Boosting of enzymatic softwood saccharification by fungal GH5 and GH26 endomannanases

Biotechnology for Biofuels - Tập 11 - Trang 1-14 - 2018
Pernille von Freiesleben1,2, Nikolaj Spodsberg1, Anne Stenbæk1, Henrik Stålbrand3, Kristian B. R. M. Krogh1, Anne S. Meyer2
1Novozymes A/S, Bagsvaerd, Denmark
2Protein Chemistry & Enzyme Technology, DTU Bioengineering, Technical University of Denmark, Kgs. Lyngby, Denmark
3Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, Lund, Sweden

Tóm tắt

Softwood is a promising feedstock for lignocellulosic biorefineries, but as it contains galactoglucomannan efficient mannan-degrading enzymes are required to unlock its full potential. Boosting of the saccharification of pretreated softwood (Canadian lodgepole pine) was investigated for 10 fungal endo-β(1→4)-mannanases (endomannanases) from GH5 and GH26, including 6 novel GH26 enzymes. The endomannanases from Trichoderma reesei (TresMan5A) and Podospora anserina (PansMan26) were investigated with and without their carbohydrate-binding module (CBM). The pH optimum and initial rates of enzyme catalysed hydrolysis were determined on pure β-mannans, including acetylated and deacetylated spruce galactoglucomannan. Melting temperature (Tm) and stability of the endomannanases during prolonged incubations were also assessed. The highest initial rates on the pure mannans were attained by GH26 endomannanases. Acetylation tended to decrease the enzymatic rates to different extents depending on the enzyme. Despite exhibiting low rates on the pure mannan substrates, TresMan5A with CBM1 catalysed highest release among the endomannanases of both mannose and glucose during softwood saccharification. The presence of the CBM1 as well as the catalytic capability of the TresMan5A core module itself seemed to allow fast and more profound degradation of portions of the mannan that led to better cellulose degradation. In contrast, the presence of the CBM35 did not change the performance of PansMan26 in softwood saccharification. This study identified TresMan5A as the best endomannanase for increasing cellulase catalysed glucose release from softwood. Except for the superior performance of TresMan5A, the fungal GH5 and GH26 endomannanases generally performed on par on the lignocellulosic matrix. The work also illustrated the importance of using genuine lignocellulosic substrates rather than simple model substrates when selecting enzymes for industrial biomass applications.

Tài liệu tham khảo

Khatri V, Meddeb-Mouelhi F, Beauregard M. New insights into the enzymatic hydrolysis of lignocellulosic polymers by using fluorescent tagged carbohydrate-binding modules. Sustain Energy Fuels. 2018;2:479–91. Berlin A, Gilkes N, Kilburn D, Bura R, Markov A, Skomarovsky A, et al. Evaluation of novel fungal cellulase preparations for ability to hydrolyze softwood substrates—evidence for the role of accessory enzymes. Enzyme Microb Technol. 2005;37:175–84. Várnai A, Huikko L, Pere J, Siika-Aho M, Viikari L. Synergistic action of xylanase and mannanase improves the total hydrolysis of softwood. Bioresour Technol. 2011;102:9096–104. Eriksson Ö, Goring DAI, Lindgren BO. Structural studies on the chemical bonds between lignins and carbohydrates in spruce wood. Wood Sci Technol. 1980;14:267–79. Barros J, Serk H, Granlund I, Pesquet I. The cell biology of lignification in higher plants. Ann Bot. 2015;115:1053–74. Timell TE. Recent progress in the chemistry of wood hemicelluloses. Wood Sci Technol. 1967;1:45–70. Moreira LRS, Filho EXF. An overview of mannan structure and mannan-degrading enzyme systems. Appl Microbiol Biotechnol. 2008;79:165–78. Xu C, Leppänen AS, Eklund P, Holmlund P, Sjöholm R, Sundberg K, et al. Acetylation and characterization of spruce (Picea abies) galactoglucomannans. Carbohydr Res. 2010;345:810–6. Lundqvist J, Teleman A, Junel L, Zacchi G, Dahlman O, Tjerneld F, et al. Isolation and characterization of galactoglucomannan from spruce (Picea abies). Carbohydr Polym. 2002;48:29–39. Willför S, Sjöholm R, Laine C, Roslund M, Hemming J, Holmbom B. Characterisation of water—soluble galactoglucomannans from Norway spruce wood and thermomechanical pulp. Carbohydr Polym. 2003;52:175–87. Bååth JA, Abad AM, Berglund J, Larsbrink J, Vilaplana F, Olsson L. Mannanase hydrolysis of spruce galactoglucomannan focusing on the influence of acetylation on enzymatic mannan degradation. Biotechnol Biofuels. 2018;11:114. Katsuraya K, Okuyama K, Hatanaka K, Oshima R, Sato T, Matsuzaki K. Constitution of konjac glucomannan: chemical analysis and 13C NMR spectroscopy. Carbohydr Polym. 2003;53:183–9. Srivastava PK, Kapoor M. Production, properties, and applications of endo-β-mannanases. Biotechnol Adv. 2017;35:1–19. Gilbert HJ, Stålbrand H, Brumer H. How the walls come crumbling down: recent structural biochemistry of plant polysaccharide degradation. Curr Opin Plant Biol. 2008;11:338–48. Malgas S, van Dyk JS, Pletschke BI. A review of the enzymatic hydrolysis of mannans and synergistic interactions between β-mannanase, β-mannosidase and α-galactosidase. World J Microbiol Biotechnol. 2015;31:1167–75. Mikkelson A, Maaheimo H, Hakala TK. Hydrolysis of konjac glucomannan by Trichoderma reesei mannanase and endoglucanases Cel7B and Cel5A for the production of glucomannooligosaccharides. Carbohydr Res. 2013;372:60–8. Tenkanen M, Makkonen M, Perttula M, Viikari L, Teleman A. Action of Trichoderma reesei mannanase on galactoglucomannan in pine kraft pulp. J Biotechnol. 1997;57:191–204. Lombard V, Ramulu HG, Drula E, Coutinho PM, Henrissat B. The carbohydrate-active enzymes database (CAZy) in 2013. Nucleic Acids Res. 2014;42:D490–5. Sinnott ML. Catalytic mechanisms of enzymic glycosyl transfer. Chem Rev. 1990;90:1171–202. Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon J, Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc Natl Acad Sci USA. 1995;92:7090–4. Withers SG. Mechanisms of glycosyl transferases and hydrolases. Carbohydr Polym. 2001;44:325–37. Zhang X, Rogowski A, Zhao L, Hahn MG, Avci U, Knox JP, et al. Understanding how the complex molecular architecture of mannan-degrading hydrolases contributes to plant cell wall degradation. J Biol Chem. 2014;289:2002–12. Tailford LE, Ducros VMA, Flint JE, Roberts SM, Morland C, Zechel DL, et al. Understanding how diverse β-mannanases recognize heterogeneous substrates. Biochemistry. 2009;48:7009–18. Couturier M, Roussel A, Rosengren A, Leone P, Stålbrand H, Berrin J. Structural and biochemical analyses of glycoside hydrolase families 5 and 26 β-(1,4)-mannanases from Podospora anserina reveal differences upon manno-oligosaccharide catalysis. J Biol Chem. 2013;288:14624–35. Marchetti R, Berrin J, Couturier M, Qader SAU, Molinaro A, Silipo A. NMR analysis of the binding mode of two fungal endo-β-1,4-mannanases from GH5 and GH26 families. Org Biomol Chem. 2016;14:314–22. von Freiesleben P, Spodsberg N, Blicher TH, Anderson L, Jørgensen H, Stålbrand H, et al. An Aspergillus nidulans GH26 endo-β-mannanase with a novel degradation pattern on highly substituted galactomannans. Enzyme Microb Technol. 2016;83:68–77. Hägglund P, Eriksson T, Collén A, Nerinckx W, Claeyssens M, Stålbrand H. A cellulose-binding module of the Trichoderma reesei β-mannanase Man5A increases the mannan-hydrolysis of complex substrates. J Biotechnol. 2003;101:37–48. Pham TA, Berrin JG, Record E, To KA, Sigoillot JC. Hydrolysis of softwood by Aspergillus mannanase: role of a carbohydrate-binding module. J Biotechnol. 2010;148:163–70. Katsimpouras C, Dimarogona M, Petropoulos P. A thermostable GH26 endo-β-mannanase from Myceliophthora thermophila capable of enhancing lignocellulose degradation. Appl Microbiol Biotechnol. 2016;100:8385–97. Montanier C, van Bueren AL, Dumon C, Flint JE, Correia MA, Prates JA, et al. Evidence that family 35 carbohydrate binding modules display conserved specificity but divergent function. Proc Natl Acad Sci USA. 2009;106:3065–70. Correia MAS, Abbott DW, Gloster TM, Fernandes VO, Prates JAM, Montanier C, et al. Signature active site architectures illuminate the molecular basis for ligand specificity in family 35 carbohydrate binding module. Biochemistry. 2010;49:6193–205. Rättö M, Siika-aho M, Buchert J, Valkeajävi A, Viikari L. Enzymatic hydrolysis of isolated and fibre-bound galactoglucomannans from pine-wood and pine kraft pulp. Appl Microbiol Biotechnol. 1993;40:449–54. Inoue H, Yano S, Sawayama S. Effect of β-mannanase and β-mannosidase supple-mentation on the total hydrolysis of softwood polysaccharides by the Talaromyces cellulolyticus cellulase system. Appl Biochem Biotechnol. 2015;176:1673–86. Couturier M, Haon M, Coutinho PM, Henrissat B, Lesage-Meessen L, Berrin J. Podospora anserina hemicellulases potentiate the Trichoderma reesei secretome for saccharification of lignocellulosic biomass. Appl Environ Microbiol. 2011;77:237–46. Chandra RP, Chu QL, Hu J, Zhong N, Lin M, Lee JS, et al. The influence of lignin on steam pretreatment and mechanical pulping of poplar to achieve high sugar recovery and ease of enzymatic hydrolysis. Bioresour Technol. 2016;199:135–41. Jørgensen H, Sanadi AR, Felby C, Lange NEK, Fischer M, Ernst S. Production of ethanol and feed by high dry matter hydrolysis and fermentation of palm kernel press cake. Appl Biochem Biotechnol. 2010;161:318–32. Dilokpimol A, Nakai H, Gotfredsen CH, Baumann MJ, Nakai N, Hachem MA, et al. Recombinant production and characterisation of two related GH5 endo-β-1,4-mannanases from Aspergillus nidulans FGSC A4 showing distinctly different transglycosylation capacity. Biochim Biophys Acta. 2011;1814:1720–9. Eriksson T, Börjesson J, Tjerneld F. Mechanism of surfactant effect in enzymatic hydrolysis of lignocellulose. Enzyme Microb Technol. 2002;31:353–64. Sørensen TH, Cruys-Bagger N, Windahl MS, Badino SF, Borch K, Westh P. Temperature effects on kinetic parameters and substrate affinity of Cel7A cellobiohydrolases. J Biol Chem. 2015;290:22193–202. Westh P, Borch K, Sørensen T, Tokin R, Kari J, Badino S, et al. Thermoactivation of a cellobiohydrolase. Biotechnol Bioeng. 2018;115:831–8. Bombeck PL, Khatri V, Meddeb-Mouelhi F, Montplaisir D, Richel A, Beauregard M. Predicting the most appropriate wood biomass for selected industrial applications: comparison of wood, pulping, and enzymatic treatments using fluorescent-tagged carbohydrate-binding modules. Biotechnol Biofuels. 2017;10:293. Åkerholm M, Salmén L. Interactions between wood polymers studied by dynamic FT-IR spectroscopy. Polymer (Guildf). 2001;42:963–9. Andersson A, Persson T, Zacchi G, Stålbrand H, Jönsson A-S. Comparison of diafiltration and size-exclusion chromatography to recover hemicelluloses from process water from thermomechanical pulping of spruce. Appl Biochem Biotechnol. 2007;137:971–83. Jacobs A, Lundqvist J, Stålbrand H, Tjerneld F, Dahlman O. Characterization of water-soluble hemicelluloses from spruce and aspen employing SEC/MALDI mass spectroscopy. Carbohydr Res. 2002;337:711–7. Lehmbeck J, Wahlbom F. Production of a monoclonal antibody in a heterokaryon fungus or in a fungal host cell. WO2005070962 A1; 2005. Lever M. A new reaction for colorimetric determination of carbohydrates. Anal Biochem. 1972;47:273–9. Sluiter A, Hames B, Ruiz R, Scarlata C, Sluiter J, Templeton D, et al. Determination of structural carbohydrates and lignin in Biomass. Technical Report: NREL/TP-510-42618; 2008. Raman R, Venkataraman M, Ramakrishnan S, Lang W, Raguram S, Sasisekharan R. Advancing glycomics: implementation strategies at the consortium for functional glycomics. Glycobiology. 2006;16:82R–90R.