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Biomolecules  2013 

Fungal Beta-Glucosidases: A Bottleneck in Industrial Use of Lignocellulosic Materials

DOI: 10.3390/biom3030612

Keywords: beta-glucosidase, cellulase, biomass, hydrolysis, biofuels

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Abstract:

Profitable biomass conversion processes are highly dependent on the use of efficient enzymes for lignocellulose degradation. Among the cellulose degrading enzymes, beta-glucosidases are essential for efficient hydrolysis of cellulosic biomass as they relieve the inhibition of the cellobiohydrolases and endoglucanases by reducing cellobiose accumulation. In this review, we discuss the important role beta-glucosidases play in complex biomass hydrolysis and how they create a bottleneck in industrial use of lignocellulosic materials. An efficient beta-glucosidase facilitates hydrolysis at specified process conditions, and key points to consider in this respect are hydrolysis rate, inhibitors, and stability. Product inhibition impairing yields, thermal inactivation of enzymes, and the high cost of enzyme production are the main obstacles to commercial cellulose hydrolysis. Therefore, this sets the stage in the search for better alternatives to the currently available enzyme preparations either by improving known or screening for new beta-glucosidases.

References

[1]  Cherubini, F. The biorefinery concept: Using biomass instead of oil for producing energy and chemicals. Energy Conver. Manag. 2010, 51, 1412–1421, doi:10.1016/j.enconman.2010.01.015.
[2]  Knauf, M.; Moniruzzaman, M. Lignocellulosic biomass processing: A perspective. Int. Sugar J. 2004, 106, 147–150.
[3]  Werpy, T.; Petersen, G.; Aden, A.; Bozell, J.; Holladay, J.; White, J.; Manheim, A. Top Value added Chemicals from Biomass, Volume 1: Results of screening for potential candidates from sugars and synthesis gas; U.S. Department of Energy: Oak Ridge, TN, USA, 2004.
[4]  U.S. Department of Energy. Biomass Feedstock Composition and Property Database;
[5]  Lynd, L.R.; Weimer, P.J.; van Zyl, W.H.; Pretorius, I.S. Microbial cellulose utilization: Fundamentals and biotechnology. Microbiol. Mol. Biol. Rev. 2002, 66, 506–577, doi:10.1128/MMBR.66.3.506-577.2002.
[6]  Beguin, P.; Aubert, J.P. The biological degradation of cellulose. FEMS Microbiol. Rev. 1994, 13, 25–58, doi:10.1111/j.1574-6976.1994.tb00033.x.
[7]  Berg, J.M.; Tymoczko, J.L.; Stryer, L. Biochemistry, 5th ed. ed.; W.H. Freeman and Company: New York, NY, USA, 2002.
[8]  Alvira, P.; Tomas-Pejo, E.; Ballesteros, M.; Negro, M.J. Pretreatment technologies for an efficient bioethanol production process based on enzymatic hydrolysis: A review. Bioresour. Technol. 2010, 101, 4851–4861, doi:10.1016/j.biortech.2009.11.093.
[9]  Mosier, N.; Wyman, C.; Dale, B.; Elander, R.; Lee, Y.Y.; Holtzapple, M.; Ladisch, M. Features of promising technologies for pretreatment of lignocellulosic biomass. Bioresour. Technol. 2005, 96, 673–686, doi:10.1016/j.biortech.2004.06.025.
[10]  Sun, Y.; Cheng, J.Y. Hydrolysis of lignocellulosic materials for ethanol production: A review. Bioresour. Technol. 2002, 83, 1–11, doi:10.1016/S0960-8524(01)00212-7.
[11]  Zhang, Y.-P.; Himmel, M.E.; Mielenz, J.R. Outlook for cellulase improvement: Screening and selection strategies. Biotechnol. Adv. 2006, 24, 452–481, doi:10.1016/j.biotechadv.2006.03.003.
[12]  Kabel, M.A.; Bos, G.; Zeevalking, J.; Voragen, A.G.J.; Schols, H.A. Effect of pretreatment severity on xylan solubility and enzymatic breakdown of the remaining cellulose from wheat straw. Bioresour. Technol. 2007, 98, 2034–2042, doi:10.1016/j.biortech.2006.08.006.
[13]  Chang, V.S.; Holtzapple, M.T. Fundamental factors affecting biomass enzymatic reactivity. Appl. Biochem. Biotechnol. 2000, 84–86, 5–37, doi:10.1385/ABAB:84-86:1-9:5.
[14]  Meyer, A.S.; Rosgaard, L.; Sorensen, H.R. The minimal enzyme cocktail concept for biomass processing. J. Cereal. Sci. 2009, 50, 337–344, doi:10.1016/j.jcs.2009.01.010.
[15]  Zhang, Y.-P.; Lynd, L.R. Toward an aggregated understanding of enzymatic hydrolysis of cellulose: Noncomplexed cellulase systems. Biotechnol. Bioeng. 2004, 88, 797–824, doi:10.1002/bit.20282.
[16]  Wang, M.; Liu, K.; Dai, L.; Zhang, J.; Fang, X. The structural and biochemical basis for cellulose biodegradation. J. Chem. Technol. Biotechnol. 2013, 88, 491–500, doi:10.1002/jctb.3987.
[17]  Harris, P.V.; Welner, D.; McFarland, K.C.; Re, E.; Poulsen, J.N.; Brown, K.; Salbo, R.; Ding, H.; Vlasenko, E.; Merino, S.; Xu, F.; Cherry, J.; Larsen, S; Leggio, L.L. Stimulation of lignocellulosic biomass hydrolysis by proteins of glycoside hydrolase family 61: Structure and function of a large, enigmatic family. Biochemistry (N Y ) 2010, 49, 3305–3316, doi:10.1021/bi100009p.
[18]  Langston, J.A.; Shaghasi, T.; Abbate, E.; Xu, F.; Vlasenko, E.; Sweeney, M.D. Oxidoreductive cellulose depolymerization by the enzymes cellobiose dehydrogenase and glycoside hydrolase 61. Appl. Environ. Microbiol. 2011, 77, 7007–7015, doi:10.1128/AEM.05815-11.
[19]  Quinlan, R.J.; Sweeney, M.D.; lo Leggio, L.; Otten, H.; Poulsen, J.N.; Johansen, K.S.; Krogh, K.B.R.M.; J?rgensen, C.I.; Tovborg, M.; Anthonsen, A.; Tryfona, T.; Walter, C.P.; Dupree, P.; Xu, F.; Davies, G.J.; Walton, P.H. Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components. Proc. Natl. Acad. Sci. USA 2011, 108, 15079–15084, doi:10.1073/pnas.1105776108.
[20]  Vaaje-Kolstad, G.; Westereng, B.; Horn, S.J.; Liu, Z.; Zhai, H.; Sorlie, M.; Eijsink, V.G.H. An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides. Science 2010, 330, 219–222, doi:10.1126/science.1192231.
[21]  Lynd, L.R.; Laser, M.S.; Bransby, D.; Dale, B.E.; Davison, B.; Hamilton, R.; Himmel, M.; Keller, M.; McMillan, J.D.; Sheehan, J.; Wyman, C.E. How biotech can transform biofuels. Nat. Biotechnol. 2008, 26, 169–172.
[22]  Banerjee, G.; Scott-Craig, J.S.; Walton, J.D. Improving enzymes for biomass conversion: A basic research perspective. Bioenergy Res. 2010, 3, 82–92, doi:10.1007/s12155-009-9067-5.
[23]  Kristensen, J.B.; Felby, C.; Jorgensen, H. Yield-determining factors in high-solids enzymatic hydrolysis of lignocellulose. Biotechnol. Biofuels 2009, 2, 11, doi:10.1186/1754-6834-2-11.
[24]  Kaar, W.; Holtzapple, M. Using lime pretreatment to facilitate the enzymic hydrolysis of corn stover. Biomass Bioenergy 2000, 18, 189–199, doi:10.1016/S0961-9534(99)00091-4.
[25]  Kim, S.; Holtzapple, M. Lime pretreatment and enzymatic hydrolysis of corn stover. Bioresour. Technol. 2005, 96, 1994–2006, doi:10.1016/j.biortech.2005.01.014.
[26]  Kim, T.; Lee, Y. Pretreatment of corn stover by soaking in aqueous ammonia. Appl. Biochem. Biotechnol. 2005, 124, 1119–1131, doi:10.1385/ABAB:124:1-3:1119.
[27]  Bura, R.; Chandra, R.; Saddler, J. Influence of xylan on the enzymatic hydrolysis of steam-pretreated corn stover and hybrid poplar. Biotechnol. Prog. 2009, 25, 315–322, doi:10.1002/btpr.98.
[28]  Zhu, J.Y.; Zhu, W.; OBryan, P.; Dien, B.S.; Tian, S.; Gleisner, R.; Pan, X.J. Ethanol production from SPORL-pretreated lodgepole pine: Preliminary evaluation of mass balance and process energy efficiency. Appl. Microbiol. Biotechnol. 2010, 86, 1355–1365, doi:10.1007/s00253-009-2408-7.
[29]  Yang, J.; Zhang, X.; Yong, Q.; Yu, S. Three-stage enzymatic hydrolysis of steam-exploded corn stover at high substrate concentration. Bioresour. Technol. 2011, 102, 4905–4908, doi:10.1016/j.biortech.2010.12.047.
[30]  Murphy, L.; Bohlin, C.; Baumann, M.J.; Olsen, S.N.; Sorensen, T.H.; Anderson, L.; Borch, K.; Westh, P. Product inhibition of five Hypocrea jecorina cellulases. Enzyme Microb. Technol. 2013, 52, 163–169, doi:10.1016/j.enzmictec.2013.01.002.
[31]  Shewale, J.G. Beta-Glucosidase - its role in cellulase synthesis and hydrolysis of cellulose. Int. J. Biochem. 1982, 14, 435–443, doi:10.1016/0020-711X(82)90109-4.
[32]  Xiao, Z.Z.; Zhang, X.; Gregg, D.J.; Saddler, J.N. Effects of sugar inhibition on cellulases and beta-glucosidase during enzymatic hydrolysis of softwood substrates. Appl. Biochem. Biotechnol. 2004, 113–116, 1115–1126.
[33]  Peterson, R.; Nevalainen, H. Trichoderma reesei RUT-C30 - thirty years of strain improvement. Microbiology 2012, 158, 58–68, doi:10.1099/mic.0.054031-0.
[34]  Reczey, K.; Brumbauer, A.; Bollok, M.; Szengyel, Z.; Zacchi, G. Use of hemicellulose hydrolysate for beta-glucosidase fermentation. Appl. Biochem. Biotechnol. 1998, 70–72, 225–235, doi:10.1007/BF02920139.
[35]  Rahman, Z.; Shida, Y.; Furukawa, T.; Suzuki, Y.; Okada, H.; Ogasawara, W.; Morikawa, Y. Application of Trichoderma reesei cellulase and xylanase promoters through homologous recombination for enhanced production of extracellular beta-glucosidase I. Biosci. Biotechnol. Biochem. 2009, 73, 1083–1089, doi:10.1271/bbb.80852.
[36]  Murray, P.; Aro, N.; Collins, C.; Grassick, A.; Penttila, M.; Saloheimo, M.; Tuohy, M. Expression in Trichoderma reesei and characterisation of a thermostable family 3 beta-glucosidase from the moderately thermophilic fungus Talaromyces emersonii. Protein Expr. Purif. 2004, 38, 248–257.
[37]  Merino, S.T.; Cherry, J. Progress and challenges in enzyme development for Biomass utilization. Biofuels 2007, 108, 95–120, doi:10.1007/10_2007_066.
[38]  S?rensen, A.; Ahring, B.K.; Lübeck, M.; Ubhayasekera, W.; Bruno, K.S.; Culley, D.E.; Lübeck, P.S. Identifying and characterizing the most significant beta-glucosidase of the novel species Aspergillus saccharolyticus. Can. J. Microbiol. 2012, 58, 1035–1046, doi:10.1139/w2012-076.
[39]  Nakazawa, H.; Kawai, T.; Ida, N.; Shida, Y.; Kobayashi, Y.; Okada, H.; Tani, S.; Sumitani, J. Kawaguchi, T.; Morikawa, Y.; Ogasawara, W. Construction of a recombinant Trichoderma reesei strain expressing Aspergillus aculeatus beta-glucosidase 1 for efficient biomass conversion. Biotechnol. Bioeng. 2012, 109, 92–99.
[40]  Dekker, R.F.H. Kinetic, inhibition, and stability properties of a commercial beta-D-glucosidase (cellobiase) preparation from Aspergillus niger and its suitability in the hydrolysis of lignocellulose. Biotechnol. Bioeng. 1986, 28, 1438–1442, doi:10.1002/bit.260280918.
[41]  Krogh, K.B.R.; Morkeberg, A.; Jorgensen, H.; Frisvad, J.C.; Olsson, L. Screening genus Penicillium for producers of cellulolytic and xylanolytic enzymes. Appl. Biochem. Biotechnol. 2004, 113–116, 389–401.
[42]  Liu, D.; Zhang, R.; Yang, X.; Zhang, Z.; Song, S.; Miao, Y.; Shen, Q. Characterization of a thermostable beta-glucosidase from Aspergillus fumigatus Z5, and its functional expression in Pichia pastoris X33. Microb. Cell Factories 2012, 11, 25, doi:10.1186/1475-2859-11-25.
[43]  Gyalai-Korpos, M.; Mangel, R.; Alvira, P.; Dienes, D.; Ballesteros, M.; Reczey, K. Cellulase production using different streams of wheat grain- and wheat straw-based ethanol processes. J. Ind. Microbiol. Biotechnol. 2011, 38, 791–802, doi:10.1007/s10295-010-0811-9.
[44]  S?rensen, A.; Teller, P.J.; Lübeck, P.S.; Ahring, B.K. Onsite enzyme production during bioethanol production from biomass: Screening for suitable fungal strains. Appl. Biochem. Biotechnol. 2011, 164, 1058–1070, doi:10.1007/s12010-011-9194-2.
[45]  Herculano, P.N.; Porto, T.S.; Moreira, K.A.; Pinto, G.A.S.; Souza-Motta, C.M.; Porto, A.L.F. Cellulase production by Aspergillus japonicus URM5620 Using Waste from Castor Bean (Ricinus communis L.) Under Solid-State Fermentation. Appl. Biochem. Biotechnol. 2011, 165, 1057–1067, doi:10.1007/s12010-011-9321-0.
[46]  Bairoch, A. The ENZYME database in 2000. Nucleic Acids Res. 2000, 28, 304–305, doi:10.1093/nar/28.1.304.
[47]  Eyzaguirre, J.; Hidalgo, M.; Leschot, A. Beta-Glucosidases from Filamentous Fungi: Properties, Structure, and Applications. In Handbook of Carbohydrate Engineering; Taylor and Francis Group, LLC: Boca Raton, FL 33487, USA, 2005; pp. 645–685.
[48]  Henrissat, B. A classification of glycosyl hydrolases based on amino-acid-sequence similarities. Biochem. J. 1991, 280, 309–316.
[49]  Bairoch, A. Prosite - a dictionary of sites and patterns in proteins. Nucleic Acids Res. 1992, 20, 2013–2018, doi:10.1093/nar/20.suppl.2013.
[50]  Varghese, J.N.; Hrmova, M.; Fincher, G.B. Three-dimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase. Structure 1999, 7, 179–190, doi:10.1016/S0969-2126(99)80024-0.
[51]  Yoshida, E.; Hidaka, M.; Fushinobu, S.; Koyanagi, T.; Minami, H.; Tamaki, H.; Kitaoka, M.; Katayama, T.; Kumagai, H. Purification, crystallization and preliminary X-ray analysis of beta-glucosidase from Kluyveromyces marxianus NBRC1777. Acta Crystallogr. Sect. F-Struct. Biol. Cryst. Commun. 2009, 65, 1190–1192, doi:10.1107/S1744309109042948.
[52]  Pozzo, T.; Pasten, J.L.; Karlsson, E.N.; Logan, D.T. Structural and functional analyses of beta-glucosidase 3B from Thermotoga neapolitana: A thermostable three-domain representative of glycoside hydrolase 3. J. Mol. Biol. 2010, 397, 724–739, doi:10.1016/j.jmb.2010.01.072.
[53]  Nakatani, Y.; Cutfield, S.M.; Cowieson, N.P.; Cutfield, J.F. Structure and activity of exo-1,3/1,4- beta-glucanase from marine bacterium Pseudoalteromonas sp BB1 showing a novel C-terminal domain. Febs. J. 2012, 279, 464–478, doi:10.1111/j.1742-4658.2011.08439.x.
[54]  McAndrew, R.P.; Park, J.I.; Heins, R.A.; Reindl, W.; Friedland, G.D.; D’haeseleer, P.; Northen, T.; Sale, K.L.; Simmons, B.A.; Adams, P.D. From soil to structure, a novel dimeric beta-glucosidase belonging to the glycoside hydrolase family 3 isolated from compost using metagenomic analysis. J. Biol. Chem. 2013, 288, 14985–14992, doi:10.1074/jbc.M113.458356.
[55]  Suzuki, K.; Sumitani, J.; Nam, Y.; Nishimaki, T.; Tani, S.; Wakagi, T.; Kawaguchi, T.; Fushinobu, S. Crystal structures of glycoside hydrolase family 3 β-glucosidase 1 from Aspergillus aculeatus. Biochem. J. 2013, 452, 211–221, doi:10.1042/BJ20130054.
[56]  Jeya, M.; Joo, A.; Lee, K.; Tiwari, M.K.; Lee, K.; Kim, S.; Lee, J. Characterization of beta-glucosidase from a strain of Penicillium purpurogenum KJS506. Appl. Microbiol. Biotechnol. 2010, 86, 1473–1484, doi:10.1007/s00253-009-2395-8.
[57]  Sinnott, M.L. Catalytic mechanisms of enzymatic glycosyl transfer. Chem. Rev. 1990, 90, 1171–1202, doi:10.1021/cr00105a006.
[58]  McCarter, J.D.; Withers, S.G. Mechanisms of enzymatic glycoside hydrolysis. Curr. Opin. Struct. Biol. 1994, 4, 885–892, doi:10.1016/0959-440X(94)90271-2.
[59]  Thongpoo, P.; McKee, L.S.; Araujo, A.C.; Kongsaeree, P.T.; Brumer, H. Identification of the acid/base catalyst of a glycoside hydrolase family 3 (GH3) beta-glucosidase from Aspergillus niger ASKU28. Biochim. Biophys. Acta-Gen. 2013, 1830, 2739–2749, doi:10.1016/j.bbagen.2012.11.014.
[60]  Davies, G.; Henrissat, B. Structures and mechanisms of glycosyl hydrolases. Structure 1995, 3, 853–859, doi:10.1016/S0969-2126(01)00220-9.
[61]  Davies, G.J.; Wilson, K.S.; Henrissat, B. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem. J. 1997, 321, 557–559.
[62]  Bhatia, Y.; Mishra, S.; Bisaria, V.S. Microbial beta-glucosidases: Cloning, properties, and applications. Crit. Rev. Biotechnol. 2002, 22, 375–407, doi:10.1080/07388550290789568.
[63]  Zahoor, S.; Javed, M.M.; Aftab, S.; Latif, F.; Ikram-ul-Haq. Metabolic engineering and thermodynamic characterization of an extracellular beta-glucosidase produced by Aspergillus niger. Afr. J. Biotechnol. 2011, 10, 8107–8116.
[64]  Elshafei, A.M.; Hassan, M.M.; Morsi, N.M.; Elghonamy, D.H. Purification and some kinetic properties of beta-glucosidase from Aspergillus terreus NRRL 265. Afr. J. Biotechnol. 2011, 10, 19556–19569.
[65]  Karnchanatat, A.; Petsom, A.; Sangvanich, P.; Piaphukiew, J.; Whalley, A.J.S.; Reynolds, C.D.; Sihanonth, P. Purification and biochemical characterization of an extracellular beta glucosidase from the wood-decaying fungus Daldinia eschscholzii (Ehrenb. :Fr.) Rehm. FEMS Microbiol lett. 2007, 270, 162–170, doi:10.1111/j.1574-6968.2007.00662.x.
[66]  Yoon, J.; Kim, K.; Cha, C. Purification and characterization of thermostable beta-glucosidase from the brown-rot basidiomycete Fomitopsis palustris grown on microcrystalline cellulose. J. Microbiol. 2008, 46, 51–55, doi:10.1007/s12275-007-0230-4.
[67]  Bhatti, H.N.; Batool, S.; Afzal, N. Production and characterization of a novel beta-glucosidase from Fusarium solani. Int. J. Agric. Biol. 2013, 15, 140–144.
[68]  Kalyani, D.; Lee, K.; Tiwari, M.K.; Ramachandran, P.; Kim, H.; Kim, I.; Jeya, M.; Lee, J. Characterization of a recombinant aryl beta-glucosidase from Neosartorya fischeri NRRL181. Appl. Microbiol. Biotechnol. 2012, 94, 413–423, doi:10.1007/s00253-011-3631-6.
[69]  Moreira Souza, F.H.; Nascimento, C.V.; Rosa, J.C.; Masui, D.C.; Leone, F.A.; Jorge, J.A.; Furriel, R.P.M. Purification and biochemical characterization of a mycelial glucose- and xylose-stimulated beta-glucosidase from the thermophilic fungus Humicola insolens. Process Biochem. 2010, 45, 272–278, doi:10.1016/j.procbio.2009.09.018.
[70]  Ramani, G.; Meera, B.; Vanitha, C.; Rao, M.; Gunasekaran, P. Production, purification, and characterization of a beta-glucosidase of Penicillium funiculosum NCL1. Appl. Biochem. Biotechnol. 2012, 167, 959–972, doi:10.1007/s12010-012-9645-4.
[71]  Choi, J.; Park, A.; Kim, Y.J.; Kim, J.; Cha, C.; Yoon, J. Purification and characterization of an extracellular beta-glucosidase produced by Phoma sp KCTC11825BP isolated from rotten mandarin peel. J. Microbiol. Biotechnol. 2011, 21, 503–508, doi:10.4014/jmb.1102.02014.
[72]  Zhang, Y.B.; Yuan, L.J.; Chen, Z.J.; Fu, L.; Lu, J.H.; Meng, Q.F.; He, H.; Yu, X.X.; Lin, F.; Teng, L.R. Purification and characterization of beta-glucosidase from a newly isolated strain Tolypocladium cylindrosporum Syzx4. Chem. Res. Chin. Univ. 2011, 27, 557–561.
[73]  Lin, J.; Pillay, B.; Singh, S. Purification and biochemical characteristics of beta-D-glucosidase from a thermophilic fungus, Thermomyces lanuginosus SSBP. Biotechnol. Appl. Biochem. 1999, 30, 81–87.
[74]  Chen, P.; Fu, X.Y.; Ng, T.B.; Ye, X.Y. Expression of a secretory beta-glucosidase from Trichoderma reesei in Pichia pastoris and its characterization. Biotechnol. Lett. 2011, 33, 2475–2479, doi:10.1007/s10529-011-0724-3.
[75]  Kubicek, C.P.; Herrera-Estrella, A.; Seidl-Seiboth, V.; Martinez, D.A.; Druzhinina, I.S.; Thon, M.; Zeilinger, S.; Casas-Flores, S.; Horwitz, B.A.; Mukherjee, P.K.; Mukherjee, M.; Kredics, L.; Alcaraz, L.D.; Aerts, A.; Antal, Z.; Atanasova, L.; Cervantes-Badillo, M.G.; Challacombe, J.; Chertkov, O.; McCluskey, K.; Coulpier, F.; Deshpande, N.; von D?hren, H.; Ebbole, D.J.; Esquivel-Naranjo, E.U.; Fekete, E.; Flipphi, M.; Glaser, F.; Gómez-Rodríguez, E.Y.; Gruber, S.; Han, C.; Henrissat, B.; Hermosa, R.; Hernández-O?ate, M.; Karaffa, L.; Kosti, I.; Le Crom, S.; Lindquist, E.; Lucas, S.; Lübeck, M.; Lübeck, P.S.; Margeot, A.; Metz, B.; Misra, M.; Nevalainen, H.; Omann, M.; Packer, N.; Perrone, G.; Uresti-Rivera, E.E.; Salamov, A.; Schmoll, M.; Seiboth, B.; Shapiro, H.; Sukno, S.; Tamayo-Ramos, J.A.; Tisch, D.; Wiest, A.; Wilkinson, H.H.; Zhang, M.; Coutinho, P.M.; Kenerley, C.M.; Monte, E.; Baker, S.E; Grigoriev, I.V. Comparative genome sequence analysis underscores mycoparasitism as the ancestral life style of Trichoderma. Genome Biol. 2011, 12, R40, doi:10.1186/gb-2011-12-4-r40.
[76]  Yan, S.; Wu, G. Prediction of optimal pH in hydrolytic reaction of beta-glucosidase. Appl. Biochem. Biotechnol. 2013, 169, 1884–1894, doi:10.1007/s12010-013-0103-8.
[77]  Banerjee, S.; Mudliar, S.; Sen, R.; Giri, B.; Satpute, D.; Chakrabarti, T.; Pandey, R.A. Commercializing lignocellulosic bioethanol: Technology bottlenecks and possible remedies. Biofuels Bioprod. Bioref. 2010, 4, 77–93, doi:10.1002/bbb.188.
[78]  Jeoh, T.; Michener, W.; Himmel, M.E.; Decker, S.R.; Adney, W.S. Implications of cellobiohydrolase glycosylation for use in biomass conversion. Biotechnol. Biofuels 2008, 1, 10.
[79]  Banerjee, G.; Car, S.; Scott-Craig, J.S.; Borrusch, M.S.; Bongers, M.; Walton, J.D. Synthetic multi-component enzyme mixtures for deconstruction of lignocellulosic biomass. Bioresour. Technol. 2010, 101, 9097–9105, doi:10.1016/j.biortech.2010.07.028.
[80]  Riou, C.; Salmon, J.M.; Vallier, M.J.; Gunata, Z.; Barre, P. Purification, characterization, and substrate specificity of a novel highly glucose-tolerant beta-glucosidase from Aspergillus oryzae. Appl. Environ. Microbiol. 1998, 64, 3607–3614.
[81]  Langston, J.; Sheehy, N.; Xu, F. Substrate specificity of Aspergillus oryzae family 3 beta-glucosidase. Biochim. Biophys. Acta-Proteins Proteomics 2006, 1764, 972–978, doi:10.1016/j.bbapap.2006.03.009.
[82]  Korotkova, O.G.; Semenova, M.V.; Morozova, V.V.; Zorov, I.N.; Sokolova, L.M.; Bubnova, T.M.; Okunev, O.N.; Sinitsyn, A.P. Isolation and properties of fungal beta-glucosidases. Biochemistry (Mosc) 2009, 74, 569–577, doi:10.1134/S0006297909050137.
[83]  Andric, P.; Meyer, A.S.; Jensen, P.A.; Dam-Johansen, K. Reactor design for minimizing product inhibition during enzymatic lignocellulose hydrolysis: I. Significance and mechanism of cellobiose and glucose inhibition on cellulolytic enzymes. Biotechnol. Adv. 2010, 28, 308–324, doi:10.1016/j.biotechadv.2010.01.003.
[84]  Dale, M.P.; Ensley, H.E.; Kern, K.; Sastry, K.A.R.; Byers, L.D. Reversible inhibitors of beta-glucosidase. Biochemistry (N Y) 1985, 24, 3530–3539, doi:10.1021/bi00335a022.
[85]  Bohlin, C.; Praestgaard, E.; Baumann, M.J.; Borch, K.; Praestgaard, J.; Monrad, R.N.; Westh, P. A comparative study of hydrolysis and transglycosylation activities of fungal beta-glucosidases. Appl. Microbiol. Biotechnol. 2013, 97, 159–169, doi:10.1007/s00253-012-3875-9.
[86]  Frutuoso, M.A.; Marana, S.R. A single amino acid residue determines the ratio of hydrolysis to transglycosylation catalyzed by beta-glucosidases. Protein Peptide Lett. 2013, 20, 102–106, doi:10.2174/092986613804096757.
[87]  McIntosh, L.P.; Hand, G.; Johnson, P.E.; Joshi, M.D.; Korner, M.; Plesniak, L.A.; Ziser, L.; Wakarchuk, W.W.; Withers, S.G. The pKa of the general acid/base carboxyl group of a glycosidase cycles during catalysis: A C-13-NMR study of Bacillus circuluns xylanase. Biochemistry (N Y) 1996, 35, 9958–9966, doi:10.1021/bi9613234.
[88]  Yeoman, C.J.; Han, Y.; Dodd, D.; Schroeder, C.M.; Mackie, R.I.; Cann, I.K.O. Thermostable enzymes as biocatalysts in the biofuel industry. Adv. Appl. Microbiol. 2010, 70, 1–55, doi:10.1016/S0065-2164(10)70001-0.
[89]  Berlin, A.; Balakshin, M.; Gilkes, N.; Kadla, J.; Maximenko, V.; Kubo, S.; Saddler, J. Inhibition of cellulase, xylanase and beta-glucosidase activities by softwood lignin preparations. J. Biotechnol. 2006, 125, 198–209, doi:10.1016/j.jbiotec.2006.02.021.
[90]  Yang, B.; Wyman, C.E. BSA treatment to enhance enzymatic hydrolysis of cellulose in lignin containing substrates. Biotechnol. Bioeng. 2006, 94, 611–617, doi:10.1002/bit.20750.
[91]  Selig, M.J.; Hsieh, C.C.; Thygesen, L.G.; Himmel, M.E.; Felby, C.; Decker, S.R. Considering water availability and the effect of solute concentration on high solids saccharification of lignocellulosic biomass. Biotechnol. Prog. 2012, 28, 1478–1490, doi:10.1002/btpr.1617.
[92]  Hawksworth, D.L. The fungal dimension of biodiversity - Magnitude, significance, and conservation. Mycol. Res. 1991, 95, 641–655, doi:10.1016/S0953-7562(09)80810-1.
[93]  Hawksworth, D.L. The magnitude of fungal diversity: The 1.5 million species estimate revisited. Mycol. Res. 2001, 105, 1422–1432, doi:10.1017/S0953756201004725.
[94]  Mares, D.; Andreotti, E.; Maldonado, M.E.; Pedrini, P.; Colalongo, C.; Romagnoli, C. Three new species of Aspergillus from Amazonian forest soil (Ecuador). Curr. Microbiol. 2008, 57, 222–229, doi:10.1007/s00284-008-9178-9.
[95]  De Vries, R.P.; Frisvad, J.C.; van de Vondervoort, P.J.I.; Burgers, K.; Kuijpers, A.F.A.; Samson, R.A.; Visser, J. Aspergillus vadensis, a new species of the group of black Aspergilli. Antonie Van Leeuwenhoek 2005, 87, 195–203, doi:10.1007/s10482-004-3194-y.
[96]  Samson, R.A.; Houbraken, J.A.M.P.; Kuijpers, A.F.A.; Frank, J.M.; Frisvad, J.C. New ochratoxin A or sclerotium producing species in Aspergillus section Nigri. Stud. Mycol. 2004, 50, 45–61.
[97]  Perrone, G.; Varga, J.; Susca, A.; Frisvad, J.C.; Stea, G.; Kocsube, S.; Tóth, B.; Kozakiewicz, Z.; Samson, R.A. Aspergillus uvarum sp nov., an uniseriate black Aspergillus species isolated from grapes in Europe. Int. J. Syst. Evol. Microbiol. 2008, 58, 1032–1039, doi:10.1099/ijs.0.65463-0.
[98]  Noonim, P.; Mahakarnchanakul, W.; Varga, J.; Frisvad, J.C.; Samson, R.A. Two novel species of Aspergillus section Nigri from Thai coffee beans. Int. J. Syst. Evol. Microbiol. 2008, 58, 1727–1734, doi:10.1099/ijs.0.65694-0.
[99]  Noonim, P.; Mahakarnchanakul, W.; Nielsen, K.F.; Frisvad, J.C.; Samson, R.A. Isolation, identification and toxigenic potential of ochratoxin A-producing Aspergillus species from coffee beans grown in two regions of Thailand. Int. J. Food Microbiol. 2008, 128, 197–202, doi:10.1016/j.ijfoodmicro.2008.08.005.
[100]  Varga, J.; Kocsube, S.; Toth, B.; Frisvad, J.C.; Perrone, G.; Susca, A.; Meijer, M.; Samson, R.A. Aspergillus brasiliensis sp nov., a biseriate black Aspergillus species with world-wide distribution. Int. J. Syst. Evol. Microbiol. 2007, 57, 1925–1932, doi:10.1099/ijs.0.65021-0.
[101]  Serra, R.; Cabanes, F.J.; Perrone, G.; Castella, G.; Venancio, A.; Mule, G.; Kozakiewicz, Z. Aspergillus ibericus: A new species of section Nigri isolated from grapes. Mycologia 2006, 98, 295–306, doi:10.3852/mycologia.98.2.295.
[102]  S?rensen, A.; Lubeck, P.S.; Lubeck, M.; Nielsen, K.F.; Ahring, B.K.; Teller, P.J.; Frisvad, J.C. Aspergillus saccharolyticus sp nov., a black Aspergillus species isolated in Denmark. Int. J. Syst. Evol. Microbiol. 2011, 61, 3077–3083, doi:10.1099/ijs.0.029884-0.
[103]  Kim, S.; Lee, C.; Kim, M.; Yeo, Y.; Yoon, S.; Kang, H.; Koo, B. Screening and characterization of an enzyme with beta-glucosidase activity from environmental DNA. J. Microbiol. Biotechnol. 2007, 17, 905–912.
[104]  Jiang, C.; Ma, G.; Li, S.; Hu, T.; Che, Z.; Shen, P.; Yan, B.; Wu, B. Characterization of a novel beta-glucosidase-like activity from a soil metagenome. J. Microbiol. 2009, 47, 542–548, doi:10.1007/s12275-009-0024-y.
[105]  Jiang, C.; Hao, Z.; Jin, K.; Li, S.; Che, Z.; Ma, G.; Wu, B. Identification of a metagenome-derived beta-glucosidase from bioreactor contents. J. Mol. Catal. B-Enzym. 2010, 63, 11–16, doi:10.1016/j.molcatb.2009.11.009.
[106]  Sternberg, D.; Vijayakumar, P.; Reese, E.T. Beta-glucosidase - microbial-production and effect on enzymatic-hydrolysis of cellulose. Can. J. Microbiol. 1977, 23, 139–147, doi:10.1139/m77-020.
[107]  S?rensen, A.; Lübeck, P.S.; Lübeck, M.; Teller, P.J.; Ahring, B.K. Beta-Glucosidases from a new Aspergillus species can substitute commercial beta-glucosidases for saccharification of lignocellulosic biomass. Can. J. Microbiol. 2011, 57, 638–650, doi:10.1139/w11-052.
[108]  Montenecourt, B.S.; Eveleigh, D.E. Selective screening methods for the isolation of high yielding cellulase mutants of Trichoderma reesei. In Hydrolysis of Cellulose: Mechanisms of Enzymic and Acid Catalysis; Brown, R.D., Jurasek, L., Eds.; American Chemical Society: Washington DC, USA, 1979; pp. 289–301.
[109]  Chirumamilla, R.R.; Muralidhar, R.; Marchant, R.; Nigam, P. Improving the quality of industrially important enzymes by directed evolution. Mol. Cell. Biochem. 2001, 224, 159–168, doi:10.1023/A:1011904405002.
[110]  Cherry, J.R.; Fidantsef, A.L. Directed evolution of industrial enzymes: An update. Curr. Opin. Biotechnol. 2003, 14, 438–443, doi:10.1016/S0958-1669(03)00099-5.
[111]  Tobin, M.B.; Gustafsson, C.; Huisman, G.W. Directed evolution: The ‘rational’ basis for ‘irrational’ design. Curr. Opin. Struct. Biol. 2000, 10, 421–427, doi:10.1016/S0959-440X(00)00109-3.
[112]  Antikainen, N.M.; Martin, S.F. Altering protein specificity: Techniques and applications. Bioorg. Med. Chem. 2005, 13, 2701–2716, doi:10.1016/j.bmc.2005.01.059.
[113]  Gonzalez-Blasco, G.; Sanz-Aparicio, J.; Gonzalez, B.; Hermoso, J.A.; Polaina, J. Directed evolution of beta-glucosidase A from Paenibacillus polymyxa to thermal resistance. J. Biol. Chem. 2000, 275, 13708–13712.
[114]  Arrizubieta, M.J.; Polaina, J. Increased thermal resistance and modification of the catalytic properties of a beta-glucosidase by random mutagenesis and in vitro recombination. J. Biol. Chem. 2000, 275, 28843–28848, doi:10.1074/jbc.M003036200.
[115]  Lebbink, J.H.G.; Kaper, T.; Bron, P.; van der Oost, J.; de Vos, W.M. Improving low-temperature catalysis in the hyperthermostable Pyrococcus furiosus beta-glucosidase CelB by directed evolution. Biochemistry (N Y) 2000, 39, 3656–3665, doi:10.1021/bi991483q.
[116]  Pei, X.; Yi, Z.; Tang, C.; Wu, Z. Three amino acid changes contribute markedly to the thermostability of beta-glucosidase BglC from Thermobifida fusca. Bioresour. Technol. 2011, 102, 3337–3342, doi:10.1016/j.biortech.2010.11.025.
[117]  Steiner, K.; Schwab, H. Recent Advances in rational approaches for enzyme engineering. Comput. Struct. Biotechnol. J. 2012, 2, doi:10.5936/csbj.201209010.
[118]  Lee, H.; Chang, C.; Jeng, W.; Wang, A.H.-J; Liang, P. Mutations in the substrate entrance region of beta-glucosidase from Trichoderma reesei improve enzyme activity and thermostability. Protein Eng. Des. Sel. 2012, 25, 733–740, doi:10.1093/protein/gzs073.

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