Penicillium chrysogenum as a fungal factory for feruloyl esterases.
Extracellular proteome
Feruloyl esterase
Fungi
Lignocellulose
Penicillium chrysogenum
Penicillium rubens
Journal
Applied microbiology and biotechnology
ISSN: 1432-0614
Titre abrégé: Appl Microbiol Biotechnol
Pays: Germany
ID NLM: 8406612
Informations de publication
Date de publication:
Feb 2023
Feb 2023
Historique:
received:
24
08
2022
accepted:
08
12
2022
revised:
05
12
2022
pubmed:
4
1
2023
medline:
19
1
2023
entrez:
3
1
2023
Statut:
ppublish
Résumé
Plant biomass is a promising substrate for biorefinery, as well as a source of bioactive compounds, platform chemicals, and precursors with multiple industrial applications. These applications depend on the hydrolysis of its recalcitrant structure. However, the effective biological degradation of plant cell walls requires several enzymatic groups acting synergistically, and novel enzymes are needed in order to achieve profitable industrial hydrolysis processes. In the present work, a feruloyl esterase (FAE) activity screening of Penicillium spp. strains revealed a promising candidate (Penicillium rubens Wisconsin 54-1255; previously Penicillium chrysogenum), where two FAE-ORFs were identified and subsequently overexpressed. Enzyme extracts were analyzed, confirming the presence of FAE activity in the respective gene products (PrFaeA and PrFaeB). PrFaeB-enriched enzyme extracts were used to determine the FAE activity optima (pH 5.0 and 50-55 °C) and perform proteome analysis by means of MALDI-TOF/TOF mass spectrometry. The studies were completed with the determination of other lignocellulolytic activities, an untargeted metabolite analysis, and upscaled FAE production in stirred tank reactors. The findings described in this work present P. rubens as a promising lignocellulolytic enzyme producer. KEY POINTS: • Two Penicillium rubens ORFs were first confirmed to have feruloyl esterase activity. • Overexpression of the ORFs produced a novel P. rubens strain with improved activity. • The first in-depth proteomic study of a P. rubens lignocellulolytic extract is shown.
Identifiants
pubmed: 36595038
doi: 10.1007/s00253-022-12335-w
pii: 10.1007/s00253-022-12335-w
doi:
Substances chimiques
Plant Extracts
0
Fungal Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
691-717Subventions
Organisme : Ministerio de Economía y Competitividad
ID : CTM2012-32026
Informations de copyright
© 2022. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.
Références
Adav SS, Ravindran A, Sze SK (2012) Quantitative proteomic analysis of lignocellulolytic enzymes by Phanerochaete chrysosporium on different lignocellulosic biomass. J Proteomics 75(5):1493–1504. https://doi.org/10.1016/j.jprot.2011.11.020
doi: 10.1016/j.jprot.2011.11.020
Alam MA, Subhan N, Hossain H, Hossain M, Reza HM, Rahman MM, Ullah MO (2016) Hydroxycinnamic acid derivatives: a potential class of natural compounds for the management of lipid metabolism and obesity. Nutr Metab 13(1):1–13. https://doi.org/10.1186/s12986-016-0080-3
doi: 10.1186/s12986-016-0080-3
Almagro Armenteros JJ, Tsirigos KD, Sønderby CK, Petersen TN, Winther O, Brunak S, von Heijne G, Nielsen H (2019) SignalP 50 improves signal peptide predictions using deep neural networks. Nat Biotechnol 37(4):420–423. https://doi.org/10.1038/s41587-019-0036-z
doi: 10.1038/s41587-019-0036-z
Arnau J, Yaver D, Hjort CM (2020) Strategies and challenges for the development of industrial enzymes using fungal cell factories. pp 179–210
Barredo Fuente JL, Rodríguez Saiz M, Moreno Valle MÁ, Collados de la Vieja AJ, Salto Maldonado F, Díez B (1998) Promotores de los genes glutamato deshidrogenasa, β-n-acetilhexosaminidasa Ƴ-actina y su utilizacion en sistemas de expresion, secrecion y antisentido de hongos filamentosos.
Barreiro C, Barredo J-L (2021) Worldwide clinical demand for antibiotics: Is it a real countdown? In: Barreiro C, Barredo J-L (eds) Antimicrobial Therapies: Methods and Protocols. Springer, US, New York, NY, pp 3–15
doi: 10.1007/978-1-0716-1358-0_1
Barreiro C, García-Estrada C, Martín JF (2012a) Proteomics methodology applied to the analysis of filamentous fungi - New trends for an impressive diverse group of organisms. In: Prasain JK (ed). vol 78. InTech, Rijeka, Croacia, pp 159–171
Barreiro C, Martín JF, García-Estrada C (2012b) Proteomics shows new faces for the old penicillin producer Penicillium chrysogenum. J Biomed Biotechnol 2012b:ID 105109, 1–15 https://doi.org/10.5772/31320
Bendtsen JD, Jensen LJ, Blom N, von Heijne G, Brunak S (2004) Feature-based prediction of non-classical and leaderless protein secretion. Protein Eng Des Sel 17(4):349–356. https://doi.org/10.1093/protein/gzh037
doi: 10.1093/protein/gzh037
Benoit I, Navarro D, Marnet N, Rakotomanomana N, Lesage-Meessen L, Sigoillot J-C, Asther M, Asther M (2006) Feruloyl esterases as a tool for the release of phenolic compounds from agro-industrial by-products. Carbohydr Res 341(11):1820–1827. https://doi.org/10.1016/j.carres.2006.04.020
doi: 10.1016/j.carres.2006.04.020
Bhatnagar D, Yu J, Ehrlich KC (2002) Toxins of filamentous fungi. Chem Immunol 81:167–206. https://doi.org/10.1159/000058867
doi: 10.1159/000058867
Boratyn GM, Camacho C, Cooper PS, Coulouris G, Fong A, Ma N, Madden TL, Matten WT, McGinnis SD, Merezhuk Y, Raytselis Y, Sayers EW, Tao T, Ye J, Zaretskaya I (2013) BLAST: a more efficient report with usability improvements. Nucleic Acids Res 41(Web Server issue):W29–33 https://doi.org/10.1093/nar/gkt282
Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72(1–2):248–254. https://doi.org/10.1016/0003-2697(76)90527-3
doi: 10.1016/0003-2697(76)90527-3
Braga CMP, Delabona PdS, Lima DJdS, Paixão DAA, Pradella JGdC, Farinas CS (2014) Addition of feruloyl esterase and xylanase produced on-site improves sugarcane bagasse hydrolysis. Bioresour Technol 170:316–324. https://doi.org/10.1016/j.biortech.2014.07.115
doi: 10.1016/j.biortech.2014.07.115
Candiano G, Bruschi M, Musante L, Santucci L, Ghiggeri GM, Carnemolla B, Orecchia P, Zardi L, Righetti PG (2004) Blue silver: a very sensitive colloidal Coomassie G-250 staining for proteome analysis. Electrophoresis 25(9):1327–1333. https://doi.org/10.1002/elps.200305844
doi: 10.1002/elps.200305844
Casqueiro J, Banuelos O, Gutierrez S, Hijarrubia MJ, Martin JF (1999) Intrachromosomal recombination between direct repeats in Penicillium chrysogenum: gene conversion and deletion events. Mol Gen Genet 261(6):994–1000. https://doi.org/10.1007/s004380051048
doi: 10.1007/s004380051048
Castanares A, McCrae SI, Wood TM (1992) Purification and properties of a feruloyl/p-coumaroyl esterase from the fungus Penicillium pinophilum. Enzyme Microb Technol 14(11):875–884. https://doi.org/10.1016/0141-0229(92)90050-X
doi: 10.1016/0141-0229(92)90050-X
Chapman J, Ismail A, Dinu C (2018) Industrial applications of enzymes: Recent advances, techniques, and outlooks. Catalysts 8(6):238–238. https://doi.org/10.3390/catal8060238
doi: 10.3390/catal8060238
Chávez R, Bull P, Eyzaguirre J (2006) The xylanolytic enzyme system from the genus Penicillium. J Biotechnol 123(4):413–433. https://doi.org/10.1016/j.jbiotec.2005.12.036
doi: 10.1016/j.jbiotec.2005.12.036
Cleveland TE, Dowd PF, Desjardins AE, Bhatnagar D, Cotty PJ (2003) United States Department of Agriculture - Agricultural Research Service research on pre-harvest prevention of mycotoxins and mycotoxigenic fungi in US crops. Pest Manage Sci 59(6–7):629–642. https://doi.org/10.1002/ps.724
doi: 10.1002/ps.724
Creek DJ, Dunn WB, Fiehn O, Griffin JL, Hall RD, Lei Z, Mistrik R, Neumann S, Schymanski EL, Sumner LW, Trengove R, Wolfender J-L (2014) Metabolite identification: are you sure? And how do your peers gauge your confidence? Metabolomics 10:350–353. https://doi.org/10.1007/s11306-014-0656-8
doi: 10.1007/s11306-014-0656-8
Crepin VF, Faulds CB, Connerton IF (2004) Functional classification of the microbial feruloyl esterases. Appl Microbiol Biotechnol 63(6):647–652. https://doi.org/10.1007/s00253-003-1476-3
doi: 10.1007/s00253-003-1476-3
Dashtban M, Schraft H, Qin W (2009) Fungal bioconversion of lignocellulosic residues; opportunities & perspectives. Int J Biol Sci 5(6):578–595. https://doi.org/10.7150/ijbs.5.578
doi: 10.7150/ijbs.5.578
de Oliveira DM, Finger-Teixeira A, Rodrigues Mota T, Salvador VH, Moreira-Vilar FC, Correa Molinari HB, Craig Mitchell RA, Marchiosi R, Ferrarese-Filho O, Dantas dos Santos W (2015) Ferulic acid: a key component in grass lignocellulose recalcitrance to hydrolysis. Plant Biotechnol J 13:1224–1232. https://doi.org/10.1111/pbi.12292
doi: 10.1111/pbi.12292
de Vries RP, Pa VanKuyk, Kester HCM, Visser J (2002) The Aspergillus niger faeB gene encodes a second feruloyl esterase involved in pectin and xylan degradation and is specifically induced in the presence of aromatic compounds. Biochem J 363(Pt 2):377–386. https://doi.org/10.1042/0264-6021:3630377
doi: 10.1042/0264-6021:3630377
Degnes KF, Kvitvang HFN, Haslene-Hox H, Aasen IM (2017) Changes in the profiles of metabolites originating from protein degradation during ripening of dry cured ham. Food Bioprocess Technol 10(6):1122–1130. https://doi.org/10.1007/s11947-017-1894-3
doi: 10.1007/s11947-017-1894-3
Díez B, Rodrí-guez-Sáiz M, la Fuente JL, Moreno MÁN, Barredo JL (2005) The nagA gene of Penicillium chrysogenum encoding β- N -acetylglucosaminidase. FEMS Microbiol Lett 242(2):257–264. https://doi.org/10.1016/j.femsle.2004.11.017
doi: 10.1016/j.femsle.2004.11.017
Dilokpimol A, Mäkelä MR, Aguilar-Pontes MV, Benoit-Gelber I, Hildén KS, de Vries RP (2016) Diversity of fungal feruloyl esterases: updated phylogenetic classification, properties, and industrial applications. Biotechnol Biofuels 9(1):231–231. https://doi.org/10.1186/s13068-016-0651-6
doi: 10.1186/s13068-016-0651-6
Dilokpimol A, Mäkelä MR, Mansouri S, Belova O, Waterstraat M, Bunzel M, Vries RPD, Hildén KS (2017) Expanding the feruloyl esterase gene family of Aspergillus niger by characterization of a feruloyl esterase, FaeC. N Biotechnol 37:200–209. https://doi.org/10.1016/j.nbt.2017.02.007
doi: 10.1016/j.nbt.2017.02.007
Dilokpimol A, Peng M, Di Falco M, Chin AWT, Hegi RMW, Granchi Z, Tsang A, Hilden KS, Makela MR, de Vries RP (2020) Penicillium subrubescens adapts its enzyme production to the composition of plant biomass. Bioresour Technol 311:123477. https://doi.org/10.1016/j.biortech.2020.123477
doi: 10.1016/j.biortech.2020.123477
Domínguez-Santos R, Kosalková K, García-Estrada C, Barreiro C, Ibáñez A, Morales A, Martín J-F (2017) Casein phosphopeptides and CaCl2 increase penicillin production and cause an increment in microbody/peroxisome proteins in Penicillium chrysogenum. J Proteomics 156:52–62. https://doi.org/10.1016/j.jprot.2016.12.021
doi: 10.1016/j.jprot.2016.12.021
Donaghy JA, McKay AM (1994) Novel screening assay for the detection of phenolic acid esterases. World J Microbiol Biotechnol 10(1):41–44. https://doi.org/10.1007/BF00357561
doi: 10.1007/BF00357561
Donaghy JA, McKay AM (1995) Production of feruloyl/rho-coumaroyl esterase activity by Penicillium expansum, Penicillium brevicompactum and Aspergillus niger. J Appl Bacteriol 79(6):657–662
doi: 10.1111/j.1365-2672.1995.tb00951.x
Donaghy J, Kelly PF, McKay AM (1998) Detection of ferulic acid esterase production by Bacillus spp. and lactobacilli. Appl Microbiol Biotechnol 50:257–260. https://doi.org/10.1007/s002530051286
doi: 10.1007/s002530051286
Drula E, Garron M-L, Dogan S, Lombard V, Henrissat B, Terrapon N (2022) The carbohydrate-active enzyme database: functions and literature. Nucleic Acids Res 50(D1):D571–D577. https://doi.org/10.1093/nar/gkab1045
doi: 10.1093/nar/gkab1045
Escamilla-Alvarado C, Pérez-Pimienta JA, Ponce-Noyola T, Poggi-Varaldo HM (2017) An overview of the enzyme potential in bioenergy-producing biorefineries. J Chem Technol Biotechnol 92(5):906–924. https://doi.org/10.1002/jctb.5088
doi: 10.1002/jctb.5088
Faulds CB (2010) What can feruloyl esterases do for us? Phytochem Rev 9(1):121–132. https://doi.org/10.1007/s11101-009-9156-2
doi: 10.1007/s11101-009-9156-2
Faulds CB, Zanichelli D, Crepin VF, Connerton IF, Juge N, Bhat MK, Waldron KW (2003) Specificity of feruloyl esterases for water-extractable and water-unextractable feruloylated polysaccharides: influence of xylanase. J Cereal Sci 38(3):281–288. https://doi.org/10.1016/S0733-5210(03)00029-8
doi: 10.1016/S0733-5210(03)00029-8
Fazary AE, Ju Y-H (2007) Feruloyl esterases as biotechnological tools: current and future perspectives. Acta Biochim Biophys Sin 39(11):811–828. https://doi.org/10.1111/j.1745-7270.2007.00348.x
doi: 10.1111/j.1745-7270.2007.00348.x
Fazary AE, Ju Y-H (2008) The large-scale use of feruloyl esterases in industry. Biotechnol Mol Biol 3(5):95–110
Fernández-Aguado M, Martín JF, Rodríguez-Castro R, García-Estrada C, Albillos SM, Teijeira F, Ullán RV (2014) New insights into the isopenicillin N transport in Penicillium chrysogenum. Metab Eng 22:89–103. https://doi.org/10.1016/j.ymben.2014.01.004
doi: 10.1016/j.ymben.2014.01.004
Fierro F, Vaca I, Castillo NI, García-Rico RO, Chávez R (2022) Penicillium chrysogenum, a vintage model with a cutting-edge profile in Biotechnology. Microorganisms 10(3):573–573. https://doi.org/10.3390/microorganisms10030573
doi: 10.3390/microorganisms10030573
Franco BE, Martínez MA, Sánchez Rodríguez MA, Wertheimer AI (2009) The determinants of the antibiotic resistance process. Infect Drug Resist 2(1):1–11. https://doi.org/10.2147/IDR.S4899
doi: 10.2147/IDR.S4899
Frisvad JC, Skouboe P, Samson RA (2005) Taxonomic comparison of three different groups of aflatoxin producers and a new efficient producer of aflatoxin B1, sterigmatocystin and 3-O-methylsterigmatocystin, Aspergillus rambellii sp. nov. Syst Appl Microbiol 28(5):442–453. https://doi.org/10.1016/j.syapm.2005.02.012
doi: 10.1016/j.syapm.2005.02.012
García-Calvo L, Ullán RV, Fernández-Aguado M, García-Lino AM, Balaña-Fouce R, Barreiro C (2018) Secreted protein extract analyses present the plant pathogen Alternaria alternata as a suitable industrial enzyme toolbox. J Proteomics 177:48–64. https://doi.org/10.1016/j.jprot.2018.02.012
doi: 10.1016/j.jprot.2018.02.012
García-Estrada C, Ullán RV, Albillos SM, Fernández-Bodega MÁ, Durek P, Von Döhren H, Martín JF (2011) A single cluster of coregulated genes encodes the biosynthesis of the mycotoxins roquefortine C and meleagrin in Penicillium chrysogenum. Chem Biol 18(11):1499–1512. https://doi.org/10.1016/j.chembiol.2011.08.012
doi: 10.1016/j.chembiol.2011.08.012
García-Estrada C, Martín JF, Cueto L, Barreiro C (2020) Omics approaches applied to Penicillium chrysogenum and penicillin production: revealing the secrets of improved productivity. Genes 11(6):712–712. https://doi.org/10.3390/genes11060712
doi: 10.3390/genes11060712
Garre V, Müller U, Tudzynski P (1998) Cloning, characterization, and targeted disruption of cpcat1, Coding for an in planta secreted catalase of Claviceps purpurea. Mol Plant-Microbe Interact 11(8):772–783. https://doi.org/10.1094/MPMI.1998.11.8.772
doi: 10.1094/MPMI.1998.11.8.772
Ghose TK (1987) Measurement of cellulase activities. Pure & Appl Chem 59(2):257–268
doi: 10.1351/pac198759020257
Gifre L, Arís A, Bach À, Garcia-Fruitós E (2017) Trends in recombinant protein use in animal production. Microb Cell Factories 16(1):40–40. https://doi.org/10.1186/s12934-017-0654-4
doi: 10.1186/s12934-017-0654-4
Gopalan N, Rodríguez-Duran LV, Saucedo-Castaneda G, Nampoothiri KM (2015) Review on technological and scientific aspects of feruloyl esterases: a versatile enzyme for biorefining of biomass. Bioresour Technol 193:534–544. https://doi.org/10.1016/j.biortech.2015.06.117
doi: 10.1016/j.biortech.2015.06.117
Guerriero G, Hausman J-F, Strauss J, Ertan H, Siddiqui KS (2016) Lignocellulosic biomass: biosynthesis, degradation, and industrial utilization. Eng Life Sci 16(1):1–16. https://doi.org/10.1002/elsc.201400196
doi: 10.1002/elsc.201400196
Gutiérrez S, Díez B, Alvarez E, Barredo JL, Martín JF (1991) Expression of the penDE gene of Penicillium chrysogenum encoding isopenicillin N acyltransferase in Cephalosporium acremonium: production of benzylpenicillin by the transformants. Mol Gen Genet 225(1):56–64
doi: 10.1007/BF00282642
Hanahan D (1983) Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166(4):557–580. https://doi.org/10.1016/S0022-2836(83)80284-8
doi: 10.1016/S0022-2836(83)80284-8
Havliš J, Thomas H, Šebela M, Shevchenko A (2003) Fast-response proteomics by accelerated in-gel digestion of proteins. Anal Chem 75(6):1300–1306. https://doi.org/10.1021/ac026136s
doi: 10.1021/ac026136s
Hermoso JA, Sanz-Aparicio J, Molina R, Juge N, González R, Faulds CB (2004) The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family. J Mol Biol 338(3):495–506. https://doi.org/10.1016/j.jmb.2004.03.003
doi: 10.1016/j.jmb.2004.03.003
Houbraken J, Frisvad JC, Samson RA (2011) Fleming’s penicillin producing strain is not Penicillium chrysogenum but P. rubens. IMA Fungus 2(1):87–95. https://doi.org/10.5598/imafungus.2011.02.01.12
doi: 10.5598/imafungus.2011.02.01.12
Huerta-Cepas J, Szklarczyk D, Heller D, Hernández-Plaza A, Forslund SK, Cook H, Mende DR, Letunic I, Rattei T, Jensen LJ, von Mering C, Bork P (2019) eggNOG 50: a hierarchical, functionally and phylogenetically annotated orthology resource based on 5090 organisms and 2502 viruses. Nucleic Acids Res 47(D1):D309–D314. https://doi.org/10.1093/nar/gky1085
doi: 10.1093/nar/gky1085
Hutnan M, Dritl M, Mrfatkova L (2000) Anaerobic biodegradation of sugar beet pulp. Biodegradation 11:203–211
doi: 10.1023/A:1011139621329
Jäger G, Büchs J (2012) Biocatalytic conversion of lignocellulose to platform chemicals. Biotechnol J 7(9):1122–1136. https://doi.org/10.1002/biot.201200033
doi: 10.1002/biot.201200033
Jami M-S, Barreiro C, García-Estrada C, Martín J-F (2010a) Proteome analysis of the penicillin producer Penicillium chrysogenum. Mol Cell Proteomics 9(6):1182–1198. https://doi.org/10.1074/mcp.M900327-MCP200
doi: 10.1074/mcp.M900327-MCP200
Jami M-S, García-Estrada C, Barreiro C, Cuadrado A-A, Salehi-Najafabadi Z, Martín J-F (2010b) The Penicillium chrysogenum extracellular proteome Conversion from a food-rotting strain to a versatile cell factory for white biotechnology. Mol Cell Proteomics 9(12):2729–2744. https://doi.org/10.1074/mcp.M110.001412
doi: 10.1074/mcp.M110.001412
Jami M-S, Martín J-F, Barreiro C, Domínguez-Santos R, Vasco-Cárdenas M-F, Pascual M, García-Estrada C (2018) Catabolism of phenylacetic acid in Penicillium rubens Proteome-wide analysis in response to the benzylpenicillin side chain precursor. J Proteomics 187(1):243–259
doi: 10.1016/j.jprot.2018.08.006
Jimenez-Flores R, Fake G, Carroll J, Hood E, Howard J (2010) A novel method for evaluating the release of fermentable sugars from cellulosic biomass. Enzyme Microb Technol 47(5):206–211. https://doi.org/10.1016/j.enzmictec.2010.07.003
doi: 10.1016/j.enzmictec.2010.07.003
Kiel JAKW, van den Berg MA, Fusetti F, Poolman B, Bovenberg RAL, Veenhuis M, van der Klei IJ (2009) Matching the proteome to the genome: the microbody of penicillin-producing Penicillium chrysogenum cells. Funct Integr Genomics 9(2):167–184. https://doi.org/10.1007/s10142-009-0110-6
doi: 10.1007/s10142-009-0110-6
Kosalková K, García-Estrada C, Ullán RV, Godio RP, Feltrer R, Teijeira F, Mauriz E, Martín JF (2009) The global regulator LaeA controls penicillin biosynthesis, pigmentation and sporulation, but not roquefortine C synthesis in Penicillium chrysogenum. Biochimie 91(2):214–225. https://doi.org/10.1016/j.biochi.2008.09.004
doi: 10.1016/j.biochi.2008.09.004
Koseki T, Furuse S, Iwano K, Matsuzawa H (1998) Purification and characterization of a feruloyl esterase from Aspergillus awamori. Biosci, Biotechnol, Biochem 62(10):2032–2034
doi: 10.1271/bbb.62.2032
Koseki T, Fushinobu S, Ardiansyah SH, Komai M (2009a) Occurrence, properties, and applications of feruloyl esterases. Appl Microbiol Biotechnol 84(5):803–810. https://doi.org/10.1007/s00253-009-2148-8
doi: 10.1007/s00253-009-2148-8
Koseki T, Hori A, Seki S, Murayama T, Shiono Y (2009b) Characterization of two distinct feruloyl esterases, AoFaeB and AoFaeC, from Aspergillus oryzae. Appl Microbiol Biotechnol 83(4):689–696. https://doi.org/10.1007/s00253-009-1913-z
doi: 10.1007/s00253-009-1913-z
Kroon PA, Williamson G, Fish NM, Archer DB, Belshaw NJ (2000) A modular esterase from Penicillium funiculosum which releases ferulic acid from plant cell walls and binds crystalline cellulose contains a carbohydrate binding module. Eur J Biochem 267(23):6740–6752. https://doi.org/10.1046/j.1432-1327.2000.01742.x
doi: 10.1046/j.1432-1327.2000.01742.x
Kühnel S, Pouvreau L, Appeldoorn MM, Hinz SWA, Schols HA, Gruppen H (2012) The ferulic acid esterases of Chrysosporium lucknowense C1: purification, characterization and their potential application in biorefinery. Enzyme Microb Technol 50(1):77–85. https://doi.org/10.1016/j.enzmictec.2011.09.008
doi: 10.1016/j.enzmictec.2011.09.008
Kumar CG, Kamle A, Mongolla P, Joseph J (2011) Parametric optimization of feruloyl esterase production from Aspergillus terreus strain GA2 isolated from tropical agro-ecosystems cultivating sweet sorghum. J Microbiol Biotechnol 21(9):947–953. https://doi.org/10.4014/jmb.1104.04014
doi: 10.4014/jmb.1104.04014
Kumar V, Singh D, Sangwan P, Gill pk (2014) Global market scenario of industrial enzymes. In: Beniwal V, Sharma AK (eds). Nova Science Publishers, Nueva York, EEUU, pp 173–196
Laich F, Fierro F, Martin JF (2002) Production of penicillin by fungi growing on food products: Identification of a complete penicillin gene cluster in Penicillium griseofulvum and a truncated cluster in Penicillium verrucosum. Appl Environ Microbiol 68(3):1211–1219. https://doi.org/10.1128/AEM.68.3.1211-1219.2002
doi: 10.1128/AEM.68.3.1211-1219.2002
Li C, Lin F, Li Y, Wei W, Wang H, Qin L, Zhou Z, Li B, Wu F, Chen Z (2016) A β-glucosidase hyper-production Trichoderma reesei mutant reveals a potential role of cel3D in cellulase production. Microb Cell Factories 15(1):151–151. https://doi.org/10.1186/s12934-016-0550-3
doi: 10.1186/s12934-016-0550-3
Liu G, Zhang L, Wei X, Zou G, Qin Y, Ma L, Li J, Zheng H, Wang S, Wang C, Xun L, Zhao G-P, Zhou Z, Qu Y (2013) Genomic and secretomic analyses reveal unique features of the lignocellulolytic enzyme system of Penicillium decumbens. PLoS ONE 8(2):e55185–e55185. https://doi.org/10.1371/journal.pone.0055185
doi: 10.1371/journal.pone.0055185
Lobanovska M, Pilla G (2017) Penicillin’s discovery and antibiotic resistance: Lessons for the future? Yale J Biol Med 90(1):135–145
López Alonso R, Ramírez de Lara C, Rivero L, Ruiz AE, Torres Zapata CT, Ullán RV (2011) Aplicación de una nueva FAE en la liberación químico-enzimática de ácido ferúlico a partir de pulpa de remolacha. Cienc Agron 19(21–25):2250–8872
De Lucca AJ (2007) Harmful fungi in both agriculture and medicine. Rev Iberoam Micol 24(1):3–13 20072403 [pii] ET - 2007/06/27
Lutzoni F, Kauff F, Cox CJ, McLaughlin D, Celio G, Dentinger C, Padamsee M, Hibbett D, James TY, Baloch E, Grube M, Reeb V, Hofstetter V, Schoch C, Arnold AE, Miadlikowska J, Spatafora J, Johnson D, Hambleton S, Crockett M, Shoemaker R, Sung GH, Lücking R, Lumbsch T, O’Donnell K, Binder M, Diederich P, Ertz D, Gueidan C, Hansen K, Harris RC, Hosaka K, Lim YW, Matheny B, Nishida H, Pfister D, Rogers J, Rossman A, Schmitt I, Sipman H, Stone J, Sugiyama J, Yahr R, Vilgalys R (2004) Assembling the fungal tree of life: Progress, classification, and evolution of subcellular traits. Am J Bot 91(10):1446–1480. https://doi.org/10.3732/ajb.91.10.1446
doi: 10.3732/ajb.91.10.1446
Lynd LR, Weimer PJ, van Zyl WH, Pretorius IS (2002) Microbial cellulose utilization: fundamentals and biotechnology. Microbiol Mol Biol Rev 66(3):506–577. https://doi.org/10.1128/MMBR.66.3.506-577.2002
doi: 10.1128/MMBR.66.3.506-577.2002
Mäkelä MR, Donofrio N, De Vries RP (2014) Plant biomass degradation by fungi. Fungal Genet Biol 72:2–9. https://doi.org/10.1016/j.fgb.2014.08.010
doi: 10.1016/j.fgb.2014.08.010
Mäkelä MR, Dilokpimol A, Koskela SM, Kuuskeri J, de Vries RP, Hildén K (2018) Characterization of a feruloyl esterase from Aspergillus terreus facilitates the division of fungal enzymes from Carbohydrate Esterase family 1 of the carbohydrate-active enzymes (CAZy) database. Microb Biotechnol 11(5):869–880. https://doi.org/10.1111/1751-7915.13273
doi: 10.1111/1751-7915.13273
Manisha YSK (2017) Technological advances and applications of hydrolytic enzymes for valorization of lignocellulosic biomass. Bioresour Technol 245:1727–1739. https://doi.org/10.1016/j.biortech.2017.05.066
doi: 10.1016/j.biortech.2017.05.066
Mardones W, Callegari E, Eyzaguirre J (2019) Corncob and sugar beet pulp induce specific sets of lignocellulolytic enzymes in Penicillium purpurogenum. Mycology 10(2):118–125. https://doi.org/10.1080/21501203.2018.1517830
doi: 10.1080/21501203.2018.1517830
Martínez-Gomariz M, Perumal P, Mekala S, Nombela C, Chaffin WL, Gil C (2009) Proteomic analysis of cytoplasmic and surface proteins from yeast cells, hyphae, and biofilms of Candida albicans. Proteomics 9(8):2230–2252. https://doi.org/10.1002/pmic.200700594
doi: 10.1002/pmic.200700594
Mathew S, Abraham TE (2004) Ferulic acid: an antioxidant found naturally in plant cell walls and feruloyl esterases involved in its release and their applications. Crit Rev Biotechnol 24(2–3):59–83. https://doi.org/10.1080/07388550490491467
doi: 10.1080/07388550490491467
Mathew S, Abraham TE (2006) Bioconversions of ferulic acid, an hydroxycinnamic acid. Crit Rev Microbiol 32(3):115–125. https://doi.org/10.1080/10408410600709628
doi: 10.1080/10408410600709628
Mattéotti C, Bauwens J, Brasseur C, Tarayre C, Thonart P, Destain J, Francis F, Haubruge E, De Pauw E, Portetelle D, Vandenbol M (2012) Identification and characterization of a new xylanase from Gram-positive bacteria isolated from termite gut (Reticulitermes santonensis). Protein Expression Purif 83(2):117–127. https://doi.org/10.1016/j.pep.2012.03.009
doi: 10.1016/j.pep.2012.03.009
McEvoy JDG (2016) Emerging food safety issues: an EU perspective. Drug Test Anal 8(5–6):511–520. https://doi.org/10.1002/dta.2015
doi: 10.1002/dta.2015
McLaughlin DJ, Hibbett DS, Lutzoni F, Spatafora JW, Vilgalys R (2009) The search for the fungal tree of life. Trends Microbiol 17(11):488–497. https://doi.org/10.1016/j.tim.2009.08.001
doi: 10.1016/j.tim.2009.08.001
Menon V, Rao M (2012) Trends in bioconversion of lignocellulose: biofuels, platform chemicals & biorefinery concept. Prog Energy Combust Sci 38(4):522–550. https://doi.org/10.1016/j.pecs.2012.02.002
doi: 10.1016/j.pecs.2012.02.002
Micard V, Renard CMGC, Thibault JF (1996) Enzymatic saccharification of sugar-beet pulp. Enzyme Microb Technol 19(3):162–170. https://doi.org/10.1016/0141-0229(95)00224-3
doi: 10.1016/0141-0229(95)00224-3
Miller JH (1972) Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, U.S., Nueva York, EEUU
Mitchell NJ, Bowers E, Hurburgh C, Wu F (2016) Potential economic losses to the US corn industry from aflatoxin contamination. Food Additives & Contaminants: Part A 33(3):540–550. https://doi.org/10.1080/19440049.2016.1138545
doi: 10.1080/19440049.2016.1138545
Muggia L, Grube M (2018) Fungal diversity in lichens: from extremotolerance to interactions with Algae. Life 8(2):15–15. https://doi.org/10.3390/life8020015
doi: 10.3390/life8020015
Nielsen H (2017) Predicting secretory proteins with SignalP. In: Kihara D (ed) vol 1611. Humana Press, Nueva York, EEUU, pp 59–73
Nielsen H, Engelbrecht J, Brunak S, Heijne GV (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10:1–6. https://doi.org/10.1142/S0129065797000537
doi: 10.1142/S0129065797000537
Nuero OM, Reyes F (2002) Enzymes for animal feeding from Penicillium chrysogenum mycelial wastes from penicillin manufacture. Lett Appl Microbiol 34(6):413–416. https://doi.org/10.1046/j.1472-765X.2002.01113.x
doi: 10.1046/j.1472-765X.2002.01113.x
Oleas G, Callegari E, Sepulveda R, Eyzaguirre J (2017) Heterologous expression, purification and characterization of three novel esterases secreted by the lignocellulolytic fungus Penicillium purpurogenum when grown on sugar beet pulp. Carbohydr Res 443–444:42–48. https://doi.org/10.1016/j.carres.2017.03.014
doi: 10.1016/j.carres.2017.03.014
Ou S, Kwok K-C (2004) Ferulic acid: pharmaceutical functions, preparation and applications in foods. J Sci Food Agric 84(11):1261–1269. https://doi.org/10.1002/jsfa.1873
doi: 10.1002/jsfa.1873
Patel AK, Singhania RR, Pandey A (2016) Novel enzymatic processes applied to the food industry. Curr Opin Food Sci 7:64–72. https://doi.org/10.1016/j.cofs.2015.12.002
doi: 10.1016/j.cofs.2015.12.002
Pérez J, Muñoz-Dorado J, de la Rubia T, Martínez J (2002) Biodegradation and biological treatments of cellulose, hemicellulose and lignin: an overview. Int Microbiol 5(2):53–63. https://doi.org/10.1007/s10123-002-0062-3
doi: 10.1007/s10123-002-0062-3
Perkins DN, Pappin DJC, Creasy DM, Cottrell JS (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20(18):3551–3567. https://doi.org/10.1002/(sici)1522-2683(19991201)20:18%3c3551::aid-elps3551%3e3.0.co;2-2
doi: 10.1002/(sici)1522-2683(19991201)20:18<3551::aid-elps3551>3.0.co;2-2
Pfaffl MW (2001) A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 29(9):45e–445. https://doi.org/10.1093/nar/29.9.e45
doi: 10.1093/nar/29.9.e45
Phuengmaung P, Sunagawa Y, Makino Y, Kusumoto T, Handa S, Sukhumsirichart W, Sakamoto T (2019) Identification and characterization of ferulic acid esterase from Penicillium chrysogenum 31B: de-esterification of ferulic acid decorated with L-arabinofuranoses and D-galactopyranoses in sugar beet pectin. Enzyme Microb Technol 131(June):109380–109380. https://doi.org/10.1016/j.enzmictec.2019.109380
doi: 10.1016/j.enzmictec.2019.109380
Pohl C, Kiel JAKW, Driessen AJM, Bovenberg RAL, Nygård Y (2016) CRISPR/Cas9 based genome editing of Penicillium chrysogenum. ACS Synth Biol:acssynbio.6b00082-acssynbio.6b00082 https://doi.org/10.1021/acssynbio.6b00082
Poonawalla FM, Patel KL, Iyengar MR (1965) Invertase production by Penicillium chrysogenum and other fungi in submerged fermentation. Appl Microbiol 13(5):749–754
doi: 10.1128/am.13.5.749-754.1965
Ralet MC, Faulds CB, Williamson G, Thibault JF (1994) Degradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger. Carbohydr Res 263(2):257–269. https://doi.org/10.1016/0008-6215(94)00177-4
doi: 10.1016/0008-6215(94)00177-4
Rasmussen R (2001) Quantification on the LightCycler. In: Meuer S, Wittwer C, Nakagawara K (eds). Springer, Berlin, Heidelberg, pp 21–34
Ravalason H, Grisel S, Chevret D, Favel A, Berrin JG, Sigoillot JC, Herpoël-Gimbert I (2012) Fusarium verticillioides secretome as a source of auxiliary enzymes to enhance saccharification of wheat straw. Bioresour Technol 114:589–596. https://doi.org/10.1016/j.biortech.2012.03.009
doi: 10.1016/j.biortech.2012.03.009
Record E, Asther M, Sigoillot C, Pagès S, Punt PJ, Delattre M, Haon M, Van Den Hondel CAMJJ, Sigoillot JC, Lesage-Meessen L, Asther M (2003) Overproduction of the Aspergillus niger feruloyl esterase for pulp bleaching application. Appl Microbiol Biotechnol 62(4):349–355. https://doi.org/10.1007/s00253-003-1325-4
doi: 10.1007/s00253-003-1325-4
Rozen S, Skaletsky H (2000) Primer3 on the WWW for general users and for biologist programmers. Methods in Molecular Biology (clifton, NJ) 132:365–386
Sakamoto T, Nishimura S, Kato T, Sunagawa Y, Tsuchiyama M, Kawasaki H (2005) Efficient extraction of ferulic acid from sugar beet pulp using the culture supernatant of Penicillium chrysogenum. J of Appl Glycosci 52(2):115–120. https://doi.org/10.5458/jag.52.115
doi: 10.5458/jag.52.115
Schneider WDH, Goncalves TA, Uchima CA, Couger MB, Prade R, Squina FM, Dillon AJP, Camassola M (2016) Penicillium echinulatum secretome analysis reveals the fungi potential for degradation of lignocellulosic biomass. Biotechnol Biofuels 9:66. https://doi.org/10.1186/s13068-016-0476-3
doi: 10.1186/s13068-016-0476-3
Sewalt V, Shanahan D, Gregg L, La Marta J, Carrillo R (2016) The generally recognized as safe (GRAS) process for industrial microbial enzymes. Ind Biotechnol 12(5):295–302. https://doi.org/10.1089/ind.2016.0011
doi: 10.1089/ind.2016.0011
Song W, Han X, Qian Y, Liu G, Yao G, Zhong Y, Qu Y (2016) Proteomic analysis of the biomass hydrolytic potentials of Penicillium oxalicum lignocellulolytic enzyme system. Biotechnol Biofuels 9(1):68–68. https://doi.org/10.1186/s13068-016-0477-2
doi: 10.1186/s13068-016-0477-2
de Souza WR (2013) Microbial degradation of lignocellulosic biomass. In: Chandel A, da Silvia SS (eds). InTech, Rijeka, Croacia, pp 135–152
Stajich JE, Berbee ML, Blackwell M, Hibbett DS, James TY, Spatafora JW, Taylor JW (2009) The Fungi. Curr Biol 19(18):R840–R845. https://doi.org/10.1016/j.cub.2009.07.004
doi: 10.1016/j.cub.2009.07.004
Taofiq O, González-Paramás A, Barreiro M, Ferreira I (2017) Hydroxycinnamic acids and their derivatives: cosmeceutical significance, challenges and future perspectives, a review. Molecules 22:281–281. https://doi.org/10.3390/molecules22020281
doi: 10.3390/molecules22020281
Tatusov RL, Fedorova ND, Jackson JD, Jacobs AR, Kiryutin B, Koonin EV, Krylov DM, Mazumder R, Mekhedov SL, Nikolskaya AN, Rao BS, Smirnov S, Sverdlov AV, Vasudevan S, Wolf YI, Yin JJ, Natale DA (2003) The COG database: an updated version includes eukaryotes. BMC Bioinformatics 4(1):41–41. https://doi.org/10.1186/1471-2105-4-41
doi: 10.1186/1471-2105-4-41
Terfehr D, Dahlmann TA, Kück U (2017) Transcriptome analysis of the two unrelated fungal β-lactam producers Acremonium chrysogenum and Penicillium chrysogenum: Velvet-regulated genes are major targets during conventional strain improvement programs. BMC Genomics 18(1):272–272. https://doi.org/10.1186/s12864-017-3663-0
doi: 10.1186/s12864-017-3663-0
Terrasan CRF, Guisan JM, Carmona EC (2016) Xylanase and β-xylosidase from Penicillium janczewskii: Purification, characterization and hydrolysis of substrates. Electron J Biotechnol 23:54–62. https://doi.org/10.1016/j.ejbt.2016.08.001
doi: 10.1016/j.ejbt.2016.08.001
Thom C (1910) Cultural studies of species of Penicillium. Bullet Bureau Animal Industry, USDA 118:1–109
Tola M, Kebede B (2016) Occurrence, importance and control of mycotoxins: a review. Cogent food agric 2(1):1–12. https://doi.org/10.1080/23311932.2016.1191103
doi: 10.1080/23311932.2016.1191103
Topakas E, Vafiadi C, Christakopoulos P (2007) Microbial production, characterization and applications of feruloyl esterases. Process Biochem 42:497–509. https://doi.org/10.1016/j.procbio.2007.01.007
doi: 10.1016/j.procbio.2007.01.007
Tripathi N, Hills CD, Singh RS, Atkinson CJ (2019) Biomass waste utilisation in low-carbon products: harnessing a major potential resource. npj Climate and Atmospheric Science 2(1) https://doi.org/10.1038/s41612-019-0093-5
Udatha DBRKG, Kouskoumvekaki I, Olsson L, Panagiotou G (2011) The interplay of descriptor-based computational analysis with pharmacophore modeling builds the basis for a novel classification scheme for feruloyl esterases. Biotechnol Adv 29(1):94–110. https://doi.org/10.1016/j.biotechadv.2010.09.003
doi: 10.1016/j.biotechadv.2010.09.003
Udatha DBRKG, Mapelli V, Panagiotou G, Olsson L (2012) Common and distant structural characteristics of feruloyl esterase families from Aspergillus oryzae. PLoS ONE 7(6):e39473–e39473. https://doi.org/10.1371/journal.pone.0039473
doi: 10.1371/journal.pone.0039473
Ullán RV, Campoy S, Casqueiro J, Fernández FJ, Martín JF (2007) Deacetylcephalosporin C production in Penicillium chrysogenum by expression of the isopenicillin N epimerization, ring expansion, and acetylation genes. Chem Biol 14:329–339. https://doi.org/10.1016/j.chembiol.2007.01.012
doi: 10.1016/j.chembiol.2007.01.012
van den Brink J, de Vries RP (2011) Fungal enzyme sets for plant polysaccharide degradation. Appl Microbiol Biotechnol 91(6):1477–1492. https://doi.org/10.1007/s00253-011-3473-2
doi: 10.1007/s00253-011-3473-2
van den Berg MA, Albang R, Albermann K, Badger JH, Daran JM, Driessen MAJ, Garcia-Estrada C, Fedorova ND, Harris DM, Heijne WHM, Joardar V, Kiel WJAK, Kovalchuk A, Martín JF, Nierman WC, Nijland JG, Pronk JT, Roubos JA, van der Klei IJ, van Peij NNME, Veenhuis M, Döhren H, Wagner C, Wortman J, Bovenberg RAL (2008) Genome sequencing and analysis of the filamentous fungus Penicillium chrysogenum. Nat Biotechnol 26(10):1161–1168. https://doi.org/10.1038/nbt.1498
doi: 10.1038/nbt.1498
van Egmond HP, Schothorst RC, Jonker MA (2007) Regulations relating to mycotoxins in food. Anal Bioanal Chem 389(1):147–157. https://doi.org/10.1007/s00216-007-1317-9
doi: 10.1007/s00216-007-1317-9
Vasco-Cárdenas MF, Baños S, Ramos A, Martín JF, Barreiro C (2013) Proteome response of Corynebacterium glutamicum to high concentration of industrially relevant C4 and C5 dicarboxylic acids. J Proteomics 85:65–88. https://doi.org/10.1016/j.jprot.2013.04.019
doi: 10.1016/j.jprot.2013.04.019
Ventola CL (2015) The antibiotic resistance crisis: part 1: causes and threats. P & T : a Peer-Reviewed Journal for Formulary Management 40(4):277–283
Vila-Donat P, Marín S, Sanchis V, Ramos AJ (2018) A review of the mycotoxin adsorbing agents, with an emphasis on their multi-binding capacity, for animal feed decontamination. Food Chem Toxicol 114:246–259. https://doi.org/10.1016/j.fct.2018.02.044
doi: 10.1016/j.fct.2018.02.044
Visagie CM, Houbraken J, Frisvad JC, Hong SB, Klaassen CHW, Perrone G, Seifert KA, Varga J, Yaguchi T, Samson RA (2014) Identification and nomenclature of the genus Penicillium. Stud Mycol 78(1):343–371. https://doi.org/10.1016/j.simyco.2014.09.001
doi: 10.1016/j.simyco.2014.09.001
Wagacha JM, Muthomi JW (2008) Mycotoxin problem in Africa: current status, implications to food safety and health and possible management strategies. Int J Food Microbiol 124(1):1–12. https://doi.org/10.1016/j.ijfoodmicro.2008.01.008
doi: 10.1016/j.ijfoodmicro.2008.01.008
Wang L, Li Z, Zhu M, Meng L, Wang H, Ng TB (2016a) An acidic feruloyl esterase from the mushroom Lactarius hatsudake: a potential animal feed supplement. Int J Biol Macromol 93:290–295. https://doi.org/10.1016/j.ijbiomac.2016.08.028
doi: 10.1016/j.ijbiomac.2016.08.028
Wang M, Carver JJ, Phelan VV, Sanchez LM, Garg N, Peng Y, Nguyen DD, Watrous J, Kapono CA, Luzzatto-Knaan T, Porto C, Bouslimani A, Melnik AV, Meehan MJ, Liu WT, Crüsemann M, Boudreau PD, Esquenazi E, Sandoval-Calderón M, Kersten RD, Pace LA, Quinn RA, Duncan KR, Hsu CC, Floros DJ, Gavilan RG, Kleigrewe K, Northen T, Dutton RJ, Parrot D, Carlson EE, Aigle B, Michelsen CF, Jelsbak L, Sohlenkamp C, Pevzner P, Edlund A, McLean J, Piel J, Murphy BT, Gerwick L, Liaw CC, Yang YL, Humpf HU, Maansson M, Keyzers RA, Sims AC, Johnson AR, Sidebottom AM, Sedio BE, Klitgaard A, Larson CB, Boya CAP, Torres-Mendoza D, Gonzalez DJ, Silva DB, Marques LM, Demarque DP, Pociute E, O’Neill EC, Briand E, Helfrich EJN, Granatosky EA, Glukhov E, Ryffel F, Houson H, Mohimani H, Kharbush JJ, Zeng Y, Vorholt JA, Kurita KL, Charusanti P, McPhail KL, Nielsen KF, Vuong L, Elfeki M, Traxler MF, Engene N, Koyama N, Vining OB, Baric R, Silva RR, Mascuch SJ, Tomasi S, Jenkins S, Macherla V, Hoffman T, Agarwal V, Williams PG, Dai J, Neupane R, Gurr J, Rodríguez AMC, Lamsa A, Zhang C, Dorrestein K, Duggan BM, Almaliti J, Allard PM, Phapale P, Nothias LF, Alexandrov T, Litaudon M, Wolfender JL, Kyle JE, Metz TO, Peryea T, Nguyen DT, VanLeer D, Shinn P, Jadhav A, Müller R, Waters KM, Shi W, Liu X, Zhang L, Knight R, Jensen PR, Palsson B, Pogliano K, Linington RG, Gutiérrez M, Lopes NP, Gerwick WH, Moore BS, Dorrestein PC, Bandeira N (2016b) Sharing and community curation of mass spectrometry data with Global Natural Products Social Molecular Networking. Nat Biotechnol 34(8):828–837. https://doi.org/10.1038/nbt.3597
doi: 10.1038/nbt.3597
Ward OP (2012) Production of recombinant proteins by filamentous fungi. Biotechnol Adv 30(5):1119–1139. https://doi.org/10.1016/j.biotechadv.2011.09.012
doi: 10.1016/j.biotechadv.2011.09.012
Wei H, Xu Q, Taylor LE, Baker JO, Tucker MP, Ding S-Y (2009) Natural paradigms of plant cell wall degradation. Curr Opin Biotechnol 20(3):330–338. https://doi.org/10.1016/j.copbio.2009.05.008
doi: 10.1016/j.copbio.2009.05.008
Wingfield P (1998) Protein precipitation using ammonium sulfate. John Wiley & Sons, Inc., Hoboken, New Jersey, United States, pp A.3F.1-A.3F.8
Xiao Z, Storms R, Tsang A (2005) Microplate-based carboxymethylcellulose assay for endoglucanase activity. Anal Biochem 342(1):176–178. https://doi.org/10.1016/j.ab.2005.01.052
doi: 10.1016/j.ab.2005.01.052
Zhang SB, Zhai HC, Wang L, Yu GH (2013) Expression, purification and characterization of a feruloyl esterase A from Aspergillus flavus. Protein Expression Purif 92(1):36–40. https://doi.org/10.1016/j.pep.2013.08.009
doi: 10.1016/j.pep.2013.08.009
Zhao W, Li C, Liang J, Sun S (2014) The Aspergillus fumigatus β -1,3-glucanosyltransferase Gel7 plays a compensatory role in maintaining cell wall integrity under stress conditions. Glycobiology 24(5):418–427. https://doi.org/10.1093/glycob/cwu003
doi: 10.1093/glycob/cwu003
Zhu Z-J, Schultz AW, Wang J, Johnson CH, Yannone SM, Patti GJ, Siuzdak G (2013) Liquid chromatography quadrupole time-of-flight mass spectrometry characterization of metabolites guided by the METLIN database. Nat Protoc 8(3):451–460. https://doi.org/10.1038/nprot.2013.004
doi: 10.1038/nprot.2013.004
Zuin VG, Ramin LZ (2018) Green and sustainable separation of natural products from agro-industrial waste: challenges, potentialities, and perspectives on emerging approaches. Top Curr Chem 376(1):3–3. https://doi.org/10.1007/s41061-017-0182-z
doi: 10.1007/s41061-017-0182-z
Zwane EN, Rose SH, van Zyl WH, Rumbold K, Viljoen-Bloom M (2014) Overexpression of Aspergillus tubingensis faeA in protease-deficient Aspergillus niger enables ferulic acid production from plant material. J Ind Microbiol Biotechnol 41(6):1027–1034. https://doi.org/10.1007/s10295-014-1430-7
doi: 10.1007/s10295-014-1430-7