Lignocellulolytic extremozymes and their biotechnological applications.
Cellulolytic
Extremophiles
Extremozymes
Ligninolytic
Journal
Extremophiles : life under extreme conditions
ISSN: 1433-4909
Titre abrégé: Extremophiles
Pays: Germany
ID NLM: 9706854
Informations de publication
Date de publication:
11 Nov 2023
11 Nov 2023
Historique:
received:
02
01
2023
accepted:
26
09
2023
medline:
13
11
2023
pubmed:
11
11
2023
entrez:
11
11
2023
Statut:
epublish
Résumé
Lignocellulolytic enzymes are used in different industrial and environmental processes. The rigorous operating circumstances of these industries, however, might prevent these enzymes from performing as intended. On the other side, extremozymes are enzymes produced by extremophiles that can function in extremely acidic or basic; hot or cold; under high or low salinity conditions. These severe conditions might denature the normal enzymes that are produced by mesophilic microorganisms. The increased stability of these enzymes has been contributed to a number of conformational modifications in their structures. These modifications may result from a few amino acid substitutions, an improved hydrophobic core, the existence of extra ion pairs and salt bridges, an increase in compactness, or an increase in positively charged amino acids. These enzymes are the best option for industrial and bioremediation activities that must be carried out under difficult conditions due to their improved stability. The review, therefore, discusses lignocellulolytic extremozymes, their structure and mechanisms along with industrial and biotechnological applications.
Identifiants
pubmed: 37950773
doi: 10.1007/s00792-023-01314-2
pii: 10.1007/s00792-023-01314-2
doi:
Substances chimiques
Acids
0
Amino Acids
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
2Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer Nature Japan KK, part of Springer Nature.
Références
Abdulmajeed Abdulmajeed AT, Şahin S, Ozmen I (2022) Production and purification of the endoglucanase enzyme from local isolate aspergillus fumigatus HBF356. Biointerface Res Appl Chem 12:4337–4347. https://doi.org/10.33263/BRIAC124.43374347
doi: 10.33263/BRIAC124.43374347
Ahmad Q, Manzoor M, Chaudhary A et al (2021) Bench-scale fermentation for second generation ethanol and hydrogen production by <scp> Clostridium thermocellum DSMZ <scp> 1313 from sugarcane bagasse. Environ Prog Sustain Energy. https://doi.org/10.1002/ep.13516
doi: 10.1002/ep.13516
Ahmed A, Nasim F, Batool K, Bibi A (2017) Microbial β-glucosidase : sources. Prod Appl 5:31–46. https://doi.org/10.12691/jaem-5-1-4
doi: 10.12691/jaem-5-1-4
Akanuma S, Bessho M, Kimura H et al (2019) Establishment of mesophilic-like catalytic properties in a thermophilic enzyme without affecting its thermal stability. Sci Rep 9:9346. https://doi.org/10.1038/s41598-019-45560-x
doi: 10.1038/s41598-019-45560-x
pubmed: 31249343
pmcid: 6597716
Arora NK, Panosyan H (2019) Extremophiles: applications and roles in environmental sustainability. Environ Sustain 2:217–218. https://doi.org/10.1007/s42398-019-00082-0
doi: 10.1007/s42398-019-00082-0
Aryan AP, Wilson B, Strauss CR, Williams PJ (1987) The properties of glycosidases of & ltem>Vitis vinifera<em> and a comparison of Their β-glucosidase activity with that of exogenous enzymes an assessment of possible applications in enology. Am J Enol Vitic 38(182):188
Atalah J, Zhou Y, Espina G et al (2018) Improved stability of multicopper oxidase–carbon nanotube conjugates using a thermophilic laccase. Catal Sci Technol 8:1272–1276. https://doi.org/10.1039/C8CY00072G
doi: 10.1039/C8CY00072G
Bano A, Chen X, Prasongsuk S et al (2019) Purification and characterization of cellulase from obligate halophilic Aspergillus flavus (TISTR 3637) and Its prospects for bioethanol production. Appl Biochem Biotechnol 189:1327–1337. https://doi.org/10.1007/s12010-019-03086-y
doi: 10.1007/s12010-019-03086-y
pubmed: 31297753
Bettache A, Copinet E, Azzouz Z et al (2020) Purification and characterization of an endoglucanase produced from Streptomyces sp. Strainbpng23. J Microbiol Biotechnol Food Sci 10:284–288. https://doi.org/10.15414/jmbfs.2020.10.2.284-288
doi: 10.15414/jmbfs.2020.10.2.284-288
Bibra M, Kunreddy V, Sani R (2018) Thermostable Xylanase Production by Geobacillus sp. strain DUSELR13, and its application in ethanol production with lignocellulosic biomass. Microorganisms 6:93. https://doi.org/10.3390/microorganisms6030093
doi: 10.3390/microorganisms6030093
pubmed: 30189618
pmcid: 6164562
Biko ODV, Viljoen-Bloom M, van Zyl WH (2020) Microbial lignin peroxidases: applications, production challenges and future perspectives. Enzyme Microb Technol 141:109669
doi: 10.1016/j.enzmictec.2020.109669
pubmed: 33051019
Brunecky R, Alahuhta M, Xu Q et al (2013) Revealing nature’s cellulase diversity: the digestion mechanism of caldicellulosiruptor bescii CelA. Science 342:1513–1516. https://doi.org/10.1126/science.1244273
doi: 10.1126/science.1244273
pubmed: 24357319
Bueno-Nieto C, Cortés-Antiquera R, Espina G et al (2023) Biochemical and spectroscopic characterization of a recombinant laccase from thermoalkaliphilic Bacillus sp. FNT with potential for degradation of polycyclic aromatic hydrocarbons (PAHs). Catalysts 13:763. https://doi.org/10.3390/catal13040763
doi: 10.3390/catal13040763
Cabrera MÁ, Blamey JM (2018) Biotechnological applications of archaeal enzymes from extreme environments. Biol Res 51:1–15
doi: 10.1186/s40659-018-0186-3
Cai L-N, Lu T, Lin D-Q, Yao S-J (2022) Discovery of extremophilic cellobiohydrolases from marine Aspergillus niger with computational analysis. Process Biochem 115:118–127. https://doi.org/10.1016/j.procbio.2022.02.016
doi: 10.1016/j.procbio.2022.02.016
Chandra R, Kumar V, Yadav S (2017) Extremophilic ligninolytic enzymes. In: Sani RK, Krishnaraj RN (eds) Extremophilic enzymatic processing of lignocellulosic feedstocks to bioenergy. Springer International Publishing, Cham, pp 115–154
doi: 10.1007/978-3-319-54684-1_8
Chang Y, Yang D, Li R et al (2021) Textile dye biodecolorization by manganese peroxidase: a review. Molecules 26:1–15
doi: 10.3390/molecules26154403
Chaturvedi S, Sarethy IP (2022) Major habitats and diversity of thermophilic fungi Bt—extremophilic fungi: ecology physiology and applications. Springer Nature Singapore, Singapore, pp 55–75
doi: 10.1007/978-981-16-4907-3_3
Chefetz B, Chen Y, Hadar Y (1998) Purification and characterization of laccase from Chaetomium thermophilium and its role in humification. Appl Environ Microbiol 64:3175–3179. https://doi.org/10.1128/aem.64.9.3175-3179.1998
doi: 10.1128/aem.64.9.3175-3179.1998
pubmed: 9726856
pmcid: 106706
Chowdhary P, Hare V, Mani S et al (2020) Recent advancement in the biotechnological application of lignin peroxidase and its future prospects. In: Chowdhary P, Raj A, Verma D, Akhter Y (eds) Microorganisms for sustainable environment and health. Elsevier, Amsterdam, pp 1–16
Chukwuma OB, Rafatullah M, Tajarudin HA, Ismail N (2020) Lignocellulolytic enzymes in biotechnological and industrial processes: a review. Sustain 12:1–31. https://doi.org/10.3390/su12187282
doi: 10.3390/su12187282
Cong B, Wang N, Liu S et al (2017) Isolation, characterization and transcriptome analysis of a novel Antarctic Aspergillus sydowii strain MS-19 as a potential lignocellulosic enzyme source. BMC Microbiol 17:1–14. https://doi.org/10.1186/s12866-017-1028-0
doi: 10.1186/s12866-017-1028-0
da Martins ES, da Gomes E, Silva R, Junior RB (2019) Production of cellulases by Thermomucor indicae-seudaticae: characterization of a thermophilic β-glucosidase. Prep Biochem Biotechnol 49:830–836. https://doi.org/10.1080/10826068.2019.1625060
doi: 10.1080/10826068.2019.1625060
pubmed: 31274051
Dar FM, Dar PM (2021) Fungal xylanases for different industrial applications. In: Abdel-Azeem AM, Yadav AN, Yadav N, Sharma M (eds) BT—industrially important fungi for sustainable development: bioprospecting for biomolecules, vol 2. Springer International Publishing, Cham, pp 515–539
doi: 10.1007/978-3-030-85603-8_14
Delgado L, Parker M, Fisk I, Paradisi F (2020) Performance of the extremophilic enzyme BglA in the hydrolysis of two aroma glucosides in a range of model and real wines and juices. Food Chem 323:126825. https://doi.org/10.1016/j.foodchem.2020.126825
doi: 10.1016/j.foodchem.2020.126825
pubmed: 32335459
Della Torre CL, Silva-Lucca RA, da Ferreira RS et al (2021) Correlation of the conformational structure and catalytic activity of the highly thermostable xylanase of thermomyces lanuginosus PC7S1T. Biocatal Biotransformation. https://doi.org/10.1080/10242422.2021.1950696
doi: 10.1080/10242422.2021.1950696
Dong M, Yang Y, Tang X et al (2016) NaCl-, protease-tolerant and cold-active endoglucanase from Paenibacillus sp. YD236 isolated from the feces of Bos frontalis. Springerplus 5:746. https://doi.org/10.1186/s40064-016-2360-9
doi: 10.1186/s40064-016-2360-9
pubmed: 27376014
pmcid: 4909688
Dutta T, Sahoo R, Sengupta R et al (2008) Novel cellulases from an extremophilic filamentous fungi Penicillium citrinum: production and characterization. J Ind Microbiol Biotechnol 35:275–282. https://doi.org/10.1007/s10295-008-0304-2
doi: 10.1007/s10295-008-0304-2
pubmed: 18210175
Ejaz U, Sohail M, Ghanemi A (2021) Cellulases: from bioactivity to a variety of industrial applications. Biomimetics 6:44
doi: 10.3390/biomimetics6030044
pubmed: 34287227
pmcid: 8293267
Elleuche S, Schröder C, Sahm K, Antranikian G (2014) Extremozymes—biocatalysts with unique properties from extremophilic microorganisms. Curr Opin Biotechnol 29:116–123. https://doi.org/10.1016/j.copbio.2014.04.003
doi: 10.1016/j.copbio.2014.04.003
pubmed: 24780224
Fan MZ, Wang W, Cheng L et al (2021) Metagenomic discovery and characterization of multi-functional and monomodular processive endoglucanases as biocatalysts. Appl Sci 11:5150
doi: 10.3390/app11115150
Fusco FA, Fiorentino G, Pedone E et al (2018a) Biochemical characterization of a novel thermostable β-glucosidase from dictyoglomus turgidum. Int J Biol Macromol 113:783–791. https://doi.org/10.1016/j.ijbiomac.2018.03.018
doi: 10.1016/j.ijbiomac.2018.03.018
pubmed: 29518444
Fusco FA, Ronca R, Fiorentino G et al (2018b) Biochemical characterization of a thermostable endomannanase/endoglucanase from dictyoglomus turgidum. Extremophiles 22:131–140. https://doi.org/10.1007/s00792-017-0983-6
doi: 10.1007/s00792-017-0983-6
pubmed: 29177717
Garbin AP, Garcia NFL, Cavalheiro GF et al (2021) β-glucosidase from thermophilic fungus Thermoascus crustaceus: production and industrial potential. An Acad Bras Ciênc 93:1–11. https://doi.org/10.1590/0001-3765202120191349
doi: 10.1590/0001-3765202120191349
Godse R, Bawane H, Tripathi J, Kulkarni R (2021) Unconventional β-glucosidases: a promising biocatalyst for industrial biotechnology. Appl Biochem Biotechnol 193:2993–3016. https://doi.org/10.1007/s12010-021-03568-y
doi: 10.1007/s12010-021-03568-y
pubmed: 33871765
Gomathy S, Sridharan R, Kumar PS et al (2021) Application of alkaline MnP immobilized Luffa fibers in mixed azo dyes degradation. Environ Technol Innov 24:101964. https://doi.org/10.1016/j.eti.2021.101964
doi: 10.1016/j.eti.2021.101964
Gomes E, Aguiar AP, Carvalho CC et al (2009) Ligninases production by basidiomycetes strains on lignocellulosic agricultural residues and their application in the decolorization of synthetic dyes. Brazilian J Microbiol 40:31–39. https://doi.org/10.1590/S1517-83822009000100005
doi: 10.1590/S1517-83822009000100005
Hait S, Mallik S, Basu S, Kundu S (2020) Finding the generalized molecular principles of protein thermal stability. Proteins Struct Funct Bioinforma 88:788–808. https://doi.org/10.1002/prot.25866
doi: 10.1002/prot.25866
Han C, Yang R, Sun Y et al (2020) Identification and characterization of a novel hyperthermostable bifunctional cellobiohydrolase- Xylanase enzyme for synergistic effect with commercial cellulase on pretreated wheat straw degradation. Front Bioeng Biotechnol 8:1–13. https://doi.org/10.3389/fbioe.2020.00296
doi: 10.3389/fbioe.2020.00296
Hildén K, Mäkelä MR (2018) Role of fungi in wood decay reference module in life sciences. Amsterdam, Elsevier
Huang C, Feng Y, Patel G et al (2021) Production, immobilization and characterization of beta-glucosidase for application in cellulose degradation from a novel Aspergillus versicolor. Int J Biol Macromol 177:437–446. https://doi.org/10.1016/j.ijbiomac.2021.02.154
doi: 10.1016/j.ijbiomac.2021.02.154
pubmed: 33636259
Jin M, Gai Y, Guo X et al (2019) Properties and applications of extremozymes from deep-sea extremophilic microorganisms: a mini review. Mar Drugs. https://doi.org/10.3390/md17120656
doi: 10.3390/md17120656
pubmed: 31888163
pmcid: 6950534
Jönsson LJ, Alriksson B, Nilvebrant N-O (2013) Bioconversion of lignocellulose: inhibitors and detoxification. Biotechnol Biofuels 6:1–10
doi: 10.1186/1754-6834-6-16
Kalsoom U, Ahsan Z, Bhatti HN et al (2022) Iron oxide nanoparticles immobilized Aspergillus flavus manganese peroxidase with improved biocatalytic, kinetic, thermodynamic, and dye degradation potentialities. Process Biochem 117:117–133. https://doi.org/10.1016/j.procbio.2022.04.002
doi: 10.1016/j.procbio.2022.04.002
Khalili Ghadikolaei K, Gharechahi J, Haghbeen K et al (2018) A cold-adapted endoglucanase from camel rumen with high catalytic activity at moderate and low temperatures: an anomaly of truly cold-adapted evolution in a mesophilic environment. Extremophiles 22:315–326. https://doi.org/10.1007/s00792-018-0999-6
doi: 10.1007/s00792-018-0999-6
pubmed: 29330650
Kuhad RC, Gupta R, Singh A (2011) Microbial cellulases and their industrial applications. Enzyme Res 2011:280696
doi: 10.4061/2011/280696
pubmed: 21912738
pmcid: 3168787
Kumar A, Arora PK (2022) Biotechnological applications of manganese peroxidases for sustainable management. Front Environ Sci 10:1–11. https://doi.org/10.3389/fenvs.2022.875157
doi: 10.3389/fenvs.2022.875157
Kumar A, Chandra R (2020) Ligninolytic enzymes and its mechanisms for degradation of lignocellulosic waste in environment. Heliyon 6:e03170. https://doi.org/10.1016/j.heliyon.2020.e03170
doi: 10.1016/j.heliyon.2020.e03170
pubmed: 32095645
pmcid: 7033530
Kuntothom T, Cairns JK (2020) Expression and characterization of TbCel12A, a thermophilic endoglucanase with potential in biomass hydrolysis. Biocatal Agric Biotechnol 30:101835. https://doi.org/10.1016/j.bcab.2020.101835
doi: 10.1016/j.bcab.2020.101835
Li DC, Li AN, Papageorgiou AC (2011) Cellulases from thermophilic fungi: recent insights and biotechnological potential. Enzyme Res 2011:308730
doi: 10.4061/2011/308730
pubmed: 22145076
pmcid: 3226318
Liu Y, Luo G, Ngo HH et al (2020) Advances in thermostable laccase and its current application in lignin-first biorefinery: a review. Bioresour Technol 298:122511
doi: 10.1016/j.biortech.2019.122511
pubmed: 31839492
Liu E, Segato F, Wilkins MR (2021) Fed-batch production of thermothelomyces thermophilus lignin peroxidase using a recombinant Aspergillus nidulans strain in stirred-tank bioreactor. Bioresour Technol 325:124700. https://doi.org/10.1016/j.biortech.2021.124700
doi: 10.1016/j.biortech.2021.124700
pubmed: 33461124
López-López A, Santiago-Hernández A, Cayetano-Cruz M et al (2023) TtCel7A: a native thermophilic bifunctional cellulose/Xylanase exogluclanase from the thermophilic biomass-degrading fungus thielavia terrestris Co3Bag1, and Its application in enzymatic hydrolysis of agroindustrial derivatives. J Fungi 9:152. https://doi.org/10.3390/jof9020152
doi: 10.3390/jof9020152
Machmudah S, Wahyudiono KH, Goto M (2017) Hydrolysis of biopolymers in near-critical and subcritical water. In: Wahyudiono HK, Goto M, Machmudah S (eds) Water extraction of bioactive compounds from plants to drug development. Elsevier, Amsterdam, pp 69–107
doi: 10.1016/B978-0-12-809380-1.00003-6
Malgas S, Thoresen M, van Dyk JS, Pletschke BI (2017) Time dependence of enzyme synergism during the degradation of model and natural lignocellulosic substrates. Enzyme Microb Technol 103:1–11
doi: 10.1016/j.enzmictec.2017.04.007
pubmed: 28554379
Mandeep LH, Shukla P (2021) Synthetic biology and biocomputational approaches for improving microbial endoglucanases toward their innovative applications. ACS Omega 6:6055–6063
doi: 10.1021/acsomega.0c05744
pubmed: 33718696
pmcid: 7948214
Masingi NN (2020) Production and characteristics of a b-glucosidase from a thermophilic bacterium and investigation of its potential as part of a cellulase cocktail for conversion of lignocellulosic biomass to fermentable sugars. University of Limpopo, Polokwane
Mohsin I, Poudel N, Li DC, Papageorgiou AC (2019) Crystal structure of a GH3 β-glucosidase from the thermophilic fungus Chaetomium thermophilum. Int J Mol Sci. https://doi.org/10.3390/ijms20235962
doi: 10.3390/ijms20235962
pubmed: 31783503
pmcid: 6929035
Mollania N, Khajeh K, Ranjbar B, Hosseinkhani S (2011) Enhancement of a bacterial laccase thermostability through directed mutagenesis of a surface loop. Enzyme Microb Technol 49:446–452. https://doi.org/10.1016/j.enzmictec.2011.08.001
doi: 10.1016/j.enzmictec.2011.08.001
pubmed: 22112616
Nhim S, Waeonukul R, Uke A et al (2022) Biological cellulose saccharification using a coculture of Clostridium thermocellum and thermobrachium celere strain A9. Appl Microbiol Biotechnol 106:2133–2145. https://doi.org/10.1007/s00253-022-11818-0
doi: 10.1007/s00253-022-11818-0
pubmed: 35157106
pmcid: 8930880
Niladevi KN (2009) Ligninolytic enzymes. In: Singh nee’ Nigam P, Pandey A (eds) Biotechnology for agro-industrial residues utilisation utilisation of Agro-residues. Springer, Netherlands, Dordrecht, pp 397–414
doi: 10.1007/978-1-4020-9942-7_22
Panwar V, Sheikh JN, Dutta T (2020) Sustainable denim bleaching by a novel thermostable Bacterial laccase. Appl Biochem Biotechnol 192:1238–1254. https://doi.org/10.1007/s12010-020-03390-y
doi: 10.1007/s12010-020-03390-y
pubmed: 32715414
Plácido J, Capareda S (2015) Ligninolytic enzymes: a biotechnological alternative for bioethanol production. Bioresour Bioprocess 2:1–12
doi: 10.1186/s40643-015-0049-5
Ratuchne A, Knob A (2021) A new and unusual β-glucosidase from Aspergillus fumigatus: Catalytic activity at high temperatures and glucose tolerance. Biocatal Agric Biotechnol. https://doi.org/10.1016/j.bcab.2021.102064
doi: 10.1016/j.bcab.2021.102064
Rehman MF, ur, Shaeer A, Batool AI, Aslam M, (2022) Chapter 2—Structure-function relationship of extremozymes. Academic Press, Cambridge, pp 9–30
Rekik H, Zaraî Jaouadi N, Bouacem K et al (2019) Physical and enzymatic properties of a new manganese peroxidase from the white-rot fungus trametes pubescens strain i8 for lignin biodegradation and textile-dyes biodecolorization. Int J Biol Macromol 125:514–525. https://doi.org/10.1016/j.ijbiomac.2018.12.053
doi: 10.1016/j.ijbiomac.2018.12.053
pubmed: 30528991
Saleem A, Waris S, Ahmed T, Tabassum R (2021) Biochemical characterization and molecular docking of cloned xylanase gene from Bacillus subtilis RTS expressed in E. coli. Int J Biol Macromol 168:310–321. https://doi.org/10.1016/j.ijbiomac.2020.12.001
doi: 10.1016/j.ijbiomac.2020.12.001
pubmed: 33309670
Sharma V, Ayothiraman S, Dhakshinamoorthy V (2019) Production of highly thermo-tolerant laccase from novel thermophilic bacterium Bacillus sp. PC-3 and its application in functionalization of chitosan film. J Biosci Bioeng 127:672–678. https://doi.org/10.1016/j.jbiosc.2018.11.008
doi: 10.1016/j.jbiosc.2018.11.008
pubmed: 30573384
Sharma V, Pugazhenthi G, Vasanth D (2022) Production and characterization of a novel thermostable laccase from Bacillus licheniformis VNQ and its application in synthesis of bioactive 1,4-naphthoquinones. J Biosci Bioeng 133:8–16. https://doi.org/10.1016/j.jbiosc.2021.09.008
doi: 10.1016/j.jbiosc.2021.09.008
pubmed: 34629297
Sharma S, Tsai M-L, Sharma V et al (2023) Environment friendly pretreatment approaches for the bioconversion of lignocellulosic biomass into biofuels and value-added products. Environments 10:6. https://doi.org/10.3390/environments10010006
doi: 10.3390/environments10010006
Singh G, Vinod AKV (2016) Catalytic properties, functional attributes and industrial applications of β-glucosidases. 3 Biotech 6:1–14. https://doi.org/10.1007/s13205-015-0328-z
doi: 10.1007/s13205-015-0328-z
pubmed: 28330071
Singh G, Verma AK, Kumar V (2016) Catalytic properties, functional attributes and industrial applications of β-glucosidases. 3 Biotech 6:1–14. https://doi.org/10.1007/s13205-015-0328-z
doi: 10.1007/s13205-015-0328-z
pubmed: 28330071
Singh A, Čížková M, Náhlík V et al (2023) Bio-removal of rare earth elements from hazardous industrial waste of CFL bulbs by the extremophile red alga Galdieria sulphuraria. Front Microbiol. https://doi.org/10.3389/fmicb.2023.1130848
doi: 10.3389/fmicb.2023.1130848
pubmed: 37901824
pmcid: 10570616
Sivasankar P, Poongodi S, Sivakumar K et al (2022) Exogenous production of cold-active cellulase from polar Nocardiopsis sp. with increased cellulose hydrolysis efficiency. Arch Microbiol 204:218. https://doi.org/10.1007/s00203-022-02830-z
doi: 10.1007/s00203-022-02830-z
pubmed: 35333982
Souii A, Ghorrab A, Hammami K et al (2022) Extremozyme-Based Technology for Biofuel Generation. In: Gupta VK, Sarker SD, Sharma M, Pirovani ME, Usmani Z, Jayabaskaran C (eds) Biomol from nat sources. Wiley, Hoboken, pp 214–251
doi: 10.1002/9781119769620.ch7
Suleiman M, Schröder C, Klippel B et al (2019) Extremely thermoactive archaeal endoglucanase from a shallow marine hydrothermal vent from Vulcano Island. Appl Microbiol Biotechnol 103:1267–1274. https://doi.org/10.1007/s00253-018-9542-z
doi: 10.1007/s00253-018-9542-z
pubmed: 30547216
Sundaramoorthy M, Youngs HL, Gold MH, Poulos TL (2005) High-resolution crystal structure of manganese peroxidase: substrate and inhibitor complexes. Biochemistry 44:6463–6470. https://doi.org/10.1021/bi047318e
doi: 10.1021/bi047318e
pubmed: 15850380
Takeda M, Baba S, Okuma J et al (2022) Metagenomic mining and structure-function studies of a hyper-thermostable cellobiohydrolase from hot spring sediment. Commun Biol 5:247. https://doi.org/10.1038/s42003-022-03195-1
doi: 10.1038/s42003-022-03195-1
pubmed: 35318423
pmcid: 8940973
Tiwari P, Misra BN, Sangwan NS (2013) β-Glucosidases from the Fungus Trichoderma: an efficient cellulase machinery in biotechnological applications. Biomed Res Int 2013:203735. https://doi.org/10.1155/2013/203735
doi: 10.1155/2013/203735
pubmed: 23984325
pmcid: 3747355
van Bueren A, Otani S, Friis EP et al (2012) Three-dimensional structure of a thermophilic family GH11 xylanase from {\it Thermobifida fusca}. Acta Crystallogr Sect F 68:141–144. https://doi.org/10.1107/S1744309111049608
doi: 10.1107/S1744309111049608
Wang Q, Ding L, Zhu C (2018) Characterization of laccase from a novel isolated white-rot fungi Trametes sp. MA-X01 and its potential application in dye decolorization. Biotechnol Biotechnol Equip 32:1477–1485. https://doi.org/10.1080/13102818.2018.1517028
doi: 10.1080/13102818.2018.1517028
Wu S, Wu S (2020) Processivity and the mechanisms of processive endoglucanases. Appl Biochem Biotechnol 190:448–463
doi: 10.1007/s12010-019-03096-w
pubmed: 31378843
Wu S, Liu B, Zhang X (2006) Characterization of a recombinant thermostable xylanase from deep-sea thermophilic Geobacillus sp. MT-1 in East Pacific. Appl Microbiol Biotechnol 72:1210–1216. https://doi.org/10.1007/s00253-006-0416-4
doi: 10.1007/s00253-006-0416-4
pubmed: 16607523
Yennamalli RM, Rader AJ, Wolt JD, Sen TZ (2011) Thermostability in endoglucanases is fold-specific. BMC Struct Biol. https://doi.org/10.1186/1472-6807-11-10
doi: 10.1186/1472-6807-11-10
pubmed: 21291533
pmcid: 3047435
Yennamalli RM, Rader AJ, Kenny AJ et al (2013) Endoglucanases: insights into thermostability for biofuel applications. Biotechnol Biofuels 6:1–9
doi: 10.1186/1754-6834-6-136
Yi Y, Xu S, Kovalevsky A et al (2021) Characterization and structural analysis of a thermophilic GH11 xylanase from compost metatranscriptome. Appl Microbiol Biotechnol 105:7757–7767. https://doi.org/10.1007/s00253-021-11587-2
doi: 10.1007/s00253-021-11587-2
pubmed: 34553251
Yousef NMH, Mawad AMM (2023) Characterization of thermo/halo stable cellulase produced from halophilic Virgibacillus salarius BM-02 using non-pretreated biomass. World J Microbiol Biotechnol 39:22. https://doi.org/10.1007/s11274-022-03446-7
doi: 10.1007/s11274-022-03446-7
Yuan X, Zhang P, Jiao S et al (2018) Overexpression and biochemical characterization of a recombinant psychrophilic endocellulase from Pseudoalteromonas sp. DY3. Int J Biol Macromol 116:100–105. https://doi.org/10.1016/j.ijbiomac.2018.05.017
doi: 10.1016/j.ijbiomac.2018.05.017
pubmed: 29733934
Zainudin MHM, Mustapha NA, Hassan MA et al (2019) A highly thermostable crude endoglucanase produced by a newly isolated thermobifida fusca strain UPMC 901. Sci Rep 9:13526. https://doi.org/10.1038/s41598-019-50126-y
doi: 10.1038/s41598-019-50126-y
pubmed: 31537863
pmcid: 6753106
Zanoni JDA, De OIB, Perrone OM et al (2021) Production and biochemical characterization of xylanases synthesized by the thermophilic fungus Rasamsonia emersonii S10 by solid-state cultivation. Eclet Quim 46:53–67. https://doi.org/10.26850/1678-4618eqj.v46.1SI.2021.p53-67
doi: 10.26850/1678-4618eqj.v46.1SI.2021.p53-67
Zarafeta D, Galanopoulou AP, Leni ME et al (2020) XynDZ5: a new thermostable GH10 xylanase. Front Microbiol. https://doi.org/10.3389/fmicb.2020.00545
doi: 10.3389/fmicb.2020.00545
pubmed: 32390953
pmcid: 7193231
Zhao B, Al Rasheed H, Ali I, Hu S (2021) Efficient enzymatic saccharification of alkaline and ionic liquid-pretreated bamboo by highly active extremozymes produced by the co-culture of two halophilic fungi. Bioresour Technol 319:124115. https://doi.org/10.1016/j.biortech.2020.124115
doi: 10.1016/j.biortech.2020.124115
pubmed: 32949831
Zhu D, Zhang P, Xie C et al (2017) Biodegradation of alkaline lignin by Bacillus ligniniphilus L1. Biotechnol Biofuels 10:44. https://doi.org/10.1186/s13068-017-0735-y
doi: 10.1186/s13068-017-0735-y
pubmed: 28239416
pmcid: 5320714
Zhu D, Adebisi WA, Ahmad F et al (2020) Recent development of extremophilic bacteria and their application in biorefinery. Front Bioeng Biotechnol. https://doi.org/10.3389/fbioe.2020.00483
doi: 10.3389/fbioe.2020.00483
pubmed: 33585426
pmcid: 7783312
Zuccaro G, Pirozzi D, Yousuf A (2019) Lignocellulosic biomass to biodiesel. lignocellulosic biomass to liquid biofuels. Elsevier, Amsterdam, pp 127–167