Pectinolytic Enzymes of Basidiomycota: Genetic Basis, Culture Conditions, Biochemical Properties, and Industrial Applications
DOI:
https://doi.org/10.15407/microbiolj88.01.083Keywords:
Basidiomycota, pectinase, biotechnology, enzyme, cultivation, enzyme purification, clarificationAbstract
Pectinases are a diverse group of enzymes responsible for the depolymerization and modification of plant cell wall polysaccharides. While bacterial and ascomycete pectinases are well studied and widely applied, the enzymatic potential of Basidiomycota remains underexplored. This review analyzes over 70 species of Basidiomycota and summarizes the genetic diversity of pectinase-encoding genes (over 100 genes associated with pectolytic activity), belonging to the CAZy families GH (8–78 genes, e.g., GH28 for polygalacturonases), PL (up to 24 genes, e.g., PL1 and PL3 for pectin/pectate lyases), and CE (up to 19 genes, e.g., CE8 and CE12 for pectinesterases). Special attention is given to the role of cultivation conditions – substrate type and concentration, temperature, pH, nitrogen supplementation, and co-cultivation – in regulating enzyme biosynthesis and activity. Pectinolytic activity varies widely (0.05 µmol/min/mL to 1163.8 units/gsubstrate), with white-rot fungi achieving the upper range. The most promising producers are from the genera Pleurotus, Trametes, and Lentinula. The review also covers isolation methods, including ammonium sulfate precipitation, dialysis, ion-exchange, and gel-filtration chromatography (purification factors 2.4–10.5, recovery 21–65%), and biochemical properties of basidiomycete pectinases, which exhibit moderate thermostability (40–60 °C optima), acidic pH optima (3.5–6.5), glycoprotein structure, and multiple isoforms. These enzymes show promising properties for fruit juice extraction, clarification, tissue maceration, and bioconversion of agro-industrial wastes. Therefore, Basidiomycota represents a valuable but insufficiently characterized source of industrial pectinases, requiring further study of new strain selection, cultivation optimization, and large-scale enzyme applications.
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Ahmed, J., Thakur, A., & Goyal, A. (2021). Emerging trends on the role of recombinant pectinolytic enzymes in industries- an overview. Biocatalysis and Agricultural Biotechnology, 38, 102200. https://doi.org/10.1016/j.bcab.2021.102200
Alberto Marim, R., Vieira Avelino, K., Wietzikoski Halabura, M. I., Lopes Araújo, N., Teodoro Santana, T., Linde, G. A., Barros Colauto, N., & Silveira do Valle, J. (2020). Lentinus crinitus response to blue light on carbohydrate-active enzymes. Bioscience Journal, 36(3), 924-931. https://doi.org/10.14393/BJ-v36n3a2020-49986
Alcântara, S. R., Leite, N. J., & da Silva, F. L. H. (2013). Scale up of polygalacturonase production by solid state fermentation process. In Food Industry. InTech.
Alfaro, M., Majcherczyk, A., Kües, U., Ramírez, L., & Pisabarro, A. G. (2020). Glucose counteracts wood-dependent induction of lignocellulolytic enzyme secretion in monokaryon and dikaryon submerged cultures of the white-rot basidiomycete Pleurotus ostreatus. Scientific Reports, 10(1), 12421. https://doi.org/10.1038/s41598-020-68969-1
Amin, F., Bhatti, H. N., & Bilal, M. (2019). Recent advances in the production strategies of microbial pectinases - A review. International Journal of Biological Macromolecules, 122, 1017-1026. https://doi.org/10.1016/j.ijbiomac.2018.09.048
Amin, F., Bhatti, H. N., Bilal, M., & Asgher, M. (2017). Multiple parameter optimizations for enhanced biosynthesis of exo-polygalacturonase enzyme and its application in fruit juice clarification. International Journal of Food Engineering, 13(2). https://doi.org/10.1515/ijfe-2016-0256
Arshad, H., Khan, S., Kanwal, A., & Afzal, I. (2020). Industrial applications of pectinases. Lahore Garrison University Journal of Life Sciences, 1(2), 121-135. https://doi.org/10.54692/lgujls.2017.010288
Bekli, S., Aktas, B., Gencer, D., & Aslim, B. (2019). Biochemical and molecular characterizations of a novel ph- and temperature-stable pectate lyase from Bacillus amyloliquefaciens s6 for industrial application. Molecular Biotechnology, 61(9), 681-693. https://doi.org/10.1007/s12033-019-00194-2
Berger, R. G., & Ersoy, F. (2022). Improved foods using enzymes from basidiomycetes. Processes, 10(4), 726. https://doi.org/10.3390/pr10040726
Bonnin, E., & Pelloux, J. (2020). Pectin degrading enzymes. in pectin: technological and physiological properties. Cham: Springer International Publishing, pp. 37-60. https://doi.org/10.1007/978-3-030-53421-9_3
Bonomini, F. M., Wisbeck, E., & MirandaGern, R. M. (2017). Produção de enzimas por Pleurotus sajor-caju e Pleurotus djamor. NBC, 7(14), 109-126.
Carli, S., Meleiro, L. P., & Ward, R. J. (2019). Biochemical and kinetic characterization of the recombinant GH28 Stereum purpureum endopolygalacturonase and its biotechnological application. International Journal of Biological Macromolecules, 137, 469-474. https://doi.org/10.1016/j.ijbiomac.2019.06.165
Carolina, F. P., AntÃ'nio, Z. de M. C., Givaldo, R. N., José, L. B., Ana, P. T. U., & Elizama, A.-O. (2021). Brewers residues and cocoa pod shells as a substrate for cultivation of Pleurotus ostreatus CCIBt 2339 and enzymes production. African Journal of Biotechnology, 20(3), 115-121. https://doi.org/10.5897/AJB2020.17242
Chandel, V., Biswas, D., Roy, S., Vaidya, D., Verma, A., & Gupta, A. (2022). Current advancements in pectin: extraction, properties and multifunctional applications. Foods, 11(17), 2683. https://doi.org/10.3390/foods11172683
Chen, L., Gong, Y., Cai, Y., Liu, W., Zhou, Y., Xiao, Y., Xu, Z., Liu, Y., Lei, X., Wang, G., Guo, M., Ma, X., & Bian, Y. (2016). Genome sequence of the edible cultivated mushroom Lentinula edodes (shiitake) reveals insights into lignocellulose degradation. PLOS ONE, 11(8), e0160336. https://doi.org/10.1371/journal.pone.0160336
Clausen, C. A., & Green III., F. (1996). Characterization of polygalacturonase from the brown-rot fungus Postia placenta. Applied Microbiology and Biotechnology, 45(6), 750-754. https://doi.org/10.1007/s002530050758
Couturier, M., Navarro, D., Chevret, D., Henrissat, B., Piumi, F., Ruiz-Dueñas, F. J., Martinez, A. T., Grigoriev, I. V., Riley, R., Lipzen, A., Berrin, J.-G., Master, E. R., & Rosso, M.-N. (2015). Enhanced degradation of softwood versus hardwood by the white-rot fungus Pycnoporus coccineus. Biotechnology for Biofuels, 8(1), 216. https://doi.org/10.1186/s13068-015-0407-8
Danylyak, N. I., Semichaevsky, V. D., Dudchenko, L. G., & Trutneva, I. A. (1989). Enzyme systems of higher basidiomycetes (in russian: Fermentnyye sistemy vysshikh bazidiomitsetov). Kyiv, Naukova Dumka.
de Siqueira, F. G., de Siqueira, A. G., de Siqueira, E. G., Carvalho, M. A., Peretti, B. M. P., Jaramillo, P. M. D., Teixeira, R. S. S., Dias, E. S., Félix, C. R., & Filho, E. X. F. (2010). Evaluation of holocellulase production by plant-degrading fungi grown on agro-industrial residues. Biodegradation, 21(5), 815-824. https://doi.org/10.1007/s10532-010-9346-z
de Souza, H. Q., de Oliveira, L. A., & Andrade, J. S. (2008). Seleção de Basidiomycetes da Amazônia para produção de enzimas de interesse biotecnológico. Ciência e Tecnologia de Alimentos, 28, 116-124. https://doi.org/10.1590/S0101-20612008000500019
Dhillon, B., Hamelin, R. C., & Rollins, J. A. (2021). Transcriptional profile of oil palm pathogen, Ganoderma boninense, reveals activation of lignin degradation machinery and possible evasion of host immune response. BMC Genomics, 22(1), 326. https://doi.org/10.1186/s12864-021-07644-9
Díaz-Godínez, G., Téllez-Téllez, M., Rodríguez, A., Obregón-Barbosa, V., Acosta-Urdapilleta, M. D. L., & Villegas, E. (2016). Enzymatic, antioxidant, antimicrobial, and insecticidal activities of Pleurotus pulmonarius and Pycnoporus cinnabarinus grown separately in an airlift reactor. BioResources, 11(2). https://doi.org/10.15376/biores.11.2.4186-4200
do Rosário Freixo, M., Karmali, A., & Arteiro, J. M. (2008). Production of polygalacturonase from Coriolus versicolor grown on tomato pomace and its chromatographic behaviour on immobilized metal chelates. Journal of Industrial Microbiology & Biotechnology, 35(6), 475-484. https://doi.org/10.1007/s10295-008-0305-1
Dudchenko, L. H., & Trutneva, І. А. (1985). Pectolytic enzymes of Coriolus pubescens (Fr.) Quel. in culture (in ukrainian: Pektolitychni fermenty Coriolus pubescens (Fr.) Quel. u kulʹturi). Ukr Bot J, 42(2), 38-40.
Dudka, I. A., Wasser, S. P., Ellanskaia, I. A., Koval, E. Z., Gorbik, L. T., Nikolskaya, E. A., Bilay, V. I., Bilay, T. I., Borisova, V. N., Sivers, V. S., Musich, E. G., Lizak, Y. V., Stryzhevskaya, A. Y., Aizenberg, V. L., Kirillova, L. M., Bezbrodova, S. I., Zaichenko, A. M., Zakordonets, L. A., Meteiko, T. Y., … Redchits, T. I. (1982). Methods of experimental mycology (in russian: Metody eksperimental'noy mikologii) (V. I. Bilai (ed.)). Kyiv, Naukova Dumka.
Falkoski, D. L., Guimarães, V. M., de Almeida, M. N., Alfenas, A. C., Colodette, J. L., & de Rezende, S. T. (2012). Characterization of cellulolytic extract from Pycnoporus sanguineus PF-2 and its application in biomass saccharification. Applied Biochemistry and Biotechnology, 166(6), 1586-1603. https://doi.org/10.1007/s12010-012-9565-3
Farani de Souza, D., Kirst Tychanowicz, G., Giatti Marques de Souza, C., & Peralta, R. M. (2006). Co-production of ligninolytic enzymes by Pleurotus pulmonarius on wheat bran solid state cultures. Journal of Basic Microbiology, 46(2), 126-134. https://doi.org/10.1002/jobm.200510014
Freitas, E. N. de, Alnoch, R. C., Contato, A. G., Nogueira, K. M. V., Crevelin, E. J., Moraes, L. A. B. de, Silva, R. N., Martínez, C. A., & Polizeli, M. de L. T. M. (2021). enzymatic pretreatment with laccases from Lentinus sajor-caju induces structural modification in lignin and enhances the digestibility of tropical forage grass (Panicum maximum) grown under future climate conditions. International Journal of Molecular Sciences, 22(17), 9445. https://doi.org/10.3390/ijms22179445
Freixo, M. do R., Karmali, A., & Arteiro, J. M. (2008). Production and chromatographic behaviour of polygalacturonase from Pleurotus ostreatus on immobilized metal chelates. Process Biochemistry, 43(5), 531-539. https://doi.org/10.1016/j.procbio.2008.01.010
Ganbarov, K. G., Kulieva, N. A., & Muradov, P. Z. (2001). Biosynthesis of pectinase by fungi of the genera Bjerkandera and Coriolus during solid-phase fermentation. Applied Biochemistry and Microbiology, 37(6), 593-595. https://doi.org/10.1023/A:1012303101102
Garg, G., Singh, A., Kaur, A., Singh, R., Kaur, J., & Mahajan, R. (2016). Microbial pectinases: an ecofriendly tool of nature for industries. 3 Biotech, 6(1), 47. https://doi.org/10.1007/s13205-016-0371-4
Garg, N., Yadav, K.., Kumar, S., & Muthukumar, M. (2014). Enzymatic properties of oyster mushroom (Pleurotus florida) exudate. The Indian Journal of Agricultural Sciences, 84(8). https://doi.org/10.56093/ijas.v84i8.43143
Haile, S., & Ayele, A. (2022). Pectinase from microorganisms and its industrial applications. The Scientific World Journal, 2022, 1-15. https://doi.org/10.1155/2022/1881305
Hamada, S., Toda, K., Ogawa, S., Kubota, K., & Miyairi, K. (2015). Characterization of the effects of C-terminal pro-sequence on self-inactivation of Stereum purpureum endopolygalacturonase I. FEMS Microbiology Letters, 362(17), fnv134. https://doi.org/10.1093/femsle/fnv134
Hong, P. N., & Lee, C. (2017). Roles of pectin methylesterases and pectin methylesterase inhibitors in plant physiology. The Journal of Agricultural, Life and Environmental Sciences, 29(1), 1-17. https://doi.org/10.12972/jales.20170001
Hori, C., Ishida, T., Igarashi, K., Samejima, M., Suzuki, H., Master, E., Ferreira, P., Ruiz-Dueñas, F. J., Held, B., Canessa, P., Larrondo, L. F., Schmoll, M., Druzhinina, I. S., Kubicek, C. P., Gaskell, J. A., Kersten, P., St. John, F., Glasner, J., Sabat, G., … Cullen, D. (2014). Analysis of the Phlebiopsis gigantea genome, transcriptome and secretome provides insight into its pioneer colonization strategies of wood. PLoS Genetics, 10(12), e1004759. https://doi.org/10.1371/journal.pgen.1004759
Inácio, F. D., Ferreira, R. O., Araujo, C. A. V. de, Peralta, R. M., & Souza, C. G. M. de. (2015). Production of enzymes and biotransformation of orange waste by oyster mushroom, Pleurotus pulmonarius (Fr.) Qul. Advances in Microbiology, 05(01), 1-8. https://doi.org/10.4236/aim.2015.51001
Jatav, R. S., Gupta, A. K., & Doshi, A. (2014). Effect of different temperatures and growth stages of blue oyster mushroom on the activity of enzymes. Mushroom Research, 23(1), 47-51.
Jin-Kyeong, K., Seong-Wha, J., Eun-Ji, K., & Do-Youn, J. (2019). Development of an apple/pear pomace fermented with Lentinus edodes mycelia. Korean Society of Food Science and Technology, 51(3), 286-294.
Kaczmarska, A., Pieczywek, P. M., Cybulska, J., & Zdunek, A. (2022). Structure and functionality of Rhamnogalacturonan I in the cell wall and in solution: A review. Carbohydrate Polymers, 278, 118909. https://doi.org/10.1016/j.carbpol.2021.118909
Kawai, M. (1972). Maceration of plant tissues by basidiomycetes: (II) On some sorts of polysaccharide decomposing activites of crude enzyme preparations. Journal of Fermentation Technology, 50(10), 691-697.
Kobayashi, N., Wada, N., Yokoyama, H., Tanaka, Y., Suzuki, T., Habu, N., & Konno, N. (2023). Extracellular enzymes secreted in the mycelial block of Lentinula edodes during hyphal growth. AMB Express, 13(1), 36. https://doi.org/10.1186/s13568-023-01547-6
Kohli, P., & Gupta, R. (2015). Alkaline pectinases: A review. Biocatalysis and Agricultural Biotechnology, 4(3), 279-285. https://doi.org/10.1016/j.bcab.2015.07.001
Kurt, S., & Buyukalaca, S. (2010). Yield performances and changes in enzyme activities of Pleurotus spp. (P. ostreatus and P. sajor-caju) cultivated on different agricultural wastes. Bioresource Technology, 101(9), 3164-3169. https://doi.org/10.1016/j.biortech.2009.12.011
Kuuskeri, J., Häkkinen, M., Laine, P., Smolander, O.-P., Tamene, F., Miettinen, S., Nousiainen, P., Kemell, M., Auvinen, P., & Lundell, T. (2016). Time-scale dynamics of proteome and transcriptome of the white-rot fungus Phlebia radiata: growth on spruce wood and decay effect on lignocellulose. Biotechnology for Biofuels, 9(1), 192. https://doi.org/10.1186/s13068-016-0608-9
Levasseur, A., Lomascolo, A., Chabrol, O., Ruiz-Dueñas, F. J., Boukhris-Uzan, E., Piumi, F., Kües, U., Ram, A. F. J., Murat, C., Haon, M., Benoit, I., Arfi, Y., Chevret, D., Drula, E., Kwon, M., Gouret, P., Lesage-Meessen, L., Lombard, V., Mariette, J., … Record, E. (2014). The genome of the white-rot fungus Pycnoporus cinnabarinus: a basidiomycete model with a versatile arsenal for lignocellulosic biomass breakdown. BMC Genomics, 15(1), 486. https://doi.org/10.1186/1471-2164-15-486
Levin, L., & Forchiassin, F. (1998). Culture conditions for the production of pectinolytic enzymes by the white‐rot fungus Trametes trogii on a laboratory scale. Acta Biotechnologica, 18(2), 157-166. https://doi.org/10.1002/abio.370180213
Li, J., Wiebenga, A., Lipzen, A., Ng, V., Tejomurthula, S., Zhang, Y., Grigoriev, I. V., Peng, M., & de Vries, R. P. (2023). Comparative genomics and transcriptomics analyses reveal divergent plant biomass-degrading strategies in fungi. Journal of Fungi, 9(8), 860. https://doi.org/10.3390/jof9080860
Liu, M., Ale, M. T., Kołaczkowski, B., Fernando, D., Daniel, G., Meyer, A. S., & Thygesen, A. (2017). Comparison of traditional field retting and Phlebia radiata Cel 26 retting of hemp fibres for fibre-reinforced composites. AMB Express, 7(1), 58. https://doi.org/10.1186/s13568-017-0355-8
Liu, N., Sun, Y., Pei, Y., Zhang, X., Wang, P., Li, X., Li, F., & Hou, Y. (2018). A pectin methylesterase inhibitor enhances resistance to verticillium wilt. Plant Physiology, 176(3), 2202-2220. https://doi.org/10.1104/pp.17.01399
López-Sandin, I., Gutiérrez-Soto, G., Elizondo-Luevano, J. H., Parra Saldívar, R., Franco Flores, M., Castillo Martínez, D., & Garza-Hernández, D. M. (2024). Aprovechamiento de residuos agroindustriales para la obtención de enzimas termoestables degradadoras de pared celular vegetal utilizando un co-cultivo de basidiomicetos. Scientia Agricolis Vita, 1(2). https://doi.org/10.29105/agricolis.v1i2.18
Majumder, K., Paul, B., & Sundas, R. (2020). An analysis of exo-polygalacturonase bioprocess in submerged and solid-state fermentation by Pleurotus ostreatus using pomelo peel powder as carbon source. Journal of Genetic Engineering and Biotechnology, 18(1), 47. https://doi.org/10.1186/s43141-020-00061-7
Mäkinen, M., Kuuskeri, J., Laine, P., Smolander, O.-P., Kovalchuk, A., Zeng, Z., Asiegbu, F. O., Paulin, L., Auvinen, P., & Lundell, T. (2019). Genome description of Phlebia radiata 79 with comparative genomics analysis on lignocellulose decomposition machinery of phlebioid fungi. BMC Genomics, 20(1), 430. https://doi.org/10.1186/s12864-019-5817-8
Masutti, D. C., Borgognone, A., Scardovi, F., Vaccari, C., & Setti, L. (2015). Effects on the enzymes production from different mixes of agro-food wastes. Chemical Engineering Transactions, 43, 487-492.
Matsumoto, S., Yamada, H., Kunishige, Y., Takenaka, S., Nakazawa, M., Ueda, M., & Sakamoto, T. (2017). Identification of a novel Penicillium chrysogenum rhamnogalacturonan rhamnohydrolase and the first report of a rhamnogalacturonan rhamnohydrolase gene. Enzyme and Microbial Technology, 98, 76-85. https://doi.org/10.1016/j.enzmictec.2016.12.008
Mehmood, T., Saman, T., Asgher, M., Irfan, M., Anwar, Z., Nadeem, F., & Siddiqa, A. (2019a). Optimization of cultural parameters for pectin methylestrase and polygalacturonase production from Schizophyllum commune in solid state fermentation. Bangladesh Journal of Botany, 48(1), 65-74. https://doi.org/10.3329/bjb.v48i1.47417
Mehmood, T., Saman, T., Irfan, M., Anwar, F., Ikram, M. S., & Tabassam, Q. (2019b). Pectinase production from Schizophyllum commune through central composite design using citrus waste and its immobilization for industrial exploitation. Waste and Biomass Valorization, 10(9), 2527-2536. https://doi.org/10.1007/s12649-018-0279-9
Miyairi, K., Nishida, K., Takarae, M., Shikanai, Y., & Okuno, T. (2002). Purification and characterization of pectate lyase I and II from fungus Stereum purpureum. J Appl Glycosci, 49(2), 99-106. https://doi.org/10.5458/jag.49.99
Miyairi, K., Toyoda, M., & Okuno, T. (2001). Purification and characterization of endo- and exo-polygalacturonases from Fomitopsis cytisina. J App Glycosci, 48(2), 105-114. https://doi.org/10.5458/jag.48.105
Miyairi, K,, Okuno, T., & Sawai, K. (1985). Purification and properties of endopolygalacturonase I from Stereum purpureum, a factor inducing silver-leaf symptoms on apple trees. Agricultural and Biological Chemistry, 49(4), 1111-1118. https://doi.org/10.1271/bbb1961.49.1111
Miyauchi, S., Hage, H., Drula, E., Lesage-Meessen, L., Berrin, J.-G., Navarro, D., Favel, A., Chaduli, D., Grisel, S., Haon, M., Piumi, F., Levasseur, A., Lomascolo, A., Ahrendt, S., Barry, K., LaButti, K. M., Chevret, D., Daum, C., Mariette, J., … Rosso, M.-N. (2020). Conserved white-rot enzymatic mechanism for wood decay in the Basidiomycota genus Pycnoporus. DNA Research, 27(2). https://doi.org/10.1093/dnares/dsaa011
Mohammad Shamim, H., Ali Abdel-Rahman, M., Shakhawat Hussain, M., Islam, M. R., & Al-Mahin, A. (2017). Bioconversion of water-hyacinth to nutritionally enriched animal feed by solid state fermentation using Pleurotus sajor-caju. Journal of Microbiology, Biotechnology and Food Sciences, 6(5), 1165-1169. https://doi.org/10.15414/jmbfs.2017.6.5.1165-1169
Mwenje, E., & Ride, J. P. (1999). Purification and characterization of an endo-polygalacturonase (PG1) from a Zimbabwean species of Armillaria. Physiological and Molecular Plant Pathology, 55(2), 131-139. https://doi.org/10.1006/pmpp.1999.0210
Normand, J., Ralet, M.-C., Thibault, J.-F., Rogniaux, H., Delavault, P., & Bonnin, E. (2010). Purification, characterization, and mode of action of a rhamnogalacturonan hydrolase from Irpex lacteus, tolerant to an acetylated substrate. Applied Microbiology and Biotechnology, 86(2), 577-588. https://doi.org/10.1007/s00253-009-2310-3
Ozojiofor, U. O., & Rasheed, Z. A. (2023). Pectinases: structure, functions and biotechnological applications. Journal of Natural and Applied Sciences Pakistan, 5(2), 1448-1464.
Papadaki, A., Kachrimanidou, V., Papanikolaou, S., Philippoussis, A., & Diamantopoulou, P. (2019). Upgrading grape pomace through Pleurotus spp. cultivation for the production of enzymes and fruiting bodies. Microorganisms, 7(7), 207. https://doi.org/10.3390/microorganisms7070207
Papinutti, V. L., & Forchiassin, F. (2007). Lignocellulolytic enzymes from Fomes sclerodermeus growing in solid-state fermentation. Journal of Food Engineering, 81(1), 54-59. https://doi.org/10.1016/j.jfoodeng.2006.10.006
Park, Y.-J., Jeong, Y.-U., & Kong, W.-S. (2018). Genome Sequencing and carbohydrate-active enzyme (CAZyme) repertoire of the white rot fungus Flammulina elastica. International Journal of Molecular Sciences, 19(8), 2379. https://doi.org/10.3390/ijms19082379
Park, Y.-J., & Kong, W.-S. (2018). Genome-wide comparison of carbohydrate-active enzymes (CAZymes) repertoire of Flammulina ononidis. Mycobiology, 46(4), 349-360. https://doi.org/10.1080/12298093.2018.1537585
Patel, V. B., Chatterjee, S., & Dhoble, A. S. (2022). A review on pectinase properties, application in juice clarification, and membranes as immobilization support. Journal of Food Science, 87(8), 3338-3354. https://doi.org/10.1111/1750-3841.16233
Quiroga, E. N., Sgariglia, M. A., Molina, C. F., Sampietro, D. A., Soberón, J. R., & Vattuone, M. A. (2009). Purification and characterization of an exo-polygalacturonase from Pycnoporus sanguineus. Mycological Research, 113(12), 1404-1410. https://doi.org/10.1016/j.mycres.2009.09.007
Rashad, M. M., Abdou, H. M., Mahmoud, A. E., & Nooman, M. U. (2009). Nutritional analysis and enzyme activities of Pleurotus ostreatus cultivated on Citrus limonium and Carica papaya wastes. Australian Journal of Basic and Applied Sciences, 3(4), 3352-3360.
Ravichandran, A., Kolte, A., Dhali, A., Gopinath, S., & Srid, M. (2022). Transcriptomic analysis of the white-rot basidiomycete Lentinus squarrosulus to provide insights into its lignocellulose biodegradation ability. https://doi.org/10.21203/rs.3.rs-1136812/v1
Ray, A., Saykhedkar, S., Ayoubi-Canaan, P., Hartson, S. D., Prade, R., & Mort, A. J. (2012). Phanerochaete chrysosporium produces a diverse array of extracellular enzymes when grown on sorghum. Applied Microbiology and Biotechnology, 93(5), 2075-2089. https://doi.org/10.1007/s00253-012-3907-5
Raymond, P., Mshandete, A. M., & Kajumulo Kivaisi, A. (2015). Production of oxidative and hydrolytic enzymes by Coprinus cinereus (Schaeff.) gray from sisal wastes supplemented with cow dung manure. Biotechnology Research International, 2015, 1-9. https://doi.org/10.1155/2015/650543
Riley, R., Salamov, A. A., Brown, D. W., Nagy, L. G., Floudas, D., Held, B. W., Levasseur, A., Lombard, V., Morin, E., Otillar, R., Lindquist, E. A., Sun, H., LaButti, K. M., Schmutz, J., Jabbour, D., Luo, H., Baker, S. E., Pisabarro, A. G., Walton, J. D., … Grigoriev, I. V. (2014). Extensive sampling of basidiomycete genomes demonstrates inadequacy of the white-rot/brown-rot paradigm for wood decay fungi. Proceedings of the National Academy of Sciences, 111(27), 9923-9928. https://doi.org/10.1073/pnas.1400592111
Ruiz-Dueñas, F. J., Barrasa, J. M., Sánchez-García, M., Camarero, S., Miyauchi, S., Serrano, A., Linde, D., Babiker, R., Drula, E., Ayuso-Fernández, I., Pacheco, R., Padilla, G., Ferreira, P., Barriuso, J., Kellner, H., Castanera, R., Alfaro, M., Ramírez, L., Pisabarro, A. G., … Martínez, A. T. (2021). Genomic analysis enlightens Agaricales lifestyle evolution and increasing peroxidase diversity. Molecular Biology and Evolution, 38(4), 1428-1446. https://doi.org/10.1093/molbev/msaa301
Ruiz, H. A., Rodríguez-Jasso, R. M., Hernandez-Almanza, A., Contreras-Esquivel, J. C., & Aguilar, C. N. (2017). Pectinolytic enzymes. In: Current developments in biotechnology and bioengineering, pp. 47-71. Elsevier. https://doi.org/10.1016/B978-0-444-63662-1.00003-8
Rytioja, J., Hildén, K., Yuzon, J., Hatakka, A., de Vries, R. P., & Mäkelä, M. R. (2014). Plant-polysaccharide-degrading enzymes from basidiomycetes. Microbiology and Molecular Biology Reviews, 78(4), 614-649. https://doi.org/10.1128/MMBR.00035-14
Sakamoto, M., Shirane, Y., Naribayashi, I., Kimura, K., Morishita, N., Sakamoto, T., & Sakai, T. (1994). Purification and characterization of a rhamnogalacturonase with protopectinase activity from Trametes sanguinea. European Journal of Biochemistry, 226(2), 285-291. https://doi.org/10.1111/j.1432-1033.1994.tb20052.x
Sakamoto, T., Hours, R. A., & Sakai, T. (1995). Enzymic pectin extraction from protopectins using microbial protopectinases. Process Biochemistry, 30(5), 403-409. https://doi.org/10.1016/0032-9592(94)00027-1
Santos, M. P. F., Bezerra, C. O., Casteliano, G. A., Uetanabaro, A. P. T., Silva, E. G. P. da, & Costa, A. M. da. (2025). Production of enzyme for Pleurotus pulmonarius by solid-state fermentation on peach-palm and cocoa waste. Fine Chemical Engineering, 102-111. https://doi.org/10.37256/fce.6120255942
Sathya, T. A., Jacob, A. M., & Khan, M. (2014). Cloning and molecular modelling of pectin degrading glycosyl hydrolase of family 28 from soil metagenomic library. Molecular Biology Reports, 41(4), 2645-2656. https://doi.org/10.1007/s11033-014-3123-8
Schimpf, U., & Schulz, R. (2016). Industrial by-products from white-rot fungi production. Part I: Generation of enzyme preparations and chemical, protein biochemical and molecular biological characterization. Process Biochemistry, 51(12), 2034-2046. https://doi.org/10.1016/j.procbio.2016.08.032
Schirp, A., Farrell, R. L., Kreber, B., & Singh, A. P. (2003). Advances in understanding the ability of sapstaining fungi to produce cell wall-degrading enzymes. Wood and Fiber Science, 35(3), 434-444.
Shanley, N. A., van den Broek, L. A. M., Voragen, A. G. J., & Coughlan, M. P. (1993). Isolation and characterization of an endopolygalacturonase from Phanerochaete chrysosporium. Journal of Biotechnology, 28(2-3), 179-197. https://doi.org/10.1016/0168-1656(93)90169-N
Sharma, N., Rathore, M., & Sharma, M. (2013). Microbial pectinase: sources, characterization and applications. Reviews in Environmental Science and Bio/Technology, 12(1), 45-60. https://doi.org/10.1007/s11157-012-9276-9
Sherief, A. A., El-Tanash, A. B., & Temraz, A. M. (2009). Lignocellulolytic enzymes and substrate utilization during growth and fruiting of Pleurotus ostreatus on some solid wastes. Journal of Environmental Science and Technology, 3(1), 18-34. https://doi.org/10.3923/jest.2010.18.34
Shoily, S. S., Fatema, K., Dina, R. B., Biswas, A., Haque, P., Rahman, M. M., Uddin, M. Z., & Sajib, A. A. (2023). The pectinolytic activity of Burkholderia cepacia and its application in the bioscouring of cotton knit fabric. Journal of Genetic Engineering and Biotechnology, 21(1), 136. https://doi.org/10.1186/s43141-023-00596-5
Shrestha, S., Rahman, M. S., & Qin, W. (2021). New insights in pectinase production development and industrial applications. Applied Microbiology and Biotechnology, 105(24), 9069-9087. https://doi.org/10.1007/s00253-021-11705-0
Singh, B., Soni, S. K., Mathur, P., & Garg, N. (2024). Microbial multienzyme viz., pectinase, cellulase and amylase production using fruit and vegetable waste as substrate - A review. Applied Microbiology, 4(3), 1232-1246. https://doi.org/10.3390/applmicrobiol4030084
Sipos, G., Prasanna, A. N., Walter, M. C., O'Connor, E., Bálint, B., Krizsán, K., Kiss, B., Hess, J., Varga, T., Slot, J., Riley, R., Bóka, B., Rigling, D., Barry, K., Lee, J., Mihaltcheva, S., LaButti, K., Lipzen, A., Waldron, R., … Nagy, L. G. (2017). Genome expansion and lineage-specific genetic innovations in the forest pathogenic fungi Armillaria. Nature Ecology & Evolution, 1(12), 1931-1941. https://doi.org/10.1038/s41559-017-0347-8
Sista Kameshwar, A. K., & Qin, W. (2018). Comparative study of genome-wide plant biomass-degrading CAZymes in white rot, brown rot and soft rot fungi. Mycology, 9(2), 93-105. https://doi.org/10.1080/21501203.2017.1419296
Stoilova, I., & Krastanov, A. (2008). Overproduction of laccase and pectinase by microbial associations in solid substrate fermentation. Applied Biochemistry and Biotechnology, 149(1), 45-51. https://doi.org/10.1007/s12010-007-8013-2
Tanaka, Y., Suzuki, T., Nakamura, L., Nakamura, M., Ebihara, S., Kurokura, T., Iigo, M., Dohra, H., Habu, N., & Konno, N. (2019). A GH family 28 endo-polygalacturonase from the brown-rot fungus Fomitopsis palustris: Purification, gene cloning, enzymatic characterization and effects of oxalate. International Journal of Biological Macromolecules, 123, 108-116. https://doi.org/10.1016/j.ijbiomac.2018.11.004
Tapre, A. R., & Jain, R. K. (2014). Pectinases: Enzymes for fruit processing industry. International Food Research Journal, 21(2), 447-453.
Urbániková, Ľ. (2021). CE16 acetylesterases: in silico analysis, catalytic machinery prediction and comparison with related SGNH hydrolases. 3 Biotech, 11(2), 84. https://doi.org/10.1007/s13205-020-02575-w
Veneault-Fourrey, C., Commun, C., Kohler, A., Morin, E., Balestrini, R., Plett, J., Danchin, E., Coutinho, P., Wiebenga, A., de Vries, R. P., Henrissat, B., & Martin, F. (2014). Genomic and transcriptomic analysis of Laccaria bicolor CAZome reveals insights into polysaccharides remodelling during symbiosis establishment. Fungal Genetics and Biology, 72, 168-181. https://doi.org/10.1016/j.fgb.2014.08.007
Wang, Y., Liao, Y., Gou, C., Zhang, H., Chen, L., & Bao, Y. (2024). Effect of Lentinus sajor-caju on the chemical composition and antioxidant activity of highland barley straw under solid-state fermentation. Frontiers in Microbiology, 15. https://doi.org/10.3389/fmicb.2024.1365254
Wu, P., Yang, S., Zhan, Z., & Zhang, G. (2020). Origins and features of pectate lyases and their applications in industry. Applied Microbiology and Biotechnology, 104(17), 7247-7260. https://doi.org/10.1007/s00253-020-10769-8
Xie, C., Yan, L., Gong, W., Zhu, Z., Tan, S., Chen, D., Hu, Z., & Peng, Y. (2016). Effects of different substrates on lignocellulosic enzyme expression, enzyme activity, substrate utilization and biological efficiency of Pleurotus eryngii. Cellular Physiology and Biochemistry, 39(4), 1479-1494. https://doi.org/10.1159/000447851
Yang, R., Meng, D., Hu, X., Ni, Y., & Li, Q. (2013). Saccharification of pumpkin residues by coculturing of Trichoderma reesei RUT-C30 and Phanerochaete chrysosporium burdsall with delayed inoculation timing. Journal of Agricultural and Food Chemistry, 61(38), 9192-9199. https://doi.org/10.1021/jf402199j
Zhang, F., Labourel, A., Haon, M., Kemppainen, M., Da Silva Machado, E., Brouilly, N., Veneault‐Fourrey, C., Kohler, A., Rosso, M., Pardo, A., Henrissat, B., Berrin, J., & Martin, F. (2022). The ectomycorrhizal basidiomycete Laccaria bicolor releases a GH28 polygalacturonase that plays a key role in symbiosis establishment. New Phytologist, 233(6), 2534-2547. https://doi.org/10.1111/nph.17940
Zhang, Y., Wang, J., Yajun, C., Zhou, M., Wang, W., Geng, M., Xu, D., & Xu, Z. (2020). Comparative genomics uncovers the genetic diversity and synthetic biology of secondary metabolite production of Trametes. Mycobiology, 48(2), 104-114. https://doi.org/10.1080/12298093.2020.1725361
Zheng, L., Xu, Y., Li, Q., & Zhu, B. (2021). Pectinolytic lyases: a comprehensive review of sources, category, property, structure, and catalytic mechanism of pectate lyases and pectin lyases. Bioresources and Bioprocessing, 8(1), 79. https://doi.org/10.1186/s40643-021-00432-z
Zhu, N., Liu, J., Yang, J., Lin, Y., Yang, Y., Ji, L., Li, M., & Yuan, H. (2016). Comparative analysis of the secretomes of Schizophyllum commune and other wood-decay basidiomycetes during solid-state fermentation reveals its unique lignocellulose-degrading enzyme system. Biotechnology for Biofuels, 9(1), 42. https://doi.org/10.1186/s13068-016-0461-x
Zilly, A., dos Santos Bazanella, G. C., Helm, C. V., Araújo, C. A. V., de Souza, C. G. M., Bracht, A., & Peralta, R. M. (2012). Solid-state bioconversion of passion fruit waste by white-rot fungi for production of oxidative and hydrolytic enzymes. Food and Bioprocess Technology, 5(5), 1573-1580. https://doi.org/10.1007/s11947-011-0532-8
Zubyk, P., & Klechak, I. (2025). Screening of Pleurotus ostreatus strains as potential pectin lyase producer. Продовольчі ресурси, 13(24), 68-73. https://doi.org/10.31073/foodresources2025-24-07
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