{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T04:48:21Z","timestamp":1787028501800,"version":"build-2736575974"},"reference-count":94,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2023,2,24]],"date-time":"2023-02-24T00:00:00Z","timestamp":1677196800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo","award":["2016\/190950-0"],"award-info":[{"award-number":["2016\/190950-0"]}]},{"name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo","award":["2021\/08120-1"],"award-info":[{"award-number":["2021\/08120-1"]}]},{"name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo","award":["Finance Code 001"],"award-info":[{"award-number":["Finance Code 001"]}]},{"DOI":"10.13039\/501100002322","name":"Coordena\u00e7\u00e3o de Aperfei\u00e7oamento de Pessoal de N\u00edvel Superior","doi-asserted-by":"publisher","award":["2016\/190950-0"],"award-info":[{"award-number":["2016\/190950-0"]}],"id":[{"id":"10.13039\/501100002322","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002322","name":"Coordena\u00e7\u00e3o de Aperfei\u00e7oamento de Pessoal de N\u00edvel Superior","doi-asserted-by":"publisher","award":["2021\/08120-1"],"award-info":[{"award-number":["2021\/08120-1"]}],"id":[{"id":"10.13039\/501100002322","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002322","name":"Coordena\u00e7\u00e3o de Aperfei\u00e7oamento de Pessoal de N\u00edvel Superior","doi-asserted-by":"publisher","award":["Finance Code 001"],"award-info":[{"award-number":["Finance Code 001"]}],"id":[{"id":"10.13039\/501100002322","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Concern over environmental impacts has spurred many efforts to replace fossil fuels with biofuels such as ethanol. However, for this to be possible, it is necessary to invest in other production technologies, such as second generation (2G) ethanol, in order to raise the levels of this product and meet the growing demand. Currently, this type of production is not yet economically feasible, due to the high costs of the enzyme cocktails used in saccharification stage of lignocellulosic biomass. In order to optimize these cocktails, the search for enzymes with superior activities has been the goal of several research groups. For this end, we have characterized the new \u03b2-glycosidase AfBgl1.3 from A. fumigatus after expression and purification in Pichia pastoris X-33. Structural analysis by circular dichroism revealed that increasing temperature destructured the enzyme; the apparent Tm value was 48.5 \u00b0C. The percentages of \u03b1-helix (36.3%) and \u03b2-sheet (12.4%) secondary structures at 25 \u00b0C were predicted. Biochemical characterization suggested that the optimal conditions for AfBgl1.3 were pH 6.0 and temperature of 40 \u00b0C. At 30 and 40 \u00b0C, the enzyme was stable and retained about 90% and 50% of its activity, respectively, after pre-incubation for 24 h. In addition, the enzyme was highly stable at pH between 5 and 8, retaining over 65% of its activity after pre-incubation for 48 h. AfBgl1.3 co-stimulation with 50\u2013250 mM glucose enhanced its specific activity by 1.4-fold and revealed its high tolerance to glucose (IC50 = 2042 mM). The enzyme was active toward the substrates salicin (495.0 \u00b1 49.0 U mg\u22121), pNPG (340.5 \u00b1 18.6 U mg\u22121), cellobiose (89.3 \u00b1 5.1 U mg\u22121), and lactose (45.1 \u00b1 0.5 U mg\u22121), so it had broad specificity. The Vmax values were 656.0 \u00b1 17.5, 706.5 \u00b1 23.8, and 132.6 \u00b1 7.1 U mg\u22121 toward p-nitrophenyl-\u03b2-D-glucopyranoside (pNPG), D-(-)-salicin, and cellobiose, respectively. AfBgl1.3 displayed transglycosylation activity, forming cellotriose from cellobiose. The addition of AfBgl1.3 as a supplement at 0.9 FPU\/g of cocktail Celluclast\u00ae 1.5L increased carboxymethyl cellulose (CMC) conversion to reducing sugars (g L\u22121) by about 26% after 12 h. Moreover, AfBgl1.3 acted synergistically with other Aspergillus fumigatus cellulases already characterized by our research group\u2014CMC and sugarcane delignified bagasse were degraded, releasing more reducing sugars compared to the control. These results are important in the search for new cellulases and in the optimization of enzyme cocktails for saccharification.<\/jats:p>","DOI":"10.3390\/ijms24054489","type":"journal-article","created":{"date-parts":[[2023,2,27]],"date-time":"2023-02-27T03:23:36Z","timestamp":1677468216000},"page":"4489","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Characterization of a New Glucose-Tolerant GH1 \u03b2-Glycosidase from Aspergillus fumigatus with Transglycosylation Activity"],"prefix":"10.3390","volume":"24","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1537-5644","authenticated-orcid":false,"given":"Lucas Matheus Soares","family":"Pereira","sequence":"first","affiliation":[{"name":"Department of Chemistry, Faculty of Philosophy, Sciences and Literature of Ribeir\u00e3o Preto, University of S\u00e3o Paulo, Ribeir\u00e3o Preto 14040-901, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0442-812X","authenticated-orcid":false,"given":"Aline Vianna","family":"Bernardi","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Faculty of Philosophy, Sciences and Literature of Ribeir\u00e3o Preto, University of S\u00e3o Paulo, Ribeir\u00e3o Preto 14040-901, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8262-8322","authenticated-orcid":false,"given":"Luis Eduardo","family":"Gerolamo","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Faculty of Philosophy, Sciences and Literature of Ribeir\u00e3o Preto, University of S\u00e3o Paulo, Ribeir\u00e3o Preto 14040-901, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wellington Ramos","family":"Pedersoli","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Immunology, Ribeir\u00e3o Preto Medical School, University of S\u00e3o Paulo, Ribeir\u00e3o Preto 14049-900, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cl\u00e1udia Batista","family":"Carraro","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Immunology, Ribeir\u00e3o Preto Medical School, University of S\u00e3o Paulo, Ribeir\u00e3o Preto 14049-900, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8992-7130","authenticated-orcid":false,"given":"Roberto do Nascimento","family":"Silva","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Immunology, Ribeir\u00e3o Preto Medical School, University of S\u00e3o Paulo, Ribeir\u00e3o Preto 14049-900, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergio Akira","family":"Uyemura","sequence":"additional","affiliation":[{"name":"Department of Clinical, Toxicological and Bromatological Analysis, School of Pharmaceutical Sciences of Ribeir\u00e3o Preto, University of S\u00e3o Paulo, Ribeir\u00e3o Preto 14040-903, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6284-387X","authenticated-orcid":false,"given":"Ta\u00edsa Magnani","family":"Dinamarco","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Faculty of Philosophy, Sciences and Literature of Ribeir\u00e3o Preto, University of S\u00e3o Paulo, Ribeir\u00e3o Preto 14040-901, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,2,24]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"9043","DOI":"10.1021\/jf1008023","article-title":"Compositional Analysis of Lignocellulosic Feedstocks. 1. Review and Description of Methods","volume":"58","author":"Sluiter","year":"2010","journal-title":"J. Agric. Food Chem."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Guti\u00e9rrez-Antonio, C., Romero-Izquierdo, A.G., G\u00f3mez-Castro, F.I., and Hern\u00e1ndez, S. (2021). Production Processes of Renewable Aviation Fuel, Elsevier.","DOI":"10.1016\/B978-0-323-90971-6.00042-5"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"874","DOI":"10.3389\/fchem.2019.00874","article-title":"Lignocellulosic Biomass: Understanding Recalcitrance and Predicting Hydrolysis","volume":"7","author":"Zoghlami","year":"2019","journal-title":"Front. Chem."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"105896","DOI":"10.1016\/j.biombioe.2020.105896","article-title":"Sugarcane Straw as a Potential Second Generation Feedstock for Biorefinery and White Biotechnology Applications","volume":"144","author":"Aguiar","year":"2021","journal-title":"Biomass Bioenergy"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"126195","DOI":"10.1016\/j.biortech.2021.126195","article-title":"Recent Advances in Lignocellulosic Biomass for Biofuels and Value-Added Bioproducts\u2014A Critical Review","volume":"344","author":"Ashokkumar","year":"2022","journal-title":"Bioresour. Technol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1089\/ind.2015.0017","article-title":"Second-Generation Ethanol: The Need Is Becoming a Reality","volume":"12","author":"Gallardo","year":"2016","journal-title":"Ind. Biotechnol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1007\/s12275-009-0159-x","article-title":"Purification and Biochemical Properties of a Glucose-Stimulated \u03b2-D-Glucosidase Produced by Humicola grisea Var. Thermoidea Grown on Sugarcane Bagasse","volume":"48","author":"Nascimento","year":"2010","journal-title":"J. Microbiol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1111\/jam.13923","article-title":"An Update on Enzymatic Cocktails for Lignocellulose Breakdown","volume":"125","author":"Lopes","year":"2018","journal-title":"J. Appl. Microbiol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1007\/s13205-015-0328-z","article-title":"Catalytic Properties, Functional Attributes and Industrial Applications of \u03b2-Glucosidases","volume":"6","author":"Singh","year":"2016","journal-title":"3 Biotech"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"100005","DOI":"10.1016\/j.engmic.2021.100005","article-title":"Integrated Engineering of Enzymes and Microorganisms for Improving the Efficiency of Industrial Lignocellulose Deconstruction","volume":"1","author":"Liu","year":"2021","journal-title":"Eng. Microbiol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/j.biombioe.2019.02.016","article-title":"Bioinformatics Applied to Biotechnology: A Review towards Bioenergy Research","volume":"123","author":"Borelli","year":"2019","journal-title":"Biomass Bioenergy"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"612","DOI":"10.3390\/biom3030612","article-title":"Fungal Beta-Glucosidases: A Bottleneck in Industrial Use of Lignocellulosic Materials","volume":"3","author":"Ahring","year":"2013","journal-title":"Biomolecules"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.tibtech.2013.10.003","article-title":"Lignocellulosic Ethanol Production at High-Gravity: Challenges and Perspectives","volume":"32","author":"Koppram","year":"2014","journal-title":"Trends Biotechnol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1002\/bit.25022","article-title":"Enzymatic Hydrolysis of Pelletized AFEXTM-Treated Corn Stover at High Solid Loadings","volume":"111","author":"Bals","year":"2014","journal-title":"Biotechnol. Bioeng."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/j.biortech.2014.02.041","article-title":"Sugar Production from Barley Straw Biomass Pretreated by Combined Alkali and Enzymatic Extrusion","volume":"158","author":"Duque","year":"2014","journal-title":"Bioresour. Technol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.biortech.2014.05.034","article-title":"Optimization of Fed-Batch Enzymatic Hydrolysis from Alkali-Pretreated Sugarcane Bagasse for High-Concentration Sugar Production","volume":"167","author":"Gao","year":"2014","journal-title":"Bioresour. Technol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1007\/s12010-014-1049-1","article-title":"The Role of Product Inhibition as a Yield-Determining Factor in Enzymatic High-Solid Hydrolysis of Pretreated Corn Stover","volume":"174","author":"Olsen","year":"2014","journal-title":"Appl. Biochem. Biotechnol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1186\/1754-6834-6-105","article-title":"Selecting \u03b2-Glucosidases to Support Cellulases in Cellulose Saccharification","volume":"6","author":"Teugjas","year":"2013","journal-title":"Biotechnol. Biofuels"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1016\/j.biortech.2018.07.137","article-title":"Glucose Tolerant and Glucose Stimulated \u03b2-Glucosidases\u2014A Review","volume":"267","author":"Salgado","year":"2018","journal-title":"Bioresour. Technol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1080\/07388550290789568","article-title":"Microbial \u03b2-Glucosidases: Cloning, Properties, and Applications","volume":"22","author":"Bhatia","year":"2002","journal-title":"Crit. Rev. Biotechnol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.molcatb.2015.09.003","article-title":"A Neurospora Crassa \u0178-Glucosidase with Potential for Lignocellulose Hydrolysis Shows Strong Glucose Tolerance and Stimulation by Glucose and Xylose","volume":"122","author":"Meleiro","year":"2015","journal-title":"J. Mol. Catal. B Enzym."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"17296","DOI":"10.1038\/srep17296","article-title":"A Mechanism of Glucose Tolerance and Stimulation of GH1 \u03b2-Glucosidases","volume":"5","author":"Yang","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.mib.2010.01.010","article-title":"Protein Engineering of Microbial Enzymes","volume":"13","author":"Bornscheuer","year":"2010","journal-title":"Curr. Opin. Microbiol."},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"de Gouv\u00eaa, P.F., Bernardi, A.V., Gerolamo, L.E., de Souza Santos, E., Ria\u00f1o-Pach\u00f3n, D.M., Uyemura, S.A., and Dinamarco, T.M. (2018). Transcriptome and Secretome Analysis of Aspergillus fumigatus in the Presence of Sugarcane Bagasse. BMC Genom., 19.","DOI":"10.1186\/s12864-018-4627-8"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1126\/science.aar5140","article-title":"Structure of the Yeast Oligosaccharyltransferase Complex Gives Insight into Eukaryotic N-Glycosylation","volume":"359","author":"Wild","year":"2018","journal-title":"Science"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.jsb.2010.07.008","article-title":"Structural and Functional Analysis of Three \u03b2-Glucosidases from Bacterium Clostridium cellulovorans, Fungus Trichoderma reesei and Termite Neotermes koshunensis","volume":"173","author":"Jeng","year":"2011","journal-title":"J. Struct. Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/j.nbt.2017.08.012","article-title":"Structural Insights into \u03b2-Glucosidase Transglycosylation Based on Biochemical, Structural and Computational Analysis of Two GH1 Enzymes from Trichoderma harzianum","volume":"40","author":"Florindo","year":"2018","journal-title":"New Biotechnol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1094","DOI":"10.1016\/j.ijbiomac.2018.04.156","article-title":"Purification and Characterization of a Novel GH1 Beta-Glucosidase from Jeotgalibacillus malaysiensis","volume":"115","author":"Liew","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Baiya, S., Pengthaisong, S., Kitjaruwankul, S., and Ketudat Cairns, J.R. (2021). Structural Analysis of Rice Os4BGlu18 Monolignol \u03b2-Glucosidase. PLoS ONE, 16.","DOI":"10.1371\/journal.pone.0241325"},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Mohamad Sobri, M.F., Abd-Aziz, S., Abu Bakar, F.D., and Ramli, N. (2020). In-Silico Characterization of Glycosyl Hydrolase Family 1 \u03b2-Glucosidase from Trichoderma asperellum UPM1. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21114035"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"W315","DOI":"10.1093\/nar\/gky497","article-title":"BeStSel: A Web Server for Accurate Protein Secondary Structure Prediction and Fold Recognition from the Circular Dichroism Spectra","volume":"46","author":"Micsonai","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1002\/bip.360221211","article-title":"Dictionary of Protein Secondary Structure: Pattern Recognition of Hydrogen-Bonded and Geometrical Features","volume":"22","author":"Kabsch","year":"1983","journal-title":"Biopolymers"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1038\/nprot.2015.053","article-title":"The Phyre2 Web Portal for Protein Modeling, Prediction and Analysis","volume":"10","author":"Kelley","year":"2015","journal-title":"Nat. Protoc."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"e23067","DOI":"10.1002\/bip.23067","article-title":"Thermal Melt Circular Dichroism Spectroscopic Studies for Identifying Stabilising Amphipathic Molecules for the Voltage-gated Sodium Channel NavMs","volume":"109","author":"Ireland","year":"2018","journal-title":"Biopolymers"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"7447","DOI":"10.1128\/AEM.01386-12","article-title":"Specific Fusion of \u03b2-1,4-Endoglucanase and \u03b2-1,4-Glucosidase Enhances Cellulolytic Activity and Helps in Channeling of Intermediates","volume":"78","author":"Adlakha","year":"2012","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1186\/s13068-016-0487-0","article-title":"Crystal Structure and Biochemical Characterization of the Recombinant ThBgl, a GH1 \u03b2-Glucosidase Overexpressed in Trichoderma harzianum under Biomass Degradation Conditions","volume":"9","author":"Santos","year":"2016","journal-title":"Biotechnol. Biofuels"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"822","DOI":"10.1016\/j.ijbiomac.2020.09.236","article-title":"Functional and Structural Characterization of a Novel GH3 \u03b2-Glucosidase from the Gut Metagenome of the Brazilian Cerrado Termite Syntermes wheeleri","volume":"165","author":"Lima","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Bashirova, A., Pramanik, S., Volkov, P., Rozhkova, A., Nemashkalov, V., Zorov, I., Gusakov, A., Sinitsyn, A., Schwaneberg, U., and Davari, M. (2019). Disulfide Bond Engineering of an Endoglucanase from Penicillium verruculosum to Improve Its Thermostability. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20071602"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"3607","DOI":"10.1128\/AEM.64.10.3607-3614.1998","article-title":"Purification, Characterization, and Substrate Specificity of a Novel Highly Glucose-Tolerant \u03b2-Glucosidase from Aspergillus oryzae","volume":"64","author":"Riou","year":"1998","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1016\/j.jbiosc.2015.03.019","article-title":"Purification and Enzymatic Characterization of Secretory Glycoside Hydrolase Family 3 (GH3) Aryl \u03b2-Glucosidases Screened from Aspergillus oryzae Genome","volume":"120","author":"Kudo","year":"2015","journal-title":"J. Biosci. Bioeng."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"108770","DOI":"10.1016\/j.lwt.2019.108770","article-title":"Fast, Inexpensive Purification of \u03b2-Glucosidase from Aspergillus niger and Improved Catalytic\/Physicochemical Properties upon the Enzyme Immobilization: Possible Broad Prospects for Industrial Applications","volume":"118","author":"Karami","year":"2020","journal-title":"LWT"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"6998","DOI":"10.1038\/s41598-020-63972-y","article-title":"A Highly Glucose Tolerant SS-Glucosidase from Malbranchea pulchella (MpBg3) Enables Cellulose Saccharification","volume":"10","author":"Monteiro","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1186\/s13068-018-1226-5","article-title":"Penicillium citrinum UFV1 \u03b2-Glucosidases: Purification, Characterization, and Application for Biomass Saccharification","volume":"11","author":"Pereira","year":"2018","journal-title":"Biotechnol. Biofuels"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"2455","DOI":"10.1007\/s12649-019-00589-x","article-title":"Biochemical Properties of Carbohydrate-Active Enzymes Synthesized by Penicillium chrysogenum Using Corn Straw as Carbon Source","volume":"11","author":"Silva","year":"2020","journal-title":"Waste Biomass Valorization"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1186\/s13068-016-0560-8","article-title":"Engineering a Highly Active Thermophilic \u03b2-Glucosidase to Enhance Its PH Stability and Saccharification Performance","volume":"9","author":"Xia","year":"2016","journal-title":"Biotechnol. Biofuels"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1287","DOI":"10.1016\/j.procbio.2012.05.004","article-title":"Consolidated Bioprocessing and Simultaneous Saccharification and Fermentation of Lignocellulose to Ethanol with Thermotolerant Yeast Strains","volume":"47","author":"Hasunuma","year":"2012","journal-title":"Process Biochem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"122494","DOI":"10.1016\/j.biortech.2019.122494","article-title":"Experimental Optimization and Techno-Economic Analysis of Bioethanol Production by Simultaneous Saccharification and Fermentation Process Using Sugarcane Straw","volume":"297","author":"Pratto","year":"2020","journal-title":"Bioresour. Technol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1016\/j.ijbiomac.2018.03.018","article-title":"Biochemical Characterization of a Novel Thermostable \u03b2-Glucosidase from Dictyoglomus turgidum","volume":"113","author":"Fusco","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1007\/s13399-019-00556-5","article-title":"Expression and Characterization of a Cold-Adapted, Salt- and Glucose-Tolerant GH1 \u03b2-Glucosidase Obtained from Thermobifida halotolerans and Its Use in Sugarcane Bagasse Hydrolysis","volume":"11","author":"Yin","year":"2021","journal-title":"Biomass Convers. Biorefin."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"2475","DOI":"10.1007\/s10529-011-0724-3","article-title":"Expression of a Secretory \u03b2-Glucosidase from Trichoderma reesei in Pichia pastoris and Its Characterization","volume":"33","author":"Chen","year":"2011","journal-title":"Biotechnol. Lett."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.procbio.2020.08.013","article-title":"Heterologous Production and Biochemical Characterization of a New Highly Glucose Tolerant GH1 \u03b2-Glucosidase from Anoxybacillus thermarum","volume":"99","author":"Salgado","year":"2020","journal-title":"Process Biochem."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"109799","DOI":"10.1016\/j.enzmictec.2021.109799","article-title":"Cloning, Expression, Biochemical Characterization, and Molecular Docking Studies of a Novel Glucose Tolerant \u03b2-Glucosidase from Saccharomonospora sp. NB11","volume":"148","author":"Belduz","year":"2021","journal-title":"Enzyme Microb. Technol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"126840","DOI":"10.1016\/j.micres.2021.126840","article-title":"Characterization of a Glucose-Stimulated \u03b2-Glucosidase from Microbulbifer sp. ALW1","volume":"251","author":"Jiang","year":"2021","journal-title":"Microbiol. Res."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1467","DOI":"10.1007\/s10482-020-01455-w","article-title":"Characterization of a Cu2+, SDS, Alcohol and Glucose Tolerant GH1 \u03b2-Glucosidase from Bacillus sp. CGMCC 1.16541","volume":"113","author":"Yin","year":"2020","journal-title":"Antonie Van Leeuwenhoek"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"784","DOI":"10.1016\/j.carbpol.2012.09.086","article-title":"Biochemical Properties of a Novel Glycoside Hydrolase Family 1 \u03b2-Glucosidase (PtBglu1) from Paecilomyces thermophila Expressed in Pichia pastoris","volume":"92","author":"Yang","year":"2013","journal-title":"Carbohydr. Polym."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1016\/j.bbrc.2009.12.038","article-title":"Structural Insights into the Substrate Recognition Properties of \u03b2-Glucosidase","volume":"391","author":"Nam","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"723678","DOI":"10.3389\/fmicb.2021.723678","article-title":"Structural and Catalytic Characterization of TsBGL, a \u03b2-Glucosidase From Thermofilum sp. Ex4484_79","volume":"12","author":"Chen","year":"2021","journal-title":"Front. Microbiol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1007\/s12010-020-03373-z","article-title":"A Novel Glucose-Tolerant GH1 \u03b2-Glucosidase and Improvement of Its Glucose Tolerance Using Site-Directed Mutation","volume":"192","author":"Sun","year":"2020","journal-title":"Appl. Biochem. Biotechnol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/j.bcab.2018.01.008","article-title":"Biochemical Characterization of an Isolated 50 kDa Beta-Glucosidase from the Thermophilic Fungus Myceliophthora thermophila M.7.7","volume":"13","author":"Gomes","year":"2018","journal-title":"Biocatal. Agric. Biotechnol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1021\/jf504333h","article-title":"\u03b2-(1\u21923)-Glucanolytic Yeasts from Brazilian Grape Microbiota: Production and Characterization of \u03b2-Glucanolytic Enzymes by Aureobasidium pullulans 1WA1 Cultivated on Fungal Mycelium","volume":"63","author":"Bauermeister","year":"2015","journal-title":"J. Agric. Food Chem."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1111\/j.1432-1033.1992.tb17332.x","article-title":"Purificication and Properties of Aspergillus niger Beta-Glucosidase","volume":"209","author":"Watanabe","year":"1992","journal-title":"Eur. J. Biochem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1289","DOI":"10.1128\/aem.44.6.1289-1295.1982","article-title":"Purification and Properties of \u03b2-Glucosidase from Aspergillus terreus","volume":"44","author":"Workman","year":"1982","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1007\/s12010-016-2344-9","article-title":"Characterization of Xylanase and Cellulase Produced by a Newly Isolated Aspergillus fumigatus N2 and Its Efficient Saccharification of Barley Straw","volume":"182","author":"Lin","year":"2017","journal-title":"Appl. Biochem. Biotechnol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"4764","DOI":"10.1038\/s41467-018-07145-6","article-title":"Calcium Stabilizes the Strongest Protein Fold","volume":"9","author":"Milles","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1351","DOI":"10.4014\/jmb.1003.03011","article-title":"Cloning and Characterization of a \u03b2-Glucosidase from Marine Microbial Metagenome with Excellent Glucose Tolerance","volume":"20","author":"Fang","year":"2010","journal-title":"J. Microbiol. Biotechnol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1007\/s00792-005-0500-1","article-title":"Characterization of a \u03b2-Glycosidase from the Thermoacidophilic Bacterium Alicyclobacillus acidocaldarius","volume":"10","author":"Rossi","year":"2006","journal-title":"Extremophiles"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"113697","DOI":"10.1016\/j.indcrop.2021.113697","article-title":"A Thermophilic, PH-Tolerant, and Highly Active GH10 Xylanase from Aspergillus fumigatus Boosted Pre-Treated Sugarcane Bagasse Saccharification by Cellulases","volume":"170","author":"Bernardi","year":"2021","journal-title":"Ind. Crops Prod."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1007\/s00249-011-0706-3","article-title":"Structural Stability and Unfolding Transition of \u03b2-Glucosidases: A Comparative Investigation on Isozymes from a Thermo-Tolerant Yeast","volume":"40","author":"Shah","year":"2011","journal-title":"Eur. Biophys. J."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"16325","DOI":"10.1039\/D0CP03062G","article-title":"The Multifaceted Effects of DMSO and High Hydrostatic Pressure on the Kinetic Constants of Hydrolysis Reactions Catalyzed by \u03b1-Chymotrypsin","volume":"22","author":"Ostermeier","year":"2020","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1007\/s10295-013-1291-5","article-title":"Highly Glucose Tolerant \u03b2-Glucosidase from Aspergillus unguis: NII 08123 for Enhanced Hydrolysis of Biomass","volume":"40","author":"Rajasree","year":"2013","journal-title":"J. Ind. Microbiol. Biotechnol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1186\/s13068-017-0932-8","article-title":"Bioprospecting of Novel Thermostable \u03b2-Glucosidase from Bacillus subtilis RA10 and Its Application in Biomass Hydrolysis","volume":"10","author":"Tiwari","year":"2017","journal-title":"Biotechnol. Biofuels"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1453","DOI":"10.1021\/jf025777l","article-title":"\u03b2-Glucosidase from the Grape Native Yeast Debaryomyces vanrijiae: Purification, Characterization, and Its Effect on Monoterpene Content of a Muscat Grape Juice","volume":"51","author":"Belancic","year":"2003","journal-title":"J. Agric. Food Chem."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/0167-4838(95)00074-5","article-title":"Properties of a Novel Glucose-Enhanced \u03b2-Glucosidase Purified from Streptomyces Sp. (ATCC 11238)","volume":"1251","author":"Rebordosa","year":"1995","journal-title":"Biochim. Biophys. Acta (BBA) Protein Struct. Mol. Enzymol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1007\/s00253-016-7803-2","article-title":"Screening, Identification, and Characterization of a Novel Saccharide-Stimulated \u03b2-Glycosidase from a Soil Metagenomic Library","volume":"101","author":"Matsuzawa","year":"2017","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1093\/abbs\/gmt061","article-title":"Expression and Characterization of a Novel Highly Glucose-Tolerant Beta-Glucosidase from a Soil Metagenome","volume":"45","author":"Lu","year":"2013","journal-title":"Acta Biochim. Biophys. Sin."},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Guo, B., Amano, Y., and Nozaki, K. (2016). Improvements in Glucose Sensitivity and Stability of Trichoderma reesei \u03b2-Glucosidase Using Site-Directed Mutagenesis. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0147301"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"1631","DOI":"10.1107\/S1399004714006920","article-title":"Structural Basis for Glucose Tolerance in GH1 \u03b2-Glucosidases","volume":"70","author":"Souza","year":"2014","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"18325","DOI":"10.1074\/jbc.M113.471342","article-title":"Characterization of a Novel \u03b2-Glucosidase from a Compost Microbial Metagenome with Strong Transglycosylation Activity","volume":"288","author":"Uchiyama","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1128\/jb.139.3.761-769.1979","article-title":"Induction of Cellulolytic Enzymes in Trichoderma reesei by Sophorose","volume":"139","author":"Sternberg","year":"1979","journal-title":"J. Bacteriol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1352","DOI":"10.1016\/j.biortech.2017.05.126","article-title":"Genetic Modification: A Tool for Enhancing Beta-Glucosidase Production for Biofuel Application","volume":"245","author":"Singhania","year":"2017","journal-title":"Bioresour. Technol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"8327","DOI":"10.1007\/s00253-020-10820-8","article-title":"Engineering of Cellobiose Phosphorylase for the Defined Synthesis of Cellotriose","volume":"104","author":"Ubiparip","year":"2020","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_82","doi-asserted-by":"crossref","unstructured":"Vianna Bernardi, A., Kimie Yonamine, D., Akira Uyemura, S., and Magnani Dinamarco, T. (2019). A Thermostable Aspergillus fumigatus GH7 Endoglucanase Over-Expressed in Pichia pastoris Stimulates Lignocellulosic Biomass Hydrolysis. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20092261"},{"key":"ref_83","doi-asserted-by":"crossref","unstructured":"Bernardi, A.V., Gerolamo, L.E., de Gouv\u00eaa, P.F., Yonamine, D.K., Pereira, L.M.S., de Oliveira, A.H.C., Uyemura, S.A., and Dinamarco, T.M. (2020). LPMO AfAA9_B and Cellobiohydrolase AfCel6A from A. fumigatus Boost Enzymatic Saccharification Activity of Cellulase Cocktail. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22010276"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly Accurate Protein Structure Prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1038\/s41592-022-01488-1","article-title":"ColabFold: Making Protein Folding Accessible to All","volume":"19","author":"Mirdita","year":"2022","journal-title":"Nat. Methods"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"W384","DOI":"10.1093\/nar\/gkt458","article-title":"GalaxyRefine: Protein Structure Refinement Driven by Side-Chain Repacking","volume":"41","author":"Heo","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1007\/BF00228148","article-title":"AQUA and PROCHECK-NMR: Programs for Checking the Quality of Protein Structures Solved by NMR","volume":"8","author":"Laskowski","year":"1996","journal-title":"J. Biomol. NMR"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1107\/S0021889892009944","article-title":"PROCHECK: A Program to Check the Stereochemical Quality of Protein Structures","volume":"26","author":"Laskowski","year":"1993","journal-title":"J. Appl. Crystallogr."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1038\/nprot.2010.181","article-title":"Circular Polymerase Extension Cloning for High-Throughput Cloning of Complex and Combinatorial DNA Libraries","volume":"6","author":"Quan","year":"2011","journal-title":"Nat. Protoc."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1016\/S0021-9258(20)78300-6","article-title":"The Colorimetric Determination of the Serum Proteins","volume":"82","author":"Greenberg","year":"1929","journal-title":"J. Biol. Chem."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"1627","DOI":"10.1021\/ac60214a047","article-title":"Smoothing and Differentiation of Data by Simplified Least Squares Procedures","volume":"36","author":"Savitzky","year":"1964","journal-title":"Anal. Chem."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1021\/ac60147a030","article-title":"Use of Dinitrosalicylic Acid Reagent for Determination of Reducing Sugar","volume":"31","author":"Miller","year":"1959","journal-title":"Anal. Chem."},{"key":"ref_93","unstructured":"Fontana, J.D., Gebara, M., Blumel, M., Schneider, H., MacKenzie, C.R., and Johnson, K.G. (1988). Methods in Enzymology, Academic Press."},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Yepes, C., Est\u00e9vez, J., Arroyo, M., and Ladero, M. (2022). Immobilization of an Industrial \u03b2-Glucosidase from Aspergillus fumigatus and Its Use for Cellobiose Hydrolysis. Processes, 10.","DOI":"10.3390\/pr10061225"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/24\/5\/4489\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T18:41:26Z","timestamp":1760121686000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/24\/5\/4489"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,2,24]]},"references-count":94,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2023,3]]}},"alternative-id":["ijms24054489"],"URL":"https:\/\/doi.org\/10.3390\/ijms24054489","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,2,24]]}}}