Lignocellulases: a review of emerging and developing enzymes, systems, and practices

Eugene M. Obeng , Siti Nurul Nadzirah Adam , Cahyo Budiman , Clarence M. Ongkudon , Ruth Maas , Joachim Jose

Bioresources and Bioprocessing ›› 2017, Vol. 4 ›› Issue (1) : 16

PDF
Bioresources and Bioprocessing ›› 2017, Vol. 4 ›› Issue (1) : 16 DOI: 10.1186/s40643-017-0146-8
Review

Lignocellulases: a review of emerging and developing enzymes, systems, and practices

Author information +
History +
PDF

Abstract

The highly acclaimed prospect of renewable lignocellulosic biocommodities as obvious replacement of their fossil-based counterparts is burgeoning within the last few years. However, the use of the abundant lignocellulosic biomass provided by nature to produce value-added products, especially bioethanol, still faces significant challenges. One of the crucial challenging factors is in association with the expression levels, stability, and cost-effectiveness of the cellulose-degrading enzymes (cellulases). Interestingly, several recommendable endeavors in the bid to curb these challenges are in pursuance. However, the existing body of literature has not well provided the updated roadmap of the advancement and key players spearheading the current success. Moreover, the description of enzyme systems and emerging paradigms with high prospects, for example, the cell-surface display system has been ill-captured in the literature. This review focuses on the lignocellulosic biocommodity pathway, with emphasis on cellulase and hemicellulase systems. The paradigm shift towards cell-surface display system and its emerging recommendable developments have also been discussed. The attempts in supplementing cellulase with other enzymes, accessory proteins, and chemical additives have also been discussed. Moreover, some of the prominent and influential discoveries in the cellulase fraternity have been discussed.

Keywords

Cellulases / Lytic polysaccharide mono-oxygenases / Cellulase systems / Cell-surface display systems / Autodisplay systems / Cellulosomes

Cite this article

Download citation ▾
Eugene M. Obeng, Siti Nurul Nadzirah Adam, Cahyo Budiman, Clarence M. Ongkudon, Ruth Maas, Joachim Jose. Lignocellulases: a review of emerging and developing enzymes, systems, and practices. Bioresources and Bioprocessing, 2017, 4(1): 16 DOI:10.1186/s40643-017-0146-8

登录浏览全文

4963

注册一个新账户 忘记密码

References

[1]

Aachmann FL, Sorlie M, Skjak-Braek G, . NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions. Proc Natl Acad Sci, 2012, 109: 18779-18784.

[2]

Anthony T, Chandra Raj K, Rajendran A, Gunasekaran P. High molecular weight cellulase-free xylanase from alkali-tolerant Aspergillus fumigatus AR1. Enzyme Microb Technol, 2003, 32: 647-654.

[3]

Badhan AK, Chadha BS, Kaur J, . Production of multiple xylanolytic and cellulolytic enzymes by thermophilic fungus Myceliophthora sp. IMI 387099. Bioresour Technol, 2007, 98: 504-510.

[4]

Balasubramanian N, Simões N. Bacillus pumilus S124A carboxymethyl cellulase; a thermo stable enzyme with a wide substrate spectrum utility. Int J Biol Macromol, 2014, 67: 132-139.

[5]

Bansal N, Tewari R, Soni R, Soni SK. Production of cellulases from Aspergillus niger NS-2 in solid state fermentation on agricultural and kitchen waste residues. Waste Manag, 2012, 32: 1341-1346.

[6]

Bayer EA, Lamed R, White BA, Flints HJ. From cellulosomes to cellulosomics. Chem Rec, 2008, 8: 364-377.

[7]

Beckham GT, Dai Z, Matthews JF, . Harnessing glycosylation to improve cellulase activity. Curr Opin Biotechnol, 2012, 23: 338-345.

[8]

Beeson WT, Phillips CM, Cate JHD, Marletta MA. Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases. J Am Chem Soc, 2012, 134: 890-892.

[9]

Begum MF, Alimon AR. Bioconversion and saccharification of some lignocellulosic wastes by Aspergillus oryzae ITCC-4857.01 for fermentable sugar production. Electron J Biotechnol, 2011

[10]

Berlin A. No barriers to cellulose breakdown. Science, 2013, 342: 1454-1456.

[11]

Böhmer N, Lutz-Wahl S, Fischer L. Recombinant production of hyperthermostable CelB from Pyrococcus furiosus in Lactobacillus sp. Appl Microbiol Biotechnol, 2012, 96: 903-912.

[12]

Borisova AS, Isaksen T, Dimarogona M, . Structural and functional characterization of a lytic polysaccharide monooxygenase with broad substrate specificity. J Biol Chem, 2015, 290: 22955-22969.

[13]

Bornscheuer U, Buchholz K, Seibel J. Enzymatic degradation of (Ligno) cellulose. Angew Chemie Int Ed, 2014, 53: 10876-10893.

[14]

Boyce A, Walsh G. Characterisation of a novel thermostable endoglucanase from Alicyclobacillus vulcanalis of potential application in bioethanol production. Appl Microbiol Biotechnol, 2015, 99: 7515-7525.

[15]

Brault G, Shareck F, Hurtubise Y, . Short-chain flavor ester synthesis in organic media by an E. coli whole-cell biocatalyst expressing a newly characterized heterologous lipase. PLoS ONE, 2014, 9: e91872.

[16]

Brunecky R, Alahuhta M, Bomble YJ, . Structure and function of the Clostridium thermocellum cellobiohydrolase A X1-module repeat: enhancement through stabilization of the CbhA complex. Acta Crystallogr Sect D Biol Crystallogr, 2012, 68: 292-299.

[17]

Busk PK, Lange L. Classification of fungal and bacterial lytic polysaccharide monooxygenases. BMC Genom, 2015, 16: 368.

[18]

Cannella D, Jørgensen H. Do new cellulolytic enzyme preparations affect the industrial strategies for high solids lignocellulosic ethanol production?. Biotechnol Bioeng, 2014, 111: 59-68.

[19]

Cannella D, Hsieh CC, Felby C, Jørgensen H. Production and effect of aldonic acids during enzymatic hydrolysis of lignocellulose at high dry matter content. Biotechnol Biofuels, 2012, 5: 26.

[20]

Cao L, van Langen L, Sheldon RA. Immobilised enzymes: carrier-bound or carrier-free?. Curr Opin Biotechnol, 2003, 14: 387-394.

[21]

Carvalho AL, Goyal A, Prates JAM, . The family 11 carbohydrate-binding module of Clostridium thermocellum Lic26A-Cel5E accommodates β-1,4- and β-1,3-1,4-mixed linked glucans at a single binding site. J Biol Chem, 2004, 279: 34785-34793.

[22]

Chandel AK, Singh OV, Venkateswar Rao L, . Bioconversion of novel substrate Saccharum spontaneum, a weedy material, into ethanol by Pichia stipitis NCIM3498. Bioresour Technol, 2011, 102: 1709-1714.

[23]

Chandel AK, Gonçalves BCM, Strap JL, da Silva SS. Biodelignification of lignocellulose substrates: an intrinsic and sustainable pretreatment strategy for clean energy production. Crit Rev Biotechnol, 2013, 1: 1-13.

[24]

Chandra RP, Bura R, Mabee WE, . Substrate pretreatment: the key to effective enzymatic hydrolysis of lignocellulosics?. Adv Biochem Eng Biotechnol, 2007, 108: 67-93.

[25]

Chang L, Ding M, Bao L, . Characterization of a bifunctional xylanase/endoglucanase from yak rumen microorganisms. Appl Microbiol Biotechnol, 2011, 90: 1933-1942.

[26]

Chhabra SR, Shockley KR, Ward DE, Kelly RM. Regulation of endo-acting glycosyl hydrolases in the hyperthermophilic bacterium Thermotoga maritima grown on glucan- and mannan-based polysaccharides. Appl Environ Microbiol, 2002, 68: 545-554.

[27]

Cho K-M, Math RK, Hong S-Y, . Changes in the activity of the multifunctional b -glycosyl hydrolase (Cel44C-Man26A) from Paenibacillus polymyxa by removal of the C-terminal region to minimum size. Biotechnol Lett, 2008, 30: 1061-1068.

[28]

Ciolacu D, Kovac J, Kokol V. The effect of the cellulose-binding domain from Clostridium cellulovorans on the supramolecular structure of cellulose fibers. Carbohydr Res, 2010, 345: 621-630.

[29]

Claus H. Laccases: structure, reactions, distribution. Micron, 2004, 35: 93-96.

[30]

Conrado RJ, Varner JD, DeLisa MP. Engineering the spatial organization of metabolic enzymes: mimicking nature’s synergy. Curr Opin Biotechnol, 2008, 19: 492-499.

[31]

Cota J, Oliveira LC, Damásio ARL, . Assembling a xylanase–lichenase chimera through all-atom molecular dynamics simulations. Biochim Biophys Acta Proteins Proteom, 2013, 1834: 1492-1500.

[32]

Courtade G, Wimmer R, Røhr ÅK, . Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase. Proc Natl Acad Sci, 2016, 113: 5922-5927.

[33]

Czjzek M, Cicek M, Zamboni V, . The mechanism of substrate (aglycone) specificity in beta-glucosidases is revealed by crystal structures of mutant maize beta -glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes. Proc Natl Acad Sci USA, 2000, 97: 13555-13560.

[34]

Das A, Paul T, Halder SK, . Production of cellulolytic enzymes by Aspergillus fumigatus ABK9 in wheat bran-rice straw mixed substrate and use of cocktail enzymes for deinking of waste office paper pulp. Bioresour Technol, 2013, 128: 290-296.

[35]

Das A, Paul T, Ghosh P, . Kinetic study of a glucose tolerant β-glucosidase from Aspergillus fumigatus ABK9 entrapped into alginate beads. Waste Biomass Valoriz, 2015, 6: 53-61.

[36]

de Carvalho CCCR. Enzymatic and whole cell catalysis: finding new strategies for old processes. Biotechnol Adv, 2011, 29: 75-83.

[37]

Decker CH, Visser J, Schreier P. β-Glucosidase multiplicity from Aspergillus tubingensis CBS 643.92: purification and characterization of four β-glucosidases and their differentiation with respect to substrate specificity, glucose inhibition and acid tolerance. Appl Microbiol Biotechnol, 2001, 55: 157-163.

[38]

Decker SR, Siika-Aho M, Viikari L. Himmel ME. Enzymatic depolymerization of plant cell hemicelluloses. Biomass recalcitrance: deconstructing the plant cell wall for bioenergy, 2008, Oxford: Blackwell Publishing, 354-378.

[39]

Demirjian DC, Morı́s-Varas F, Cassidy CS. Enzymes from extremophiles. Curr Opin Chem Biol, 2001, 5: 144-151.

[40]

di Lauro B, Rossi M, Moracci M. Characterization of a β-glycosidase from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius. Extremophiles, 2006, 10: 301-310.

[41]

Doherty WOS, Mousavioun P, Fellows CM. Value-adding to cellulosic ethanol: lignin polymers. Ind Crops Prod, 2011, 33: 259-276.

[42]

Dwivedi UN, Singh P, Pandey VP, Kumar A. Structure–function relationship among bacterial, fungal and plant laccases. J Mol Catal B Enzym, 2011, 68: 117-128.

[43]

Easton R. Glycosylation of proteins—structure, function and analysis. Life Sci Tech Bull, 2011, 60: 1-5.

[44]

Egorova K, Antranikian G. Industrial relevance of thermophilic Archaea. Curr Opin Microbiol, 2005, 8: 649-655.

[45]

Eibinger M, Ganner T, Bubner P, . Cellulose surface degradation by a lytic polysaccharide monooxygenase and its effect on cellulase hydrolytic efficiency. J Biol Chem, 2014, 289: 35929-35938.

[46]

Elleuche S, Schröder C, Sahm K, Antranikian G. Extremozymes—biocatalysts with unique properties from extremophilic microorganisms. Curr Opin Biotechnol, 2014, 29: 116-123.

[47]

Eriksson T, Börjesson J, Tjerneld F. Mechanism of surfactant effect in enzymatic hydrolysis of lignocellulose. Enzyme Microb Technol, 2002, 31: 353-364.

[48]

Falkoski DL, Guimarães VM, de Almeida MN, . Chrysoporthe cubensis: a new source of cellulases and hemicellulases to application in biomass saccharification processes. Bioresour Technol, 2013, 130: 296-305.

[49]

Fan Z, Wagschal K, Chen W, . Multimeric hemicellulases facilitate biomass conversion. Appl Environ Microbiol, 2009, 75: 1754-1757.

[50]

Fierobe Bayer EA, Tardif C, . Degradation of cellulose substrates by cellulosome chimeras. J Biol Chem, 2002, 277: 49621-49630.

[51]

Fontes CMGA, Gilbert HJ. Cellulosomes: highly efficient nanomachines designed to deconstruct plant cell wall complex carbohydrates. Annu Rev Biochem, 2010, 79: 655-681.

[52]

Frandsen KEH, Simmons TJ, Dupree P, . The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases. Nat Chem Biol, 2016, 12: 298-303.

[53]

Furtado GP, Ribeiro LF, Lourenzoni MR, Ward RJ. A designed bifunctional laccase/-1,3-1,4-glucanase enzyme shows synergistic sugar release from milled sugarcane bagasse. Protein Eng Des Sel, 2013, 26: 15-23.

[54]

Gallezot P. Conversion of biomass to selected chemical products. Chem Soc Rev, 2012, 41: 1538-1558.

[55]

Gao D, Uppugundla N, Chundawat SP, . Hemicellulases and auxiliary enzymes for improved conversion of lignocellulosic biomass to monosaccharides. Biotechnol Biofuels, 2011, 4: 5.

[56]

Garvey M, Klose H, Fischer R, . Cellulases for biomass degradation: comparing recombinant cellulase expression platforms. Trends Biotechnol, 2013, 31: 581-593.

[57]

González-Candelas L, Aristoy MC, Polaina J, Flors A. Cloning and characterization of two genes from Bacillus polymyxa expressing beta-glucosidase activity in Escherichia coli. Appl Environ Microbiol, 1989, 55: 3173-3177.

[58]

Graham JE, Clark ME, Nadler DC, . Identification and characterization of a multidomain hyperthermophilic cellulase from an archaeal enrichment. Nat Commun, 2011, 2: 375.

[59]

Günata Z, Vallier MJ. Production of a highly glucose-tolerant extracellular β-glucosidase by three Aspergillus strains. Biotechnol Lett, 1999, 21: 219-223.

[60]

Haki G. Developments in industrially important thermostable enzymes: a review. Bioresour Technol, 2003, 89: 17-34.

[61]

Hanif A, Yasmeen A, Rajoka MI. Induction, production, repression, and de-repression of exoglucanase synthesis in Aspergillus niger. Bioresour Technol, 2004, 94: 311-319.

[62]

Harris PV, Welner D, McFarland KC, . Stimulation of lignocellulosic biomass hydrolysis by proteins of glycoside hydrolase family 61: structure and function of a large, enigmatic family. Biochemistry, 2010, 49: 3305-3316.

[63]

Harris PV, Xu F, Kreel NE, . New enzyme insights drive advances in commercial ethanol production. Curr Opin Chem Biol, 2014, 19: 162-170.

[64]

Hemsworth GR, Davies GJ, Walton PH. Recent insights into copper-containing lytic polysaccharide mono-oxygenases. Curr Opin Struct Biol, 2013, 23: 660-668.

[65]

Hemsworth GR, Taylor EJ, Kim RQ, . The copper active site of CBM33 polysaccharide oxygenases. J Am Chem Soc, 2013, 135: 6069-6077.

[66]

Hendriks ATWM, Zeeman G. Pretreatments to enhance the digestibility of lignocellulosic biomass. Bioresour Technol, 2009, 100: 10-18.

[67]

Himmel ME, Xu Q, Luo Y, . Microbial enzyme systems for biomass conversion: emerging paradigms. Biofuels, 2010, 1: 323-341.

[68]

Hirano N, Hasegawa H, Nihei S, Haruki M. Cell-free protein synthesis and substrate specificity of full-length endoglucanase CelJ (Cel9D-Cel44A), the largest multi-enzyme subunit of the Clostridium thermocellum cellulosome. FEMS Microbiol Lett, 2013, 344: 25-30.

[69]

Horn S, Vaaje-Kolstad G, Westereng B, Eijsink VG. Novel enzymes for the degradation of cellulose. Biotechnol Biofuels, 2012, 5: 45.

[70]

Hyeon JE, You SK, Kang DH, . Enzymatic degradation of lignocellulosic biomass by continuous process using laccase and cellulases with the aid of scaffoldin for ethanol production. Process Biochem, 2014, 49: 1266-1273.

[71]

Isaksen T, Westereng B, Aachmann FL, . A C4-oxidizing lytic polysaccharide monooxygenase cleaving both cellulose and cello-oligosaccharides. J Biol Chem, 2014, 289: 2632-2642.

[72]

Islam R, Özmihçi S, Cicek N, . Enhanced cellulose fermentation and end-product synthesis by Clostridium thermocellum with varied nutrient compositions under carbon-excess conditions. Biomass Bioenergy, 2013, 48: 213-223.

[73]

Jagtap SS, Dhiman SS, Kim T-S, . Characterization of a β-1,4-glucosidase from a newly isolated strain of Pholiota adiposa and its application to the hydrolysis of biomass. Biomass Bioenergy, 2013, 54: 181-190.

[74]

Jose J. Autodisplay: efficient bacterial surface display of recombinant proteins. Appl Microbiol Biotechnol, 2006, 69: 607-614.

[75]

Jose J, Meyer TF. The autodisplay story, from discovery to biotechnical and biomedical applications. Microbiol Mol Biol Rev, 2007, 71: 600-619.

[76]

Jose J, Maas RM, Teese MG. Autodisplay of enzymes—molecular basis and perspectives. J Biotechnol, 2012, 161: 92-103.

[77]

Jung S, Song Y, Kim HM, Bae H-J. Enhanced lignocellulosic biomass hydrolysis by oxidative lytic polysaccharide monooxygenases (LPMOs) GH61 from Gloeophyllum trabeum. Enzyme Microb Technol, 2015, 77: 38-45.

[78]

Juturu V, Wu JC. Microbial cellulases: engineering, production and applications. Renew Sustain Energy Rev, 2014, 33: 188-203.

[79]

Kanafusa-Shinkai S, Wakayama J, Tsukamoto K, . Degradation of microcrystalline cellulose and non-pretreated plant biomass by a cell-free extracellular cellulase/hemicellulase system from the extreme thermophilic bacterium Caldicellulosiruptor bescii. J Biosci Bioeng, 2013, 115: 64-70.

[80]

Kang SW, Park YS, Lee JS, . Production of cellulases and hemicellulases by Aspergillus niger KK2 from lignocellulosic biomass. Bioresour Technol, 2004, 91: 153-156.

[81]

Karkehabadi S, Hansson H, Kim S, . 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.

[82]

Karlsson J, Saloheimo M, Siika-aho M, . Homologous expression and characterization of Cel61A (EG IV) of Trichoderma reesei. Eur J Biochem, 2001, 268: 6498-6507.

[83]

Kazenwadel F, Franzreb M, Rapp BE. Synthetic enzyme supercomplexes: co-immobilization of enzyme cascades. Anal Methods, 2015, 7: 4030-4037.

[84]

Kengen SWM, Luesink EJ, Stams AJM, Zenhder AJB. Purification and characterization of an extremely thermostable beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus. Eur J Biochem, 1993, 213: 305-312.

[85]

Khattak WA, Ul-Islam M, Park JK. Prospects of reusable endogenous hydrolyzing enzymes in bioethanol production by simultaneous saccharification and fermentation. Korean J Chem Eng, 2012, 29: 1467-1482.

[86]

Khattak WA, Ul-Islam M, Ullah MW, . Yeast cell-free enzyme system for bio-ethanol production at elevated temperatures. Process Biochem, 2014, 49: 357-364.

[87]

Khattak WA, Ullah MW, Ul-Islam M, . Developmental strategies and regulation of cell-free enzyme system for ethanol production: a molecular prospective. Appl Microbiol Biotechnol, 2014, 98: 9561-9578.

[88]

Kim S, Kim CH. Production of cellulase enzymes during the solid-state fermentation of empty palm fruit bunch fiber. Bioprocess Biosyst Eng, 2012, 35: 61-67.

[89]

Kim T-W, Chokhawala HA, Nadler D, . Binding modules alter the activity of chimeric cellulases: effects of biomass pretreatment and enzyme source. Biotechnol Bioeng, 2010, 107: 601-611.

[90]

Kim CS, Seo JH, Kang DG, Cha HJ. Engineered whole-cell biocatalyst-based detoxification and detection of neurotoxic organophosphate compounds. Biotechnol Adv, 2014, 32: 652-662.

[91]

Kim HM, Jung S, Lee KH, . Improving lignocellulose degradation using xylanase–cellulase fusion protein with a glycine–serine linker. Int J Biol Macromol, 2015, 73: 215-221.

[92]

Kim Y, Kreke T, Ko JK, Ladisch MR. Hydrolysis-determining substrate characteristics in liquid hot water pretreated hardwood. Biotechnol Bioeng, 2015, 112: 677-687.

[93]

Kisukuri CM, Andrade LH. Production of chiral compounds using immobilized cells as a source of biocatalysts. Org Biomol Chem, 2015, 13: 10086-10107.

[94]

Koeck DE, Wibberg D, Koellmeier T, . Draft genome sequence of the cellulolytic Clostridium thermocellum wild-type strain BC1 playing a role in cellulosic biomass degradation. J Biotechnol, 2013, 168: 62-63.

[95]

Koshland DE. Stereochemistry and the mechanism of enzymatic reactions. Biol Rev, 1953, 28: 416-436.

[96]

Kracher D, Scheiblbrandner S, Felice AKG, . Extracellular electron transfer systems fuel cellulose oxidative degradation. Science, 2016, 352: 1098-1101.

[97]

Kranen E, Detzel C, Weber T, Jose J. Autodisplay for the co-expression of lipase and foldase on the surface of E. coli: washing with designer bugs. Microb Cell Fact, 2014, 13: 19.

[98]

Lahtinen M, Kruus K, Boer H, . The effect of lignin model compound structure on the rate of oxidation catalyzed by two different fungal laccases. J Mol Catal B Enzym, 2009, 57: 204-210.

[99]

Lee CY, Yu KO, Kim SW, Han SO. Enhancement of the thermostability and activity of mesophilic Clostridium cellulovorans EngD by in vitro DNA recombination with Clostridium thermocellum CelE. J Biosci Bioeng, 2010, 109: 331-336.

[100]

Lee H-L, Chang C-K, Teng K-H, Liang P-H. Construction and characterization of different fusion proteins between cellulases and β-glucosidase to improve glucose production and thermostability. Bioresour Technol, 2011, 102: 3973-3976.

[101]

Lee H-L, Chang C-K, Jeng W-Y, . Mutations in the substrate entrance region of β-glucosidase from Trichoderma reesei improve enzyme activity and thermostability. Protein Eng Des Sel, 2012, 25: 733-740.

[102]

Li D, Li X, Dang W, . Characterization and application of an acidophilic and thermostable β-glucosidase from Thermofilum pendens. J Biosci Bioeng, 2013, 115: 490-496.

[103]

Liang Y, Si T, Ang EL, Zhao H. Engineered pentafunctional minicellulosome for simultaneous saccharification and ethanol fermentation in Saccharomyces cerevisiae. Appl Environ Microbiol, 2014, 80: 6677-6684.

[104]

Liu D, Zhang R, Yang X, . Thermostable cellulase production of Aspergillus fumigatus Z5 under solid-state fermentation and its application in degradation of agricultural wastes. Int Biodeterior Biodegrad, 2011, 65: 717-725.

[105]

Matano Y, Hasunuma T, Kondo A. Cell recycle batch fermentation of high-solid lignocellulose using a recombinant cellulase-displaying yeast strain for high yield ethanol production in consolidated bioprocessing. Bioresour Technol, 2013, 135: 403-409.

[106]

Mate DM, Alcalde M. Laccase engineering: from rational design to directed evolution. Biotechnol Adv, 2015, 33: 25-40.

[107]

Mateo C, Palomo JM, Fernandez-Lorente G, . Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme Microb Technol, 2007, 40: 1451-1463.

[108]

Mesas JM, Rodríguez MC, Alegre MT. Basic characterization and partial purification of β-glucosidase from cell-free extracts of Oenococcus oeni ST81. Lett Appl Microbiol, 2012, 55: 247-255.

[109]

Moilanen U, Kellock M, Galkin S, Viikari L. The laccase-catalyzed modification of lignin for enzymatic hydrolysis. Enzyme Microb Technol, 2011, 49: 492-498.

[110]

Moraïs S, Barak Y, Caspi J, . Contribution of a xylan-binding module to the degradation of a complex cellulosic substrate by designer cellulosomes. Appl Environ Microbiol, 2010, 76: 3787-3796.

[111]

Moraïs S, Barak Y, Lamed R, . Paradigmatic status of an endo- and exoglucanase and its effect on crystalline cellulose degradation. Biotechnol Biofuels, 2012, 5: 78.

[112]

Mosier N, Wyman C, Dale B, . Features of promising technologies for pretreatment of lignocellulosic biomass. Bioresour Technol, 2005, 96: 673-686.

[113]

Mot AC, Silaghi-Dumitrescu R. Laccases: complex architectures for one-electron oxidations. Biochem, 2012, 77: 1395-1407.

[114]

Müller G, Várnai A, Johansen KS, . Harnessing the potential of LPMO-containing cellulase cocktails poses new demands on processing conditions. Biotechnol Biofuels, 2015, 8: 187.

[115]

Nakashima K, Endo K, Shibasaki-kitakawa N, Yonemoto T. A fusion enzyme consisting of bacterial expansin and endoglucanase for the degradation of highly crystalline cellulose. RSC Adv, 2014, 4: 43815-43820.

[116]

Nakatani Y, Yamada R, Ogino C, Kondo A. Synergetic effect of yeast cell-surface expression of cellulase and expansin-like protein on direct ethanol production from cellulose. Microb Cell Fact, 2013, 12: 66.

[117]

Nam KH, Sung MW, Hwang KY. Structural insights into the substrate recognition properties of β-glucosidase. Biochem Biophys Res Commun, 2010, 391: 1131-1135.

[118]

Oberoi HS, Rawat R, Chadha BS. Response surface optimization for enhanced production of cellulases with improved functional characteristics by newly isolated Aspergillus niger HN-2. Antonie Van Leeuwenhoek, 2014, 105: 119-134.

[119]

Pandiyan K, Tiwari R, Rana S, . Comparative efficiency of different pretreatment methods on enzymatic digestibility of Parthenium sp. World J Microbiol Biotechnol, 2014, 30: 55-64.

[120]

Parisutham V, Kim TH, Lee SK. Feasibilities of consolidated bioprocessing microbes: from pretreatment to biofuel production. Bioresour Technol, 2014, 161: 431-440.

[121]

Park S, Baker JO, Himmel ME, . Cellulose crystallinity index: measurement techniques and their impact on interpreting cellulase performance. Biotechnol Biofuels, 2010, 3: 10.

[122]

Park S, Ransom C, Mei C, . The quest for alternatives to microbial cellulase mix production: corn stover-produced heterologous multi-cellulases readily deconstruct lignocellulosic biomass into fermentable sugars. J Chem Technol Biotechnol, 2011, 86: 633-641.

[123]

Park M, Sun Q, Liu F, . Positional assembly of enzymes on bacterial outer membrane vesicles for cascade reactions. PLoS ONE, 2014, 9: 1-6.

[124]

Patagundi BI, Shivasharan CT, Kaliwal BB. Isolation and characterization of cellulase producing bacteria from soil. Int J Curr Microbiol Appl Sci, 2014, 3: 59-69.

[125]

Pearsall SM, Rowley CN, Berry A. Advances in pathway engineering for natural product biosynthesis. ChemCatChem, 2015, 7: 3078-3093.

[126]

Percival Zhang YH. Production of biocommodities and bioelectricity by cell-free synthetic enzymatic pathway biotransformations: challenges and opportunities. Biotechnol Bioeng, 2010, 105: 663-667.

[127]

Percival Zhang YH, Himmel ME, Mielenz JR. Outlook for cellulase improvement: screening and selection strategies. Biotechnol Adv, 2006, 24: 452-481.

[128]

Pereira JH, Chen Z, McAndrew RP, . Biochemical characterization and crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima. J Struct Biol, 2010, 172: 372-379.

[129]

Perevalova AA. Desulfurococcus fermentans sp. nov., a novel hyperthermophilic archaeon from a Kamchatka hot spring, and emended description of the genus Desulfurococcus. Int J Syst Evol Microbiol, 2005, 55: 995-999.

[130]

Phillips CM, Beeson WT, Cate JH, Marletta MA. Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa. ACS Chem Biol, 2011, 6: 1399-1406.

[131]

Quinlan RJ, Sweeney MD, Lo Leggio L, . Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components. Proc Natl Acad Sci, 2011, 108: 15079-15084.

[132]

Rabinovich ML, Melnik MS, Bolobova AV. Microbial cellulases (review). Appl Biochem Microbiol, 2002, 38: 305-321.

[133]

Rajasree KP, Mathew GM, Pandey A, Sukumaran RK. Highly glucose tolerant β-glucosidase from Aspergillus unguis: NII 08123 for enhanced hydrolysis of biomass. J Ind Microbiol Biotechnol, 2013, 40: 967-975.

[134]

Reed PT, Izquierdo JA, Lynd LR. Cellulose fermentation by Clostridium thermocellum and a mixed consortium in an automated repetitive batch reactor. Bioresour Technol, 2014, 155: 50-56.

[135]

Ribeiro LF, Furtado GP, Lourenzoni MR, . Engineering bifunctional laccase-xylanase chimeras for improved catalytic performance. J Biol Chem, 2011, 286: 43026-43038.

[136]

Ribeiro LF, Nicholes N, Tullman J, . Insertion of a xylanase in xylose binding protein results in a xylose-stimulated xylanase. Biotechnol Biofuels, 2015, 8: 118.

[137]

Riou C, Salmon JM, Vallier MJ, . Purification, characterization, and substrate specificity of a novel highly glucose-tolerant beta-glucosidase from Aspergillus oryzae. Appl Environ Microbiol, 1998, 64: 3607-3614.

[138]

Roedl A. Production and energetic utilization of wood from short rotation coppice—a life cycle assessment. Int J Life Cycle Assess, 2010, 15: 567-578.

[139]

Rollin JA, Tam TK, Zhang YHP. New biotechnology paradigm: cell-free biosystems for biomanufacturing. Green Chem, 2013, 15: 1708-1719.

[140]

Sakthi SS, Saranraj P, Rajasekar M. Optimization for cellulase production by Aspergillus niger using paddy straw as substrate. Int J Adv Sci Tech Res, 2011, 1: 68-85.

[141]

Schiraldi C, De Rosa M. The production of biocatalysts and biomolecules from extremophiles. Trends Biotechnol, 2002, 20: 515-521.

[142]

Schoffelen S, van Hest JCM. Multi-enzyme systems: bringing enzymes together in vitro. Soft Matter, 2012, 8: 1736.

[143]

Schröder C, Elleuche S, Blank S, Antranikian G. Characterization of a heat-active archaeal β-glucosidase from a hydrothermal spring metagenome. Enzyme Microb Technol, 2014, 57: 48-54.

[144]

Schülein M. Protein engineering of cellulases. Biochim Biophys Acta Protein Struct Mol Enzymol, 2000, 1543: 239-252.

[145]

Schumacher SD, Hannemann F, Teese MG, . Autodisplay of functional CYP106A2 in Escherichia coli. J Biotechnol, 2012, 161: 104-112.

[146]

Schüürmann J, Quehl P, Festel G, Jose J. Bacterial whole-cell biocatalysts by surface display of enzymes: toward industrial application. Appl Microbiol Biotechnol, 2014, 98: 8031-8046.

[147]

Segato F, Damásio ARL, de Lucas RC, . Genome analyses highlight the different biological roles of cellulases. Microbiol Mol Biol Rev, 2014, 78: 588-613.

[148]

Shallom D, Shoham Y. Microbial hemicellulases. Curr Opin Microbiol, 2003, 6: 219-228.

[149]

Sharrock KR. Cellulase assay methods: a review. J Biochem Biophys Methods, 1988, 17: 81-105.

[150]

Sherief AA, El-Tanash AB, Atia N. Cellulase production by Aspergillus fumigatus grown on mixed substrate of rice straw and wheat bran. Res J Microbiol, 2010, 5: 199-211.

[151]

Shi R, Li Z, Ye Q, . Heterologous expression and characterization of a novel thermo-halotolerant endoglucanase Cel5H from Dictyoglomus thermophilum. Bioresour Technol, 2013, 142: 338-344.

[152]

Shin KC, Oh DK. Characterization of a novel recombinant B-glucosidase from Sphingopyxis alaskensis that specifically hydrolyzes the outer glucose at the C-3 position in protopanaxadiol-type ginsenosides. J Biotechnol, 2014, 172: 30-37.

[153]

Smith MR, Khera E, Wen F. Engineering novel and improved biocatalysts by cell surface display. Ind Eng Chem Res, 2015, 54: 4021-4032.

[154]

Sohail M, Siddiqi R, Ahmad A, Khan SA. Cellulase production from Aspergillus niger MS82: effect of temperature and pH. N Biotechnol, 2009, 25: 437-441.

[155]

Soni R, Nazir A, Chadha BS. Optimization of cellulase production by a versatile Aspergillus fumigatus fresenius strain (AMA) capable of efficient deinking and enzymatic hydrolysis of Solka floc and bagasse. Ind Crops Prod, 2010, 31: 277-283.

[156]

Stern J, Kahn A, Vazana Y, . Significance of relative position of cellulases in designer cellulosomes for optimized cellulolysis. PLoS ONE, 2015, 10: e0127326.

[157]

Tachaapaikoon C, Kosugi A, Pason P, . Isolation and characterization of a new cellulosome-producing Clostridium thermocellum strain. Biodegradation, 2012, 23: 57-68.

[158]

Tozakidis IEP, Quehl P, Schüürmann J, Jose J. Let’s do it outside: neue Biokatalysatoren mittels surface display. BIOspektrum, 2015, 21: 668-671.

[159]

Tozakidis IEP, Brossette T, Lenz F, . Proof of concept for the simplified breakdown of cellulose by combining Pseudomonas putida strains with surface displayed thermophilic endocellulase, exocellulase and β-glucosidase. Microb Cell Fact, 2016, 15: 103-114.

[160]

Turner NJ. Directed evolution of enzymes for applied biocatalysis. Trends Biotechnol, 2003, 21: 474-478.

[161]

Ulrich A, Klimke G, Wirth S. Diversity and activity of cellulose-decomposing bacteria, isolated from a sandy and a loamy soil after long-term manure application. Microb Ecol, 2008, 55: 512-522.

[162]

Vaaje-Kolstad G, Westereng B, Horn SJ, . An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides. Science, 2010, 330: 219-222.

[163]

van den Burg B. Extremophiles as a source for novel enzymes. Curr Opin Microbiol, 2003, 6: 213-218.

[164]

Varzakas T, Arapoglou D, Israilides C. Kinetics of endoglucanase and endoxylanase uptake by soybean seeds. J Biosci Bioeng, 2006, 101: 111-119.

[165]

Vieille C, Zeikus GJ. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev, 2001, 65: 1-43.

[166]

Wahlström R, Rahikainen J, Kruus K, Suurnäkki A. Cellulose hydrolysis and binding with Trichoderma reesei Cel5A and Cel7A and their core domains in ionic liquid solutions. Biotechnol Bioeng, 2014, 111: 726-733.

[167]

Walton PH, Davies GJ. On the catalytic mechanisms of lytic polysaccharide monooxygenases. Curr Opin Chem Biol, 2016, 31: 195-207.

[168]

Wang Z, Bay H, Chew K, Geng A. High-loading oil palm empty fruit bunch saccharification using cellulases from Trichoderma koningii MF6. Process Biochem, 2014, 49: 673-680.

[169]

Watanabe T, Sato T, Yoshioka S, . Purificication and properties of Aspergillus niger beta-glucosidase. Eur J Biochem, 1992, 209: 651-659.

[170]

Westereng B, Cannella D, Wittrup Agger J, . Enzymatic cellulose oxidation is linked to lignin by long-range electron transfer. Sci Rep, 2015, 5: 18561.

[171]

Willick GE, Seligy VL. Multiplicity in cellulases of Schizophyllum commune. Derivation partly from heterogeneity in transcription and glycosylation. Eur J Biochem, 1985, 151: 89-96.

[172]

Wilson DB. Cellulases and biofuels. Curr Opin Biotechnol, 2009, 20: 295-299.

[173]

Wilson DB (2015) Processive cellulases. Elsevier B.V

[174]

Wu T, Huang C, Ko T, . Diverse substrate recognition mechanism revealed by Thermotoga maritima Cel5A structures in complex with cellotetraose, cellobiose and mannotriose. Biochim Biophys Acta Proteins Proteom, 2011, 1814: 1832-1840.

[175]

Yagüe E, Béguin P, Aubert JP. Nucleotide sequence and deletion analysis of the cellulase-encoding gene celH of Clostridium thermocellum. Gene, 1990, 89: 61-67.

[176]

Yamada R, Hasunuma T, Kondo A. Endowing non-cellulolytic microorganisms with cellulolytic activity aiming for consolidated bioprocessing. Biotechnol Adv, 2013, 31: 754-763.

[177]

Yang S-J, Kataeva I, Hamilton-Brehm SD, . Efficient degradation of lignocellulosic plant biomass, without pretreatment, by the Thermophilic AnaerobeAnaerocellum thermophilum” DSM 6725. Appl Environ Microbiol, 2009, 75: 4762-4769.

[178]

Ye X, Rollin J, Zhang YP. Thermophilic α-glucan phosphorylase from Clostridium thermocellum: cloning, characterization and enhanced thermostability. J Mol Catal B Enzym, 2010, 65: 110-116.

[179]

Yuan S-F, Wu T-H, Lee H-L, . Biochemical characterization and structural analysis of a bifunctional cellulase/xylanase from Clostridium thermocellum. J Biol Chem, 2015, 290: 5739-5748.

[180]

Zechel DL, Withers SG. Glycosidase mechanisms: anatomy of a finely tuned catalyst. Acc Chem Res, 2000, 33: 11-18.

[181]

Zhang YHP. Substrate channeling and enzyme complexes for biotechnological applications. Biotechnol Adv, 2011, 29: 715-725.

[182]

Zhang Y-HP, Lynd LR. Toward an aggregated understanding of enzymatic hydrolysis of cellulose: noncomplexed cellulase systems. Biotechnol Bioeng, 2004, 88: 797-824.

[183]

Zhao L, Xie J, Zhang X, . Overexpression and characterization of a glucose-tolerant β-glucosidase from Thermotoga thermarum DSM 5069T with high catalytic efficiency of ginsenoside Rb1 to Rd. J Mol Catal B Enzym, 2013, 95: 62-69.

[184]

Zverlov VV, Velikodvorskaya GA, Schwarz WH. Two new cellulosome components encoded downstream of celI in the genome of Clostridium thermocellum: the non-processive endoglucanase CelN and the possibly structural protein CseP. Microbiology, 2003, 149: 515-524.

[185]

Zverlov VV, Schantz N, Schwarz WH. A major new component in the cellulosome of Clostridium thermocellum is a processive endo-β-1,4-glucanase producing cellotetraose. FEMS Microbiol Lett, 2005, 249: 353-358.

Funding

Autodisplay Biotech GmbH(GL00139)

AI Summary AI Mindmap
PDF

115

Accesses

0

Citation

Detail

Sections
Recommended

AI思维导图

/