991, 45:383-388.
75. Blanchette RA, Krueger EW, Haight JE, Akhtar M, Akin DE: Cell wall alterations in loblolly pine wood decayed by the white-rot fungus, Ceriporiopsis subvermispora. J Biotechnol 1997, 53:203-213.
76. Hammel KE, Kapich AN, Jensen KA Jr, Ryan ZC: Reactive oxygen species as agents of wood decay by fungi. Enzyme Microbial Technol 2002, 30:445-453.
77. Goodell B: Brown rot degradation of wood: Our evolving view. Wood Deterioration and Preservation: Advances in Our Changing World American Chemical Society Series. Oxford University PressGoodell B, Nicholas D, Schultz T 2003, 97-118.
78. 13C-labeled tetramethylammonium hydroxide thermochemolysis: implications for fungal degradation of wood. J Biol Inorg Chem 2009, 8:1253-1263.
79. Rätto M, Ritschkoff AC, Viikari L: The effect of oxidative pretreatment on cellulose degradadion by Poria placenta and Trichoderma reesei cellulases. Appl Microbiol Biotechnol 1997, 48:53-57.
80. Schilling JS, Tewalt JP, Duncan SM: Synergy between pretreatment lignocellulose modifications and saccharification efficiency in two brown rot fungal systems. Appl Microbiol Biotechnol 2009, 84:465-475.
81. Wang W, Gao PJ: Function and mechanism of a low-molecular weight peptide produced by Gloephyllum trabeum in biodegrdation of cellulose. J Biotechnol 2003, 101:119-130.