Abstract
Cellulolytic fungi usually have multiple genes for C1-oxidizing auxiliary activity 9 (AA9) lytic polysaccharide monooxygenases (LPMOs) in their genomes, but their potential functional differences are less understood. In this study, two C1-oxidizing AA9 LPMOs, SbLPMO9A and SbLPMO9B, were identified from Sordaria brevicollis, and their differences, particularly in terms of thermostability, reducing agent specificity, and synergy with cellulase, were explored. The two enzymes exhibited weak binding to cellulose and intolerance to hydrogen peroxide. Their oxidative activity was influenced by cellulose crystallinity and surface morphology, and both enzymes tended to oxidize celluloses of lower crystallinity and high surface area. Comparably, SbLPMO9A had much better thermostability than SbLPMO9B, which may be attributed to the presence of a carbohydrate binding module 1 (CBM1)-like sequence at its C-terminus. In addition, the two enzymes exhibited different specificities and responsivities toward electron donors. SbLPMO9A and SbLPMO9B were able to boost the catalytic efficiency of endoglucanase I (EGI) on physically and chemically pretreated substrates but with different degrees of synergy. Substrate- and enzyme-specific synergism was observed by comparing the synergistic action of SbLPMO9A or SbLPMO9B with commercial Celluclast 1.5L on three kinds of cellulosic substrates. On regenerated amorphous cellulose and PFI (Papirindustriens Forskningsinstitut)-fibrillated bleached eucalyptus pulp, SbLPMO9B showed a higher synergistic effect than SbLPMO9A, while on delignified wheat straw, the synergistic effect of SbLPMO9A was higher than that of SbLPMO9B. On account of its excellent thermostability and boosting effect on the enzymatic hydrolysis of delignified wheat straw, SbLPMO9A may have high application potential in biorefineries for lignocellulosic biomass.
Key points
• C1-oxidizing SbLPMO9A displayed higher thermostability than SbLPMO9B, probably due to the presence of a CBM1-like module.
• The oxidative activity of the two SbLPMO9s on celluloses increased with decreasing cellulose crystallinity or increasing beating degree.
• The two SbLPMO9s boosted the catalytic efficiency of cellulase, but the synergistic effect was substrate- and enzyme-specific.
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All data generated or analyzed during this study are included in this published article and the supplementary information file.
References
Agger JW, Isaksen T, Varnai A, Vidal-Melgosa S, Willats WGT, Ludwig R, Horn SJ, Eijsink VGH, Westereng B (2014) Discovery of LPMO activity on hemicelluloses shows the importance of oxidative processes in plant cell wall degradation. Proc Natl Acad Sci USA 111(17):6287–6292. https://doi.org/10.1073/pnas.1323629111
Bennati-Granier C, Garajova S, Champion C, Grisel S, Haon M, Zhou S, Fanuel M, Ropartz D, Rogniaux H, Gimbert I, Record E, Berrin JG (2015) Substrate specificity and regioselectivity of fungal AA9 lytic polysaccharide monooxygenases secreted by Podospora anserina. Biotechnol Biofuels 8:1–14. https://doi.org/10.1186/s13068-015-0274-3
Bissaro B, Røhr ÅK, Müller G, Chylenski P, Skaugen M, Forsberg Z, Horn SJ, Vaaje-Kolstad G, Eijsink VGH (2017) Oxidative cleavage of polysaccharides by monocopper enzymes depends on H2O2. Nat Chem Biol 13:1123–1128. https://doi.org/10.1038/nchembio.2470
Bissaro B, Várnai A, Røhr ÅK, Eijsink VGH (2018) Oxidoreductases and reactive oxygen species in conversion of lignocellulosic biomass. Microbiol Mol Biol Rev 82(4):1–51. https://doi.org/10.1128/MMBR.00029-18
Breslmayr E, Hanžek M, Hanrahan A, Leitner C, Kittl R, Šantek B, Oostenbrink C, Ludwig R (2018) A fast and sensitive activity assay for lytic polysaccharide monooxygenase. Biotechnol Biofuels 11:1–13. https://doi.org/10.1186/s13068-018-1063-6
Calderaro F, Keser M, Akeroyd M, Bevers LE, Eijsink VGH, Várnai A, van den Berg MA (2020) Characterization of an AA9 LPMO from Thielavia australiensis, TausLPMO9B, under industrially relevant lignocellulose saccharification conditions. Biotechnol Biofuels 13:1–17. https://doi.org/10.1186/s13068-020-01836-3
Cannella D, Möllers KB, Frigaard NU, Jensen PE, Bjerrum MJ, Johansen KS, Felby C (2016) Light-driven oxidation of polysaccharides by photosynthetic pigments and a metalloenzyme. Nat Commun 7:1–8. https://doi.org/10.1038/ncomms11134
Chalak A, Villares A, Moreau C, Haon M, Grisel S, D’Orlando A, Herpoël-Gimbert I, Labourel A, Cathala B, Berrin JG (2019) Influence of the carbohydrate-binding module on the activity of a fungal AA9 lytic polysaccharide monooxygenase on cellulosic substrates. Biotechnol Biofuels 12:1–10. https://doi.org/10.1186/s13068-019-1548-y
Chen K, Liu X, Long L, Ding S (2017) Cellobiose dehydrogenase from Volvariella volvacea and its effect on the saccharification of cellulose. Process Biochem 60:52–58. https://doi.org/10.1016/j.procbio.2017.05.023
Chen KX, Zhang X, Long LK, Ding SJ (2021) Comparison of C4-oxidizing and C1/C4-oxidizing AA9 LPMOs in substrate adsorption, H2O2-driven activity and synergy with cellulase on celluloses of different crystallinity. 269:118305. https://doi.org/10.1016/j.carbpol.2021.118305.
Chylenski P, Bissaro B, Sorlie M, Rohr AK, Varnai A, Horn SJ, Eijsink VGH (2019) Lytic polysaccharide monooxygenases in enzymatic processing of lignocellulosic biomass. ACS Catal 9(6):4970–4991. https://doi.org/10.1021/acscatal.9b00246
Edgar RC (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32:1792–1797. https://doi.org/10.1093/nar/gkh340
Eibinger M, Ganner T, Bubner P, Rošker S, Kracher D, Haltrich D, Ludwig R, Plank H, Nidetzky B (2014) Cellulose surface degradation by a lytic polysaccharide monooxygenase and its effect on cellulase hydrolytic efficiency. J Biol Chem 289:35929–35938. https://doi.org/10.1074/jbc.M114.602227
Ezeilo UR, Zakaria II, Huyop F, Wahab RA (2017) Enzymatic breakdown of lignocellulosic biomass: the role of glycosyl hydrolases and lytic polysaccharide monooxygenases. Biotechnol Biotechnol Equip 31:647–662. https://doi.org/10.1080/13102818.2017.1330124
Frommhagen M, Koetsier MJ, Westphal AH, Visser J, Hinz SWA, Vincken JP, Van Berkel WJH, Kabel MA, Gruppen H (2016) Lytic polysaccharide monooxygenases from Myceliophthora thermophila C1 differ in substrate preference and reducing agent specificity. Biotechnol Biofuels 9:1–17. https://doi.org/10.1186/s13068-016-0594-y
Frommhagen M, Sforza S, Westphal AH, Visser J, Hinz SWA, Koetsier MJ, Van Berkel WJH, Gruppen H, Kabel MA (2015) Discovery of the combined oxidative cleavage of plant xylan and cellulose by a new fungal polysaccharide monooxygenase. Biotechnol Biofuels 8:4–15. https://doi.org/10.1186/s13068-015-0284-1
Frommhagen M, Westphal AH, Hilgers R, Koetsier MJ, Hinz SWA, Visser J, Gruppen H, van Berkel WJH, Kabel MA (2018) Quantification of the catalytic performance of C1-cellulose-specific lytic polysaccharide monooxygenases. Appl Microbiol Biotechnol 102:1281–1295. https://doi.org/10.1007/s00253-017-8541-9
Gao W, Xiang Z, Chen K, Yang R, Yang F (2015) Effect of depth beating on the fiber properties and enzymatic saccharification efficiency of softwood kraft pulp. Carbohydr Polym 127:400–406. https://doi.org/10.1016/j.carbpol.2015.04.005
Garrido MM, Landoni M, Sabbadin F, Valacco MP, Couto A, Bruce NC, Wirth SA, Campos E (2020) PsAA9A, a C1-specific AA9 lytic polysaccharide monooxygenase from the white-rot basidiomycete Pycnoporus sanguineus. Appl Microbiol Biotechnol 104:9631–9643. https://doi.org/10.1007/s00253-020-10911-6
Guo X, Sang J, Chai C, An Y, Wei Z, Zhang H, Ma L, Dai Y, Lu F, Liu F (2020) A lytic polysaccharide monooxygenase from Myceliophthora thermophila C1 and its characterization in cleavage of glycosidic chain of cellulose. Biochem Eng J 162:107712. https://doi.org/10.1016/j.bej.2020.107712
Hangasky JA, Iavarone AT, Marletta MA (2018) Reactivity of O2 versus H2O2 with polysaccharide monooxygenases. Proc Natl Acad Sci USA 115:4915–4920. https://doi.org/10.1073/pnas.1801153115
Hegnar OA, Petrovic DM, Bissaro B, Alfredsen G, Várnai A, Eijsink VGH (2018) pH-Dependent relationship between catalytic activity and hydrogen peroxide production shown via characterization of a lytic polysaccharide monooxygenase from Gloeophyllum trabeum. Appl Environ Microbiol 85:1–15. https://doi.org/10.1128/AEM.02612-18
Hu J, Tian D, Renneckar S, Saddler JN (2018) Enzyme mediated nanofibrillation of cellulose by the synergistic actions of an endoglucanase, lytic polysaccharide monooxygenase (LPMO) and xylanase. Sci Rep 8:4–11. https://doi.org/10.1038/s41598-018-21016-6
Huang J, Xue Y, Han J, Liu J, Gan L, Long M (2020) Recombinant expression of lytic polysaccharide monooxygenase and its functional characterization. BioResources 15:7143–7158. https://doi.org/10.15376/BIORES.15.3.7143-7158.
Hüttner S, Várnai A, Petrović DM, Bach CX, Kim Anh DT, Thanh VN, Eijsink VGH, Larsbrink J, Olsson L (2019) Specific xylan activity revealed for AA9 lytic polysaccharide monooxygenases of the thermophilic fungus Malbranchea cinnamomea by functional characterization. Appl Environ Microbiol 85:1–13. https://doi.org/10.1128/AEM.01408-19
Isikgor FH, Becer CR (2015) Lignocellulosic biomass: a sustainable platform for the production of biobased chemicals and polymers. Polym Chem 6:4497–4559. https://doi.org/10.1039/c5py00263j
Jagadeeswaran G, Gainey L, Prade R, Mort AJ (2016) A family of AA9 lytic polysaccharide monooxygenases in Aspergillus nidulans is differentially regulated by multiple substrates and at least one is active on cellulose and xyloglucan. Appl Microbiol Biotechnol 100:4535–4547. https://doi.org/10.1007/s00253-016-7505-9
Jones SM, Transue WJ, Meier KK, Kelemen B, Solomon EI (2020) Kinetic analysis of amino acid radicals formed in H2O2-driven CuI+ LPMO reoxidation implicates dominant homolytic reactivity. Proc Natl Acad Sci USA 117(22):11916–11922. https://doi.org/10.1073/pnas.1922499117
Kadowaki MAS, Várnai A, Jameson JK, Leite AET, Costa-Filho AJ, Kumagai PS, Prade RA, Polikarpov I, Eijsink VGH (2018) Functional characterization of a lytic polysaccharide monooxygenase from the thermophilic fungus Myceliophthora thermophila. PLoS ONE 13:1–16. https://doi.org/10.1371/journal.pone.0202148
Karnaouri A, Muraleedharan MN, Dimarogona M, Topakas E, Rova U, Sandgren M, Christakopoulos P (2017) Recombinant expression of thermostable processive MtEG5 endoglucanase and its synergism with MtLPMO from Myceliophthora thermophila during the hydrolysis of lignocellulosic substrates. Biotechnol Biofuels 10:1–17. https://doi.org/10.1186/s13068-017-0813-1
Keller MB, Badino SF, Blossom BM, McBrayer B, Borch K, Westh P (2020) Promoting and impeding effects of lytic polysaccharide monooxygenases on glycoside hydrolase activity. ACS Sustain Chem Eng 8:14117–14126. https://doi.org/10.1021/acssuschemeng.0c04779
Kim IJ, Seo N, An HJ, Kim JH, Harris PV, Kim KH (2017) Type-dependent action modes of TtAA9E and TaAA9A acting on cellulose and differently pretreated lignocellulosic substrates. Biotechnol Biofuels 10:1–9. https://doi.org/10.1186/s13068-017-0721-4
Kittl R, Kracher D, Burgstaller D, Haltrich D, Ludwig R (2012) Production of four Neurospora crassa lytic polysaccharide monooxygenases in Pichia pastoris monitored by a fluorimetric assay. Biotechnol Biofuels 5:79. https://doi.org/10.1186/1754-6834-5-79
Klinke HB, Thomsen AB, Ahring BK (2004) Inhibition of ethanol-producing yeast and bacteria by degradation products produced during pre-treatment of biom. Appl Microbiol Biotechnol 66:10–26. https://doi.org/10.1007/s00253-004-1642-2
Koskela S, Wang S, Xu D, Yang X, Li K, Berglund LA, McKee LS, Bulone V, Zhou Q (2019) Lytic polysaccharide monooxygenase (LPMO) mediated production of ultra-fine cellulose nanofibres from delignified softwood fibres. Green Chem 21:5924–5933. https://doi.org/10.1039/c9gc02808k
Kracher D, Andlar M, Furtmüller PG, Ludwig R (2018) Active-site copper reduction promotes substrate binding of fungal lytic polysaccharide monooxygenase and reduces stability. J Biol Chem 293:1676–1687. https://doi.org/10.1074/jbc.RA117.000109
Kracher D, Scheiblbrandner S, Felice AKG, Breslmayr E, Preims M, Ludwicka K, Haltrich D, Eijsink VGH, Ludwig R (2016) Extracellular electron transfer systems fuel cellulose oxidative degradation. Science 352:1098–1101. https://doi.org/10.1126/science.aaf3165
Kruys A, Huhndorf SM, Miller AN (2015a) Coprophilous contributions to the phylogeny of Lasiosphaeriaceae and allied taxa within Sordariales (Ascomycota, Fungi). Fungal Divers 70(1):101–113. https://doi.org/10.1007/s13225-014-0296-3
Kumar S, Stecher G, Tamura K (2016) MEGA7: molecular evolutionary genetics analysis version 7.0 for bigger datasets. Mol Biol Evol 33:1870–1874. https://doi.org/10.1093/molbev/msw054
Laurent CVFP, Sun PC, Scheiblbrandner S, Csarman F, Cannazza P, Frommhagen M, van Berkel WJH (2019) Influence of lytic polysaccharide monooxygenase active site segments on activity and affinity. Int J Mol Sci 20(24):6219. https://doi.org/10.3390/ijms20246219
Lenfant N, Hainaut M, Terrapon N, Drula E, Lombard V, Henrissat B (2017) A bioinformatics analysis of 3400 lytic polysaccharide oxidases from family AA9. Carbohyd Res 448:166–174. https://doi.org/10.1016/j.carres.2017.04.012
Li F, Sun X, Yu W, Shi C, Zhang X, Yu H, Ma F (2021) Enhanced konjac glucomannan hydrolysis by lytic polysaccharide monooxygenases and generating prebiotic oligosaccharides. Carbohydr Polym 253:117241. https://doi.org/10.1016/j.carbpol.2020.117241
Liu B, Kognole AA, Wu M, Westereng B, Crowley MF, Kim S, Dimarogona M, Payne CM, Sandgren M (2018) Structural and molecular dynamics studies of a C1-oxidizing lytic polysaccharide monooxygenase from Heterobasidion irregulare reveal amino acids important for substrate recognition. FEBS J 285:2225–2242. https://doi.org/10.1111/febs.14472
Lo Leggio L, Welner D, De Maria L (2012) A structural overview of GH61 proteins - fungal cellulose degrading polysaccharide monooxygenases. Comput Struct Biotechnol 2:e201209019. https://doi.org/10.5936/csbj.201209019
Lo Leggio L, Weihe CD, Poulsen JCN, Sweeney M, Rasmussen F, Lin J, De Maria L, Wogulis M (2018) Structure of a lytic polysaccharide monooxygenase from Aspergillus fumigatus and an engineered thermostable variant. Carbohydr Res 469:55–59. https://doi.org/10.1016/j.carres.2018.08.009
Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31:426–428. https://doi.org/10.1021/ac60147a030
Monclaro AV, Petrović DM, Alves GSC, Costa MMC, Midorikawa GEO, Miller RNG, Filho EXF, Eijsink VGH, Várnai A (2020) Characterization of two family AA9 LPMOs from Aspergillus tamarii with distinct activities on xyloglucan reveals structural differences linked to cleavage specificity. PLoS ONE 15:1–19. https://doi.org/10.1371/journal.pone.0235642
Moreau C, Tapin-Lingua S, Grisel S, Gimbert I, Le Gall S, Meyer V, Petit-Conil M, Berrin JG, Cathala B, Villares A (2019) Lytic polysaccharide monooxygenases (LPMOs) facilitate cellulose nanofibrils production. Biotechnol Biofuels 12:13–17. https://doi.org/10.1186/s13068-019-1501-0
Müller G, Chylenski P, Bissaro B, Eijsink VGH, Horn SJ (2018) The impact of hydrogen peroxide supply on LPMO activity and overall saccharification efficiency of a commercial cellulase cocktail. Biotechnol Biofuels 11:209. https ://doi.org/https://doi.org/10.1186/s1306 8–018–1199–4.
Nakagawa YS, Eijsink VGH, Totani K, Vaaje-Kolstad G (2013) Conversion of α-chitin substrates with varying particle size and crystallinity reveals substrate preferences of the chitinases and lytic polysaccharide monooxygenase of Serratia marcescens. J Agric Food Chem 61:11061–11066. https://doi.org/10.1021/jf402743e
Nekiunaite L, Petrović DM, Westereng B, Vaaje-Kolstad G, Hachem MA, Várnai A, Eijsink VGH (2016) FgLPMO9A from Fusarium graminearum cleaves xyloglucan independently of the backbone substitution pattern. FEBS Lett 590:3346–3356. https://doi.org/10.1002/1873-3468.12385
Petrović DM, Várnai A, Dimarogona M, Mathiesen G, Sandgren M, Westereng B, Eijsink VGH (2019) Comparison of three seemingly similar lytic polysaccharide monooxygenases from Neurospora crassa suggests different roles in plant biomass degradation. J Biol Chem 294:15068–15081. https://doi.org/10.1074/jbc.RA119.008196
Phillips CM, Beeson WT, Cate JH, Marletta MA (2011) Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa. ACS Chem Biol 6:1399–1406. https://doi.org/10.1021/cb200351
Segal L, Creely JJ, Martin AE, Conrad CM (1959) An empirical method for estimating the degree of crystallinity of native cellulose using the x-ray diffractometer. Text Res J 29:786–794. https://doi.org/10.1177/004051755902901003
Semenova MV, Gusakov AV, Telitsin VD, Rozhkova AM, Kondratyeva EG, Sinitsyn AP (2020) Purification and characterization of two forms of the homologously expressed lytic polysaccharide monooxygenase (PvLPMO9A) from Penicillium verruculosum. BBA-Proteins Proteom 186(1):140297. https://doi.org/10.1016/j.bbapap.2019.140297
Shi Y, Chen K, Long L, Ding S (2021) A highly xyloglucan active lytic polysaccharide monooxygenase EpLPMO9A from Eupenicillium parvum 4–14 shows boosting effect on hydrolysis of complex lignocellulosic substrates. Int J Biol Macromol 167:202–213. https://doi.org/10.1016/j.ijbiomac.2020.11.177
Simmons TJ, Frandsen KEH, Ciano L, Tryfona T, Lenfant N, Poulsen JC, Wilson LFL, Tandrup T, Tovborg M, Schnorr K, Johansen KS, Henrissat B, Walton PH, Lo Leggio L, Dupree P (2017) Structural and electronic determinants of lytic polysaccharide monooxygenase reactivity on polysaccharide substrates. Nat Commun 8:1064. https://doi.org/10.1038/s41467-017-01247-3
Sun P, Laurent CVFP, Scheiblbrandner S, Frommhagen M, Kouzounis D, Sanders MG, van Berkel WJH, Ludwig R, Kabel MA (2020) Configuration of active site segments in lytic polysaccharide monooxygenases steers oxidative xyloglucan degradation. Biotechnol Biofuels 13:1–19. https://doi.org/10.1186/s13068-020-01731-x
Tokin R, Ipsen JØ, Westh P, Johansen KS (2020) The synergy between LPMOs and cellulases in enzymatic saccharification of cellulose is both enzyme- and substrate-dependent. Biotechnol Lett 42:1975–1984. https://doi.org/10.1007/s10529-020-02922-0
Vaaje-Kolstad G, Westereng B, Horn SJ, Liu Z, Zhai H, Sørlie M, Eijsink VGH (2010) An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides. Science 330:219–222. https://doi.org/10.1126/science.1192231
Vaaje-Kolstad G, Forsberg Z, Loose JSM, Bissaro B, Eijsink VGH (2017) Structural diversity of lytic polysaccharide monooxygenases. Curr Opin Struc Biol 44:67–76. https://doi.org/10.1016/j.sbi.2016.12.012
Valenzuela SV, Valls C, Schink V, Sánchez D, Roncero MB, Diaz P, Martínez J, Pastor FIJ (2019) Differential activity of lytic polysaccharide monooxygenases on celluloses of different crystallinity. Effectiveness in the sustainable production of cellulose nanofibrils. Carbohydr Polym 207:59–67. https://doi.org/10.1016/j.carbpol.2018.11.076
Vu VV, Beeson WT, Phillips CM, Cate JHD, Marletta MA (2014) Determinants of regioselective hydroxylation in the fungal polysaccharide monooxygenases. J Am Chem Soc 136:562–565. https://doi.org/10.1021/ja409384b
Westereng B, Ishida T, Vaaje-Kolstad G, Wu M, Eijsink VGH, Igarashi K, Samejima M, Ståhlberg J, Horn SJ, Sandgren M (2011) The putative endoglucanase PcGH61D from Phanerochaete chrysosporium is a metal-dependent oxidative enzyme that cleaves cellulose. PLoS ONE 6:e27807. https://doi.org/10.1371/journal.pone.0027807
Westereng B, Agger JW, Horn SJ, Vaaje-Kolstad G, Aachmann FL, Stenstrom YH, Eijsink VGH (2013) Efficient separation of oxidized cello-oligosaccharides generated by cellulose degrading lytic polysaccharide monooxygenases. J Chromatogr A 1271:144–152. https://doi.org/10.1016/j.chroma.2012.11.048
Xu H, Li B, Mu X, Yu G, Liu C, Zhang Y, Wang H (2014) Quantitative characterization of the impact of pulp refining on enzymatic saccharification of the alkaline pretreated corn stover. Bioresour Technol 169:19–26. https://doi.org/10.1016/j.biortech.2014.06.068
Yang J, Xu P, Long L, Ding S (2021) Production of lactobionic acid using an immobilized cellobiose dehydrogenase/laccase system on magnetic chitosan spheres. Process Biochem 100:1–9. https://doi.org/10.1016/j.procbio.2020.09.024
Zhang YHP, Cui J, Lynd LR, Kuang LR (2006) A transition from cellulose swelling to cellulose dissolution by o-phosphoric acid: evidence from enzymatic hydrolysis and supramolecular structure. Biomacromol 7:644–648. https://doi.org/10.1021/bm050799c
Zhang R, Liu Y, Zhang Y, Feng D, Hou S, Guo W, Niu K, Jiang Y, Han L, Sindhu L, Fang X (2019) Identification of a thermostable fungal lytic polysaccharide monooxygenase and evaluation of its effect on lignocellulosic degradation. Appl Microbiol Biotechnol 103:5739–5750. https://doi.org/10.1007/s00253-019-09928-3
Zheng F, Ding S (2013) Processivity and enzymatic mode of a glycoside hydrolase family 5 endoglucanase from Volvariella volvacea. Appl Environ Microbiol 79:989–996. https://doi.org/10.1128/AEM.02725-12
Zhou H, Li T, Yu Z, Ju J, Zhang H, Tan H, Li K, Yin H (2019) A lytic polysaccharide monooxygenase from Myceliophthora thermophila and its synergism with cellobiohydrolases in cellulose hydrolysis. Int J Biol Macromol 139:570–576. https://doi.org/10.1016/j.ijbiomac.2019.08.004
Kruys Å, Huhndorf SM, Miller AN (2015b) Coprophilous contributions to the phylogeny of Lasiosphaeriaceae and allied taxa within Sordariales (Ascomycota, Fungi). Fungal Diversity 70(1):101–113
Acknowledgements
The authors thank Prof. Shen Kuizhong and Han Shanming from the Institute of Chemical Industry of Forest Products, Chinese Academy of Forestry for their assistance in the preparation of PFI-fibrillated eucalyptus pulp.
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This work was supported by a research grant (No. 31270628) from the National Natural Science Foundation of China and a project funded by the Priority Academic Program Development of Jiangsu Higher Education Institutions and the Doctorate Fellowship Foundation of Nanjing Forestry University.
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ZX and CKX performed the experiments and data analysis and drafted the manuscript. LLK helped to design some experiments. DSJ designed the work, analyzed the data, and revised the manuscript. All authors read and approved the final manuscript.
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Zhang, X., Chen, K., Long, L. et al. Two C1-oxidizing AA9 lytic polysaccharide monooxygenases from Sordaria brevicollis differ in thermostability, activity, and synergy with cellulase. Appl Microbiol Biotechnol 105, 8739–8759 (2021). https://doi.org/10.1007/s00253-021-11677-1
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DOI: https://doi.org/10.1007/s00253-021-11677-1