Enzymatic deconstruction of plant biomass by fungal enzymes
Tóm tắt
Từ khóa
Tài liệu tham khảo
Cherubini, 2010, The biorefinery concept: using biomass instead of oil for producing energy and chemicals, Energ Convers Manage, 51, 1412, 10.1016/j.enconman.2010.01.015
McCann, 2015, Biomass recalcitrance: a multi-scale, multi-factor, and conversion-specific property, J Exp Bot, 66, 4109, 10.1093/jxb/erv267
Cragg, 2015, Lignocellulose degradation mechanisms across the Tree of Life, Curr Opin Chem Biol, 29, 108, 10.1016/j.cbpa.2015.10.018
Mäkelä, 2014, Plant biomass degradation by fungi, Fungal Genet Biol, 72, 2, 10.1016/j.fgb.2014.08.010
Kubicek, 2012
Druzhinina, 2016, Familiar stranger: ecological genomics of the model saprotroph and industrial enzyme producer Trichoderma reesei breaks the stereotypes, Adv Appl Microbiol, 95, 96
Gupta, 2016, Fungal enzymes for bio-products from sustainable and waste biomass, Trends Biochem Sci, 41, 631, 10.1016/j.tibs.2016.04.006
Beckham, 2014, Towards a molecular-level theory of carbohydrate processivity in glycoside hydrolases, Curr Opin Biotechnol, 27, 96, 10.1016/j.copbio.2013.12.002
Harris, 2014, New enzyme insights drive advances in commercial ethanol production, Curr Opin Chem Biol, 19, 162, 10.1016/j.cbpa.2014.02.015
Kurašin, 2011, Processivity of cellobiohydrolases is limited by the substrate, J Biol Chem, 286, 169, 10.1074/jbc.M110.161059
Brady, 2015, Cellobiohydrolase 1 from Trichoderma reesei degrades cellulose in single cellobiose steps, Nat Commun, 6, 10149, 10.1038/ncomms10149
Nakamura, 2014, Trade-off between processivity and hydrolytic velocity of cellobiohydrolases at the surface of crystalline cellulose, J Am Chem Soc, 136, 4584, 10.1021/ja4119994
Knott, 2014, The mechanism of cellulose hydrolysis by a two-step, retaining cellobiohydrolase elucidated by structural and transition path sampling studies, J Am Chem Soc, 136, 321, 10.1021/ja410291u
Knott, 2014, Carbohydrate–protein interactions that drive processive polysaccharide translocation in enzymes revealed from a computational study of cellobiohydrolase processivity, J Am Chem Soc, 136, 8810, 10.1021/ja504074g
Colussi, 2015, Probing substrate interactions in the active tunnel of a catalytically deficient cellobiohydrolase (Cel7), J Biol Chem, 290, 2444, 10.1074/jbc.M114.624163
Shang, 2013, Systems-level modeling with molecular resolution elucidates the rate-limiting mechanisms of cellulose decomposition by cellobiohydrolases, J Biol Chem, 288, 29081, 10.1074/jbc.M113.497412
Johansen, 2016, Discovery and industrial applications of lytic polysaccharide mono-oxygenases, Biochem Soc Trans, 44, 143, 10.1042/BST20150204
Corrêa, 2015, 9AA9 and AA10: from enigmatic to essential enzymes, Appl Microbiol Biotechnol
Morgenstern, 2014, Fungal cellulose degradation by oxidative enzymes: from dysfunctional GH61 family to powerful lytic polysaccharide monooxygenase family, Brief Funct Genomics, 13, 471, 10.1093/bfgp/elu032
Phillips, 2011, Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa, ACS Chem Biol, 6, 1399, 10.1021/cb200351y
Eibinger, 2014, Cellulose surface degradation by a lytic polysaccharide monooxygenase and its effect on cellulase hydrolytic efficiency, J Biol Chem, 289, 35929, 10.1074/jbc.M114.602227
Sun, 2015, Accessory enzymes influence cellulase hydrolysis of the model substrate and the realistic lignocellulosic biomass, Enzyme Microb Technol, 79–80, 42, 10.1016/j.enzmictec.2015.06.020
Agger, 2014, Discovery of LPMO activity on hemicelluloses shows the importance of oxidative processes in plant cell wall degradation, Proc Natl Acad Sci U S A, 111, 6287, 10.1073/pnas.1323629111
Borisova, 2015, Structural and functional characterization of a lytic polysaccharide monooxygenase with broad substrate specificity, J Biol Chem, 290, 22955, 10.1074/jbc.M115.660183
Müller, 2015, Harnessing the potential of LPMO-containing cellulase cocktails poses new demands on processing conditions, Biotechnol Biofuels, 8, 187, 10.1186/s13068-015-0376-y
Dimarogona, 2012, Lignin boosts the cellulase performance of a GH-61 enzyme from Sporotrichum thermophile, Bioresour Technol, 110, 480, 10.1016/j.biortech.2012.01.116
Hu, 2014, Substrate factors that influence the synergistic interaction of AA9 and cellulases during the enzymatic hydrolysis of biomass, Energy Environ Sci, 7, 2308, 10.1039/C4EE00891J
Rodríguez-Zuñiga, 2015, Lignocellulose pretreatment technologies affect the level of enzymatic cellulose oxidation by LPMO, Green Chem, 17, 2896, 10.1039/C4GC02179G
Várnai, 2014, Carbohydrate-binding modules of fungal cellulases: occurrence in nature, function, and relevance in industrial biomass conversion, Adv Appl Microbiol, 88, 103, 10.1016/B978-0-12-800260-5.00004-8
Walker, 2015, Multifunctional cellulase catalysis targeted by fusion to different carbohydrate-binding modules, Biotechnol Biofuels, 8, 220, 10.1186/s13068-015-0402-0
Inoue, 2015, Contribution of a family 1 carbohydrate-binding module in thermostable glycoside hydrolase 10 xylanase from Talaromyces cellulolyticus toward synergistic enzymatic hydrolysis of lignocellulose, Biotechnol Biofuels, 8, 77, 10.1186/s13068-015-0259-2
Várnai, 2013, Carbohydrate-binding modules (CBMs) revisited: reduced amount of water counterbalances the need for CBMs, Biotechnol Biofuels, 6, 30, 10.1186/1754-6834-6-30
Mello, 2014, Family 1 carbohydrate binding-modules enhance saccharification rates, AMB Express, 4, p36, 10.1186/s13568-014-0036-9
Strobel, 2016, Engineering Cel7A carbohydrate binding module and linker for reduced lignin inhibition, Biotechnol Bioeng, 113, 1369, 10.1002/bit.25889
Georgelis, 2015, Bacterial expansins and related proteins from the world of microbes, Appl Microbiol Biotechnol, 99, 3807, 10.1007/s00253-015-6534-0
Saloheimo, 2002, Swollenin, a Trichoderma reesei protein with sequence similarity to the plant expansins, exhibits disruption activity on cellulosic materials, Eur J Biochem, 269, 4202, 10.1046/j.1432-1033.2002.03095.x
Gourlay, 2013, Swollenin aids in the amorphogenesis step during the enzymatic hydrolysis of pretreated biomass, Bioresour Technol, 142, 498, 10.1016/j.biortech.2013.05.053
Andberg, 2015, Swollenin from Trichoderma reesei exhibits hydrolytic activity against cellulosic substrates with features of both endoglucanases and cellobiohydrolases, Bioresour Technol, 181, 105, 10.1016/j.biortech.2015.01.024
Sun, 2016, The role of pretreatment in improving the enzymatic hydrolysis of lignocellulosic materials, Bioresour Technol, 199, 49, 10.1016/j.biortech.2015.08.061
Silveira, 2015, Current pretreatment technologies for the development of cellulosic ethanol and biorefineries, ChemSusChem, 8, 3366, 10.1002/cssc.201500282
Xu, 2016, Advances in improving the performance of cellulase in ionic liquids for lignocellulose biorefinery, Bioresour Technol, 200, 961, 10.1016/j.biortech.2015.10.031
Nordwald, 2014, Charge engineering of cellulases improves ionic liquid tolerance and reduces lignin inhibition, Biotechnol Bioengin, 111, 1541, 10.1002/bit.25216
Wahlstrom, 2014, Cellulose hydrolysis and binding with Trichoderma reesei Cel5A and Cel7A and their core domains in ionic liquid solutions, Biotechnol Bioengin, 111, 726, 10.1002/bit.25144
Li, 2015, Ionic liquid induced inactivation of cellobiohydrolase I from Trichoderma reesei, Green Chem, 17, 1618, 10.1039/C4GC02136C
Wolski, 2016, Engineering ionic liquid-tolerant cellulases for biofuels production, Protein Eng Des Sel, 29, 117, 10.1093/protein/gzv066
Nguyen, 2015, Rheology of lignocellulose suspensions and impact of hydrolysis: a review, Adv Biochem Eng Biotechnol, 149, 325
Liguori, 2016, Bioreactors for lignocellulose conversion into fermentable sugars for production of high added value products, Appl Microbiol Biotechnol, 100, 597, 10.1007/s00253-015-7125-9
Viikari, 2007, Thermostable enzymes in lignocellulose hydrolysis, Adv Biochem Eng Biotechnol, 108, 121
Cobucci-Ponzano, 2013, Extremophilic (Hemi) cellulolytic microorganisms and enzymes, 111
Bhalla, 2013, Improved lignocellulose conversion to biofuels with thermophilic bacteria and thermostable enzymes, Bioresour Technol, 128, 751, 10.1016/j.biortech.2012.10.145
Heinzelman, 2010, Efficient screening of fungal cellobiohydrolase class I enzymes for thermostabilizing sequence blocks by SCHEMA structure-guided recombination, Protein Eng Des Sel, 23, 871, 10.1093/protein/gzq063
Heinzelman, 2009, SCHEMA recombination of a fungal cellulase uncovers a single mutation that contributes markedly to stability, J Biol Chem, 284, 26229, 10.1074/jbc.C109.034058
Komor, 2012, Highly thermostable fungal cellobiohydrolase I (Cel7A) engineered using predictive methods, Protein Eng Des Sel, 25, 827, 10.1093/protein/gzs058
Wu, 2013, Engineered thermostable fungal Cel6A and Cel7A cellobiohydrolases hydrolyze cellulose efficiently at elevated temperatures, Biotechnol Bioeng, 110, 1874, 10.1002/bit.24864