Abstract
Cellulolytic enzymes are found in various microorganisms, however, ascomycete fungi are the most effective in cellulose hydrolysis. In world practice, the enzymes of the fungus Trichoderma, which is the ancestor of all cellulolytic enzymes producers, are still used as a source of industrial cellulases. At the moment there are other promising cellulase-producing fungi. These include fungal strains belonging to the genera Aspergillus, Myceliophtora (Chrysosporium), Chaetomium etc. The most promising strain among other microorganisms is the ascomycete cellulolytic Penicillium verruculosum, which contains cellulases with higher molecular activity and better operational characteristics. Using fungus P. verruculosum as a host, an expression system has been created that allows one to obtain improved enzyme complexes containing a «finely tuned» set of enzymes capable of effectively destroying plant polysaccharides under specified technological conditions.
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References
Adney WS, Jeoh T, Beckham GT et al (2009) Probing the role of N-linked glycans in the stability and activity of fungal cellobiohydrolases by mutational analysis. Cellulose 16:699–709
Bajaj P, Mahajan R (2019) Cellulase and xylanase synergism in industrial biotechnology. Appl Microbiol Biot 103:8711–8724. https://doi.org/10.1007/s00253-019-10146-0
Baker JO, Ehrman CI, Adney WS et al (1998) Hydrolysis of cellulose using ternary mixtures of purified cellulases. Appl Biochem Biotechnol 70-72:395–403
Bashirova A, Pramanik S, Volkov P et al (2019) Disulfide bond engineering of an endoglucanase from Penicillium verruculosum to improve its Thermostability. Int J Mol Sci 20:1602. https://doi.org/10.3390/ijms20071602
Berlin A, Balakshin M, Gilkes N et al (2006a) Inhibition of cellulase, xylanase and beta-glucosidase activities by softwood lignin preparations. J Biotechnol 125:198–209. https://doi.org/10.1016/j.jbiotec.2006.02.021
Berlin A, Gilkes N, Kilburn D et al (2005) Evaluation of novel fungal cellulase preparations for ability to hydrolyze softwood substrates - evidence for the role of accessory enzymes. Enzyme Microb Technol 37:175–184
Berlin A, Gilkes N, Kilburn D et al (2006b) Evaluation of cellulase preparations for hydrolysis of hardwood substrates. Appl Biochem Biotech 130:528–545
Bulakhov AG, Gusakov AV, Chekushina AV et al (2016) Isolation of homogeneous polysaccharide monooxygenases from fungal sources and investigation of their synergism with cellulases when acting on cellulose. Biochemistry-Moscow 81:530–537
Bulakhov AG, Volkov PV, Rozhkova AM et al (2017) Using an inducible promoter of a gene encoding Penicillium verruculosum Glucoamylase for production of enzyme preparations with enhanced Cellulase performance. PLoS One 12:e0170404. https://doi.org/10.1371/journal.pone.0170404
Chekushina AV, Dotsenko GS, Sinitsyn AP (2013) Comparing the efficiency of plant material bioconversion processes using biocatalysts based on Trichoderma and Penicillium verruculosum enzyme preparations. Catal Ind 5:98–104. https://doi.org/10.1134/S2070050413010042
Contreras F, Pramanik S, Rozhkova AM et al (2020) Engineering Robust Cellulases for Tailored Lignocellulosic Degradation Cocktails. Int J Mol Sci:21. https://doi.org/10.3390/ijms21051589
Denisenko YA, Gusakov AV, Rozhkova AM et al (2017) Site-directed mutagenesis of GH10 xylanase a from Penicillium canescens for determining factors affecting the enzyme thermostability. Int J Biol Macromol 104:665–671. https://doi.org/10.1016/j.ijbiomac.2017.06.079
Denisenko YA, Gusakov AV, Rozhkova AM et al (2019) Protein engineering of GH10 family xylanases for gaining a resistance to cereal proteinaceous inhibitors. Biocatal Agric Biote 17:690–695. https://doi.org/10.1016/j.bcab.2019.01.042
Denisenko YA, Korotkova OG, Zorov IN et al (2021) Heterologous Expression of Thermogutta terrifontis Endo-Xanthanase in Penicillium verruculosum, Isolation and Primary Characterization of the Enzyme. Biochemistry-Moscow 86:489–495. https://doi.org/10.1134/S000629792104009x
Dotsenko AS, Dotsenko GS, Rozhkova AM et al (2020a) Rational design and structure insights for thermostability improvement of Penicillium verruculosum Cel7A cellobiohydrolase. Biochimie 176:103–109. https://doi.org/10.1016/j.biochi.2020.06.007
Dotsenko AS, Gusakov AV, Rozhkova AM et al (2016a) Effect of N-linked glycosylation on the activity and other properties of recombinant endoglucanase IIa (Cel5A) from Penicillium verruculosum. Protein Eng Des Sel 29:495–501. https://doi.org/10.1093/protein/gzw030
Dotsenko AS, Gusakov AV, Volkov PV et al (2016b) N-linked glycosylation of recombinant cellobiohydrolase I (Cel7A) from Penicillium verruculosum and its effect on the enzyme activity. Biotechnol Bioeng 113:283–291. https://doi.org/10.1002/bit.25812
Dotsenko AS, Pramanik S, Gusakov AV et al (2019) Critical effect of proline on thermostability of endoglucanase II from Penicillium verruculosum. Biochem Eng J 152:107397. https://doi.org/10.1016/j.bej.2019.107395
Dotsenko AS, Rozhkova AM, Zorov IN et al (2020b) Protein surface engineering of endoglucanase Penicillium verruculosum for improvement in thermostability and stability in the presence of 1-butyl-3-methylimidazolium chloride ionic liquid. Bioresour Technol 296:122370. https://doi.org/10.1016/j.biortech.2019.122370
Dotsenko GS, Gusakov AV, Rozhkova AM et al (2015) Heterologous beta-glucosidase in a fungal cellulase system: comparison of different methods for development of multienzyme cocktails. Process Biochem 50:1258–1263. https://doi.org/10.1016/j.procbio.2015.05.008
Fulop L, Ecker J (2020) An overview of biomass conversion: exploring new opportunities. Peerj 8:e9586. https://doi.org/10.7717/peerj.9586
Gao L, Wang F, Gao F et al (2011) Purification and characterization of a novel cellobiohydrolase (PdCel6A) from Penicillium decumbens JU-A10 for bioethanol production. Bioresour Technol 102:8339–8342. https://doi.org/10.1016/j.biortech.2011.06.033
Guo HL, Chang YJ, Lee DJ (2018) Enzymatic saccharification of lignocellulosic biorefinery: research focuses. Bioresour Technol 252:198–215. https://doi.org/10.1016/j.biortech.2017.12.062
Gupta VK, Schmoll M, Herreraestrella A et al (2014) Biotechnology and biology of Trichoderma. Biotechnology and Biology of Trichoderma:1–549
Gusakov AV (2011) Alternatives to Trichoderma reesei in biofuel production. Trends Biotechnol 29:419–425. https://doi.org/10.1016/j.tibtech.2011.04.004
Gusakov AV (2014) Comment on “revealing Nature's Cellulase diversity: the digestion mechanism of Caldicellulosiruptor bescii CelA”. Science 344:578-a. https://doi.org/10.1126/science.1251248
Gusakov AV, Dotsenko AS, Rozhkova AM et al (2017) N-linked glycans are an important component of the processive machinery of cellobiohydrolases. Biochimie 132:102–108. https://doi.org/10.1016/j.biochi.2016.11.004
Gusakov AV, Salanovich TN, Antonov AI et al (2007) Design of highly efficient cellulase mixtures for enzymatic hydrolysis of cellulose. Biotechnol Bioeng 97:1028–1038. https://doi.org/10.1002/bit.21329
Gusakov AV, Sinitsyn AP (2012) Cellulases from Penicillium species for producing fuels from biomass. Adv Biochem Eng Biot 3:463–477. https://doi.org/10.4155/bfs.12.41
Harris PV, Welner D, Mcfarland KC et al (2010) Stimulation of lignocellulosic biomass hydrolysis by proteins of glycoside hydrolase family 61: structure and function of a large, enigmatic family. Biochemistry 49:3305–3316
Hemsworth GR, Davies GJ, Walton PH (2013) Recent insights into copper-containing lytic polysaccharide mono-oxygenases. Curr Opin Struc Biol 23:660–668
Horn SJ, Vaaje-Kolstad G, Westereng B et al (2012) Novel enzymes for the degradation of cellulose. Biotechnol Biofuels 5:45. https://doi.org/10.1186/1754-6834-5-45
Ikeda Y, Hayashi H, Okuda N et al (2007) Efficient cellulase production by the filamentous fungus Acremonium cellulolyticus. Biotechnol Prog 23:333–338. https://doi.org/10.1021/bp060201s
Ko JK, Ximenes E, Kim Y et al (2015) Adsorption of enzyme onto lignins of liquid hot water pretreated hardwoods. Biotechnol Bioeng 112:447–456. https://doi.org/10.1002/bit.25359
Korotkova OG, Semenova MV, Morozova VV et al (2009) Isolation and properties of fungal beta-glucosidases. Biochemistry (Mosc) 74:569–577. https://doi.org/10.1134/s0006297909050137
Kruszewska JS (1999) Heterologous expression of genes in filamentous fungi. Acta Biochim Pol 46:181–195. https://doi.org/10.18388/abp.1999_4196
Kubicek CP, Mikus M, Schuster A et al (2009) Metabolic engineering strategies for the improvement of cellulase production by Hypocrea jecorina. Biotechnol Biofuels 2:19. https://doi.org/10.1186/1754-6834-2-19
Levasseur A, Drula E, Lombard V et al (2013) Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes. Biotechnol Biofuels 6:41. https://doi.org/10.1186/1754-6834-6-41
Liao HP, Fan XT, Mei XL et al (2015) Production and characterization of cellulolytic enzyme from Penicillium oxalicum GZ-2 and its application in lignocellulose saccharification. Biomass Bioenergy 74:122–134
Liberato MV, Silveira RL, Prates ET et al (2016) Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism (vol 6, 23473, 2016). Sci Rep-Uk 6
Liu T, Wang TH, Li X et al (2008) Improved heterologous gene expression in Trichoderma reesei by cellobiohydrolase I gene (cbh1) promoter optimization. Acta Bioch Bioph Sin 40:158–165. https://doi.org/10.1111/j.1745-7270.2008.00388.x
Lynd LR, Weimer PJ, Van Zyl WH et al (2002) Microbial cellulose utilization: fundamentals and biotechnology. Microbiol Mol Biol R 66:506-+
Mach RL, Zeilinger S (2003) Regulation of gene expression in industrial fungi: Trichoderma. Appl Microbiol Biot 60:515–522. https://doi.org/10.1007/s00253-002-1162-x
Maeda RN, Barcelos CA, Santa Anna LM et al (2013) Cellulase production by Penicillium funiculosum and its application in the hydrolysis of sugar cane bagasse for second generation ethanol production by fed batch operation. J Biotechnol 163:38–44. https://doi.org/10.1016/j.jbiotec.2012.10.014
Margeot A, Hahn-Hagerdal B, Edlund M et al (2009) New improvements for lignocellulosic ethanol. Curr Opin Biotechnol 20:372–380. https://doi.org/10.1016/j.copbio.2009.05.009
Martins LF, Kolling D, Camassola M et al (2008) Comparison of Penicillium echinulatum and Trichoderma reesei cellulases in relation to their activity against various cellulosic substrates. Bioresour Technol 99:1417–1424. https://doi.org/10.1016/j.biortech.2007.01.060
Merino ST, Cherry J (2007) Progress and challenges in enzyme development for biomass utilization. Adv Biochem Eng Biotechnol 108:95–120. https://doi.org/10.1007/10_2007_066
Morozova VV, Gusakov AV, Andrianov RM et al (2010) Cellulases of Penicillium verruculosum. Biotechnol J 5:871–880. https://doi.org/10.1002/biot.201000050
Payne CM, Knott BC, Mayes HB et al (2015) Fungal Cellulases. Chem Rev 115:1308–1448
Phillips CM, Beeson WT, Cate JH et al (2011) Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa. ACS Chem Biol 6:1399–1406
Pramanik S, Semenova MV, Rozhkova AM et al (2021) An engineered cellobiohydrolase I for sustainable degradation of lignocellulosic biomass. Biotechnol Bioeng 118:4014–4027. https://doi.org/10.1002/bit.27877
Quinlan RJ, Sweeney MD, Lo Leggio L et al (2011) Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components. Proc Natl Acad Sci U S A 108:15079–15084. https://doi.org/10.1073/pnas.1105776108
Rahikainen JL, Martin-Sampedro R, Heikkinen H et al (2013a) Inhibitory effect of lignin during cellulose bioconversion: the effect of lignin chemistry on non-productive enzyme adsorption. Bioresour Technol 133:270–278. https://doi.org/10.1016/j.biortech.2013.01.075
Rahikainen JL, Moilanen U, Nurmi-Rantala S et al (2013b) Effect of temperature on lignin-derived inhibition studied with three structurally different cellobiohydrolases. Bioresour Technol 146:118–125. https://doi.org/10.1016/j.biortech.2013.07.069
Rashmi R, Siddalingamurthy KR (2018) Microbial xyloglucanases: a comprehensive review. Biocatal Biotransformation 36:280–295. https://doi.org/10.1080/10242422.2017.1417394
Rubtsova EA, Bushina EV, Rozhkova AM et al (2015) Novel enzyme preparations with high pectinase and Hemicellulase activity based on Penicillium canescens strains. Appl Biochem Micro 51:591–599. https://doi.org/10.1134/S0003683815050142
Saunders G, Picknett TM, Tuite MF et al (1989) Heterologous gene-expression in filamentous fungi. Trends Biotechnol 7:283–287. https://doi.org/10.1016/0167-7799(89)90048-6
Semenova MV, Gusakov AV, Telitsin VD et al (2021) Enzymatic destruction of cellulose: characteristics of the kinetic interaction of lytic polysaccharide monooxygenases and individual Cellulases. Appl Biochem Micro 57:618–625. https://doi.org/10.1134/S0003683821050136
Semenova MV, Gusakov AV, Volkov PV et al (2019) Enhancement of the enzymatic cellulose saccharification by Penicillium verruculosum multienzyme cocktails containing homologously overexpressed lytic polysaccharide monooxygenase. Mol Biol Rep 46:2363–2370. https://doi.org/10.1007/s11033-019-04693-y
Sidar A, Albuquerque ED, Voshol GP et al (2020) Carbohydrate binding modules: diversity of domain architecture in amylases and Cellulases from filamentous microorganisms. Front Bioeng Biotech 8
Singh A, Patel AK, Adsul M et al (2017) Genetic modification: a tool for enhancing cellulase secretion. Biofuel Res J 4:600–610. https://doi.org/10.18331/Brj2017.4.2.5
Singh G, Verma AK, Kumar V (2016) Catalytic properties, functional attributes and industrial applications of beta-glucosidases. 3 Biotech 6:3. https://doi.org/10.1007/s13205-015-0328-z
Singhania RR, Saini JK, Saini R et al (2014) Bioethanol production from wheat straw via enzymatic route employing Penicillium janthinellum cellulases. Bioresour Technol 169:490–495. https://doi.org/10.1016/j.biortech.2014.07.011
Sinitsyn AP, Korotkova OG, Rubtsova EA et al (2020a) Construction of recombinant producers of enzyme preparations for feed production with an expression system based on Penicillium verruculosum fungus. Appl Biochem Micro 56:875–880
Sinitsyn AP, Korotkova OG, Sinitsyna OA et al (2016) Optimizing the composition of Cellulase enzyme complex from Penicillium verruculosum: enhancing hydrolytic capabilities via genetic engineering. Catal Ind 8:101–106. https://doi.org/10.1134/S2070050416010128
Sinitsyn AP, Rubtsova EA, Shashkov IA et al (2017) Preparation and properties of new biocatalysts for the degradation of nonstarch plant polysaccharides. Catal Ind 9:349–356. https://doi.org/10.1134/S2070050417040092
Sinitsyn AP, Sinitsyna OA (2021) Bioconversion of renewable plant biomass. Second-generation biofuels: raw materials, biomass pretreatment, enzymes, processes, and cost. Analysis. Biochemistry-Moscow 86:S166–S195. https://doi.org/10.1134/S0006297921140121
Sinitsyn AP, Sinitsyna OA, Zorov IN et al (2020b) Exploring the capabilities of the Penicillium verruculosum expression system for the development of producers of enzymes for the effective degradation of renewable plant biomass: a review. Appl Biochem Micro 56:638–646
Skomarovskii AA, Gusakov AV, Okunev ON et al (2005) Studies of hydrolytic activity of enzyme preparations of Penicillium and Trychoderma fungi. Prikl Biokhim Mikrobiol 41:210–212
Steffien D, Aubel I, Bertau M (2014) Enzymatic hydrolysis of pre-treated lignocellulose with Penicillium verruculosum cellulases. J Mol Catal B-Enzym 103:29–35
Su XY, Schmitz G, Zhang ML et al (2012) Heterologous gene expression in filamentous fungi. Adv Appl Microbiol 81(81):1–61. https://doi.org/10.1016/B978-0-12-394382-8.00001-0
Teugjas H, Valjamae P (2013) Selecting beta-glucosidases to support cellulases in cellulose saccharification. Biotechnol Biofuels 6
Vaaje-Kolstad G, Westereng B, Horn SJ et al (2010) An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides. Science 330:219–222. https://doi.org/10.1126/science.1192231
Vlasenko EY, Ryan AI, Shoemaker CF et al (1998) The use of capillary viscometry, reducing end-group analysis, and size exclusion chromatography combined with multi-angle laser light scattering to characterize endo-1,4-beta-D-glucanases on carboxymethylcellulose: a comparative evaluation of the three methods. Enzyme Microb Technol 23:350–359
Volkov PV, Gusakov AV, Rubtsova EA et al (2019) Properties of a recombinant GH49 family dextranase heterologously expressed in two recipient strains of Penicillium species. Biochimie 157:123–130. https://doi.org/10.1016/j.biochi.2018.11.010
Volkov PV, Rozhkova AM, Gusakov AV et al (2014) Homologous cloning, purification and characterization of highly active cellobiohydrolase I (Cel7A) from Penicillium canescens. Protein Expr Purif 103:1–7. https://doi.org/10.1016/j.pep.2014.08.011
Wu SS, Wu SF (2020) Processivity and the mechanisms of Processive endoglucanases. Appl Biochem Biotech 190:448–463
Ye Y, Li X, Cao Y et al (2017) A beta-xylosidase hyper-production Penicillium oxalicum mutant enhanced ethanol production from alkali-pretreated corn Stover. Bioresour Technol 245:734–742. https://doi.org/10.1016/j.biortech.2017.08.155
Zhao XH, Wang W, Tong B et al (2016) A newly isolated Penicillium oxalicum 16 Cellulase with high efficient synergism and high tolerance of monosaccharide. Appl Biochem Biotech 178:173–183. https://doi.org/10.1007/s12010-015-1866-x
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This research was funded by the Russian Foundation for Basic Research (RFBR No. 18-54-80027) and Ministry of Science and High Education.
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Rozhkova, A.M., Gusakov, A.V., Dotsenko, A.S., Sinitsyna, O.A., Sinitsyn, A.P. (2022). Capabilities of the Ascomycete Fungus Penicillium Verruculosum and its Enzymes for Conversion of Cellulosic Feedstock. In: Soccol, C.R., Amarante Guimarães Pereira, G., Dussap, CG., Porto de Souza Vandenberghe, L. (eds) Liquid Biofuels: Bioethanol. Biofuel and Biorefinery Technologies, vol 12. Springer, Cham. https://doi.org/10.1007/978-3-031-01241-9_11
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