{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,22]],"date-time":"2026-08-22T06:24:01Z","timestamp":1787379841645,"version":"build-2736575974"},"reference-count":96,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,8,21]],"date-time":"2026-08-21T00:00:00Z","timestamp":1787270400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,8,21]],"date-time":"2026-08-21T00:00:00Z","timestamp":1787270400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["FEBS Open Bio"],"abstract":"<jats:p>\n                    Microbial esterases are versatile and stable enzymes with a wide range of biotechnological applications. However, few esterases have been characterized from archaea, an important source of extremophilic enzymes. In this study, we report the biochemical characterization and crystal structure of Ta0887, a novel esterase from the thermoacidophilic archaeon\n                    <jats:italic>Thermoplasma acidophilum<\/jats:italic>\n                    . The protein was successfully cloned, expressed, and purified in\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    . Light scattering assays revealed that Ta0887 is a monomer in solution. Activity assays using\n                    <jats:italic>p<\/jats:italic>\n                    \u2010nitrophenyl (\n                    <jats:italic>p<\/jats:italic>\n                    \u2010NP) esters confirmed its esterase activity, showing a substrate preference for\n                    <jats:italic>p<\/jats:italic>\n                    \u2010NP hexanoate (C6). Furthermore, the substitution of Ser95 with alanine completely abolished enzymatic activity, thereby confirming its essential role as the nucleophilic residue of the catalytic triad. The enzyme exhibited optimal activity at 65\u2009\u00b0C and pH 8.0. Notably, Ta0887 displayed high thermal stability, retaining 66% residual activity after incubation at 80\u2009\u00b0C for 2\u2009h, consistent with its thermal denaturation midpoint temperature of 80.6\u2009\u00b0C. The crystal structure of Ta0887, resolved at 1.93\u2009\u00c5, revealed an \u03b1\/\u03b2\u2010hydrolase core domain consisting of an eight\u2010strand \u03b2\u2010sheet, surrounded by seven \u03b1\u2010helices, and a cap domain comprising four \u03b1\u2010helices. Ta0887 features a large substrate\u2010binding pocket at the interface between the two domains that contains the conserved residues Ser95, Asp187, and His215 of the catalytic triad. Further analysis indicates that an efficiently packed hydrophobic core is a key feature for the observed thermostability. The findings from this study provide a basis for the future engineering of Ta0887 with the aim of enhancing its potential for industrial and biotechnological applications.\n                  <\/jats:p>","DOI":"10.1002\/2211-5463.70327","type":"journal-article","created":{"date-parts":[[2026,8,22]],"date-time":"2026-08-22T05:52:22Z","timestamp":1787377942000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Structural and biochemical insights into the thermostable esterase Ta0887 from\n                    <i>Thermoplasma acidophilum<\/i>"],"prefix":"10.1002","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8869-3790","authenticated-orcid":false,"given":"Alejandro","family":"Delgado\u2010Rey","sequence":"first","affiliation":[{"name":"IPICYT, Divisi\u00f3n de Biolog\u00eda Molecular, Instituto Potosino de Investigaci\u00f3n Cient\u00edfica y Tecnol\u00f3gica A.C.  San Luis Potos\u00ed M\u00e9xico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5144-710X","authenticated-orcid":false,"given":"Miriam Livier","family":"Llamas\u2010Garc\u00eda","sequence":"additional","affiliation":[{"name":"IPICYT, Divisi\u00f3n de Biolog\u00eda Molecular, Instituto Potosino de Investigaci\u00f3n Cient\u00edfica y Tecnol\u00f3gica A.C.  San Luis Potos\u00ed M\u00e9xico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3951-9726","authenticated-orcid":false,"given":"Gabriela M.","family":"Montero\u2010Mor\u00e1n","sequence":"additional","affiliation":[{"name":"Facultad de Ciencias Qu\u00edmicas Universidad Aut\u00f3noma de San Luis Potos\u00ed  M\u00e9xico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leticia","family":"Santos","sequence":"additional","affiliation":[{"name":"IPICYT, Divisi\u00f3n de Biolog\u00eda Molecular, Instituto Potosino de Investigaci\u00f3n Cient\u00edfica y Tecnol\u00f3gica A.C.  San Luis Potos\u00ed M\u00e9xico"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3313-0165","authenticated-orcid":false,"given":"Samuel","family":"Lara\u2010Gonz\u00e1lez","sequence":"additional","affiliation":[{"name":"IPICYT, Divisi\u00f3n de Biolog\u00eda Molecular, Instituto Potosino de Investigaci\u00f3n Cient\u00edfica y Tecnol\u00f3gica A.C.  San Luis Potos\u00ed M\u00e9xico"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,8,21]]},"reference":[{"key":"e_1_2_10_2_1","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1016\/j.jmb.2008.10.075","article-title":"Crystal structure and biochemical properties of a novel thermostable esterase containing an immunoglobulin\u2010like domain","volume":"385","author":"Levisson M","year":"2009","journal-title":"J Mol Biol"},{"key":"e_1_2_10_3_1","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1007\/978-1-61779-600-5_1","article-title":"Lipases: an overview","volume":"861","author":"Casas\u2010Godoy L","year":"2012","journal-title":"Methods Mol Biol"},{"key":"e_1_2_10_4_1","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/B978-0-08-100596-5.21640-5","volume-title":"Encyclopedia of Food Chemistry","author":"Lai OM","year":"2019"},{"key":"e_1_2_10_5_1","doi-asserted-by":"crossref","first-page":"1219","DOI":"10.1002\/jobm.201500081","article-title":"Molecular cloning and characterization of a new and highly thermostable esterase from Geobacillus sp. JM6","volume":"55","author":"Zhu Y","year":"2015","journal-title":"J Basic Microbiol"},{"key":"e_1_2_10_6_1","first-page":"1","volume-title":"Aerobic Utilization of Hydrocarbons, Oils and Lipids","author":"Kovacic F","year":"2018"},{"issue":"1","key":"e_1_2_10_7_1","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1042\/bj3430177","article-title":"Bacterial lipolytic enzymes: classification and properties","volume":"343","author":"Arpigny JL","year":"1999","journal-title":"Biochem J"},{"key":"e_1_2_10_8_1","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1146\/annurev.micro.53.1.315","article-title":"Bacterial biocatalysts: molecular biology, three\u2010dimensional structures, and biotechnological applications of lipases","volume":"53","author":"Jaeger KE","year":"1999","journal-title":"Ann Rev Microbiol"},{"key":"e_1_2_10_9_1","doi-asserted-by":"crossref","DOI":"10.3390\/biom11111552","article-title":"Identification and biochemical characterization of a novel hormone\u2010sensitive lipase family esterase Est19 from the Antarctic bacterium Pseudomonas sp. E2\u201015","volume":"11","author":"Liu X","year":"2021","journal-title":"Biomolecules"},{"key":"e_1_2_10_10_1","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2023.128302","article-title":"Structure\u2010directed bioengineering the lid1 of cold\u2010adapted Pseudomonas sp. TB11 esterase to boost catalytic capacity","volume":"255","author":"Sha L","year":"2024","journal-title":"Int J Biol Macromol"},{"key":"e_1_2_10_11_1","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1002\/ejlt.200900143","article-title":"Protein engineering and discovery of lipases","volume":"112","author":"Kourist R","year":"2010","journal-title":"Eur J Lipid Sci Technol"},{"key":"e_1_2_10_12_1","doi-asserted-by":"crossref","first-page":"1214","DOI":"10.1016\/j.csbj.2021.01.047","article-title":"Biochemical and structural characterization of a novel thermophilic esterase EstD11 provide catalytic insights for the HSL family","volume":"19","author":"Miguel\u2010Ruano V","year":"2021","journal-title":"Comput Struct Biotechnol J"},{"key":"e_1_2_10_13_1","doi-asserted-by":"crossref","DOI":"10.1038\/srep38886","article-title":"Metagenomic mining for thermostable esterolytic enzymes uncovers a new family of bacterial esterases","volume":"6","author":"Zarafeta D","year":"2016","journal-title":"Sci Rep"},{"key":"e_1_2_10_14_1","unstructured":"ResearchGV(2022)Hydrolase enzymes market size share & trends analysis report by product (esterase glycosylase) by application (pharmaceutical food & beverage) by region and segment forecasts 2022\u20132030."},{"key":"e_1_2_10_15_1","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/B978-0-12-818322-9.00013-7","volume-title":"Physiological and Biotechnological Aspects of Extremophiles","author":"De Luca V","year":"2020"},{"key":"e_1_2_10_16_1","doi-asserted-by":"crossref","first-page":"7069","DOI":"10.1007\/s00253-021-11520-7","article-title":"Thermostable lipases and their dynamics of improved enzymatic properties","volume":"105","author":"Hamdan SH","year":"2021","journal-title":"Appl Microbiol Biotechnol"},{"key":"e_1_2_10_17_1","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1021\/op020019h","article-title":"High\u2010throughput screening of thermostable Esterases for industrial bioconversions","volume":"6","author":"Lagarde D","year":"2002","journal-title":"Org Process Res Dev"},{"key":"e_1_2_10_18_1","doi-asserted-by":"crossref","DOI":"10.1016\/j.biotechadv.2022.108054","article-title":"Archaeal lipolytic enzymes: current developments and further prospects","volume":"61","author":"Meghwanshi GK","year":"2022","journal-title":"Biotechnol Adv"},{"key":"e_1_2_10_19_1","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1007\/s00792-008-0139-9","article-title":"Extremely thermostable esterases from the thermoacidophilic euryarchaeon Picrophilus torridus","volume":"12","author":"Hess M","year":"2008","journal-title":"Extremophiles"},{"key":"e_1_2_10_20_1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S1381-1177(03)00064-X","article-title":"Cloning, purification and properties of a hyperthermophilic esterase from archaeon Aeropyrum pernix K1","volume":"24","author":"Gao R","year":"2003","journal-title":"J Mol Catal B Enzym"},{"key":"e_1_2_10_21_1","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/j.pep.2004.01.010","article-title":"A novel phospholipase A2\/esterase from hyperthermophilic archaeon Aeropyrum pernix K1","volume":"35","author":"Wang B","year":"2004","journal-title":"Protein Expr Purif"},{"key":"e_1_2_10_22_1","doi-asserted-by":"crossref","first-page":"13823","DOI":"10.1038\/s41598-018-32059-0","article-title":"The Thaumarchaeon N. gargensis carries functional bioABD genes and has a promiscuous E. coli \u0394bioH\u2010complementing esterase EstN1","volume":"8","author":"Chow J","year":"2018","journal-title":"Sci Rep"},{"key":"e_1_2_10_23_1","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/S1389-1723(05)00310-5","article-title":"Molecular cloning and characterization of a thermostable carboxylesterase from an archaeon, Sulfolobus shibatae DSM5389: non\u2010linear kinetic behavior of a hormone\u2010sensitive lipase family enzyme","volume":"98","author":"Ejima K","year":"2004","journal-title":"J Biosci Bioeng"},{"key":"e_1_2_10_24_1","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1111\/j.1574-6968.2004.tb09633.x","article-title":"A novel thermostable esterase from the thermoacidophilic archaeon Sulfolobus tokodaii strain 7","volume":"236","author":"Suzuki Y","year":"2004","journal-title":"FEMS Microbiol Lett"},{"key":"e_1_2_10_25_1","doi-asserted-by":"crossref","first-page":"3071","DOI":"10.1111\/j.1742-4658.2012.08687.x","article-title":"Structure and stability of a thermostable carboxylesterase from the thermoacidophilic archaeon Sulfolobus tokodaii","volume":"279","author":"Angkawidjaja C","year":"2012","journal-title":"FEBS J"},{"key":"e_1_2_10_26_1","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/S0378-1119(01)00879-4","article-title":"A carboxylesterase from the hyperthermophilic archaeon Sulfolobus solfataricus: cloning of the gene, characterization of the protein","volume":"283","author":"Morana A","year":"2002","journal-title":"Gene"},{"key":"e_1_2_10_27_1","doi-asserted-by":"crossref","first-page":"2289","DOI":"10.1271\/bbb.68.2289","article-title":"Thermostable esterase from a thermoacidophilic archaeon: purification and characterization for enzymatic resolution of a chiral compound","volume":"68","author":"Kim S","year":"2004","journal-title":"Biosci Biotechnol Biochem"},{"key":"e_1_2_10_28_1","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.molcatb.2013.05.019","article-title":"Cloning, expression, purification, and characterization of a thermostable esterase from the archaeon Sulfolobus solfataricus P1","volume":"94","author":"Nam J\u2010K","year":"2013","journal-title":"J Mol Catal B Enzym"},{"key":"e_1_2_10_29_1","doi-asserted-by":"crossref","first-page":"820","DOI":"10.1016\/j.bbagen.2006.01.009","article-title":"A carboxylesterase from the thermoacidophilic archaeon Sulfolobus solfataricus P1; purification, characterization, and expression","volume":"1760","author":"Park Y\u2010J","year":"2006","journal-title":"Biochim Biophys Acta Gen Subj"},{"key":"e_1_2_10_30_1","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1042\/bj2500453","article-title":"Purification and characterization of a heat\u2010stable esterase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius","volume":"250","author":"Sobek H","year":"1988","journal-title":"Biochem J"},{"key":"e_1_2_10_31_1","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1042\/bj2610993","article-title":"Further kinetic and molecular characterization of an extremely heat\u2010stable carboxylesterase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius","volume":"261","author":"Sobek H","year":"1989","journal-title":"Biochem J"},{"key":"e_1_2_10_32_1","doi-asserted-by":"crossref","first-page":"16885","DOI":"10.3390\/ijms150916885","article-title":"Biochemical characterization of a carboxylesterase from the archaeon Pyrobaculum sp. 1860 and a rational explanation of its substrate specificity and thermostability","volume":"15","author":"Shao H","year":"2014","journal-title":"Int J Mol Sci"},{"key":"e_1_2_10_33_1","doi-asserted-by":"crossref","first-page":"3925","DOI":"10.1128\/AEM.68.8.3925-3931.2002","article-title":"Extremely stable and versatile carboxylesterase from a Hyperthermophilic archaeon","volume":"68","author":"Hotta Y","year":"2002","journal-title":"Appl Environ Microbiol"},{"key":"e_1_2_10_34_1","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1006\/abbi.1999.1497","article-title":"Cloning, overexpression, and properties of a new thermophilic and thermostable esterase with sequence similarity to hormone\u2010sensitive lipase subfamily from the archaeon Archaeoglobus fulgidus","volume":"373","author":"Manco G","year":"2000","journal-title":"Arch Biochem Biophys"},{"key":"e_1_2_10_35_1","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1007\/s12275-007-0185-5","article-title":"Cloning and characterization of thermostable esterase from Archaeoglobus fulgidus","volume":"46","author":"Kim S\u2010B","year":"2008","journal-title":"J Microbiol"},{"key":"e_1_2_10_36_1","doi-asserted-by":"crossref","DOI":"10.1038\/srep25542","article-title":"Structural and biochemical characterisation of Archaeoglobus fulgidus esterase reveals a bound CoA molecule in the vicinity of the active site","volume":"6","author":"Sayer C","year":"2016","journal-title":"Sci Rep"},{"key":"e_1_2_10_37_1","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1126\/science.7725097","article-title":"Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 a resolution","volume":"268","author":"L\u00f6we J","year":"1995","journal-title":"Science"},{"key":"e_1_2_10_38_1","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1126\/science.7725107","article-title":"Proteasome from Thermoplasma acidophilum: a threonine protease","volume":"268","author":"Seem\u00fcller E","year":"1995","journal-title":"Science"},{"key":"e_1_2_10_39_1","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1016\/S0969-2126(94)00118-9","article-title":"The crystal structure of citrate synthase from the thermophilic archaeon, Thermoplasma acidophilum","volume":"2","author":"Russell RJM","year":"1994","journal-title":"Structure"},{"key":"e_1_2_10_40_1","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1006\/jmbi.2000.4240","article-title":"Thermostability and thermoactivity of citrate synthases from the thermophilic and hyperthermophilic archaea, Thermoplasma acidophilum and Pyrococcus furiosus","volume":"304","author":"Arnott MA","year":"2000","journal-title":"J Mol Biol"},{"key":"e_1_2_10_41_1","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1093\/jb\/mvg083","article-title":"Purification and characterization of geranylgeranylglyceryl phosphate synthase from a thermoacidophilic archaeon, Thermoplasma acidophilum","volume":"133","author":"Nemoto N","year":"2003","journal-title":"J Biochem"},{"key":"e_1_2_10_42_1","doi-asserted-by":"crossref","first-page":"1105","DOI":"10.1515\/BC.2004.144","article-title":"Thermoplasma acidophilum TAA43 is an archaeal member of the eukaryotic meiotic branch of AAA ATPases","volume":"385","author":"Santos L","year":"2004","journal-title":"Biol Chem"},{"key":"e_1_2_10_43_1","doi-asserted-by":"crossref","first-page":"1256","DOI":"10.1093\/glycob\/cws094","article-title":"Cell surface glycoproteins from Thermoplasma acidophilum are modified with an N\u2010linked glycan containing 6\u2010C\u2010sulfofucose","volume":"22","author":"Vinogradov E","year":"2012","journal-title":"Glycobiology"},{"key":"e_1_2_10_44_1","doi-asserted-by":"crossref","first-page":"1034","DOI":"10.1016\/j.jmb.2007.01.029","article-title":"Structural insights into unique substrate selectivity of Thermoplasma acidophilum d\u2010aldohexose dehydrogenase","volume":"367","author":"Yasutake Y","year":"2007","journal-title":"J Mol Biol"},{"key":"e_1_2_10_45_1","doi-asserted-by":"crossref","first-page":"1416","DOI":"10.1126\/science.170.3965.1416","article-title":"A thermophilic, acidophilic mycoplasma isolated from a coal refuse pile","volume":"170","author":"Darland G","year":"1970","journal-title":"Science"},{"key":"e_1_2_10_46_1","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1128\/jb.116.2.1019-1028.1973","article-title":"Characterization of the membranes of Thermoplasma acidophilum","volume":"116","author":"Smith PF","year":"1973","journal-title":"J Bacteriol"},{"key":"e_1_2_10_47_1","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1038\/35035069","article-title":"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum","volume":"407","author":"Ruepp A","year":"2000","journal-title":"Nature"},{"key":"e_1_2_10_48_1","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1385\/1-59259-890-0:571","volume-title":"The Proteomics Protocols Handbook","author":"Gasteiger E","year":"2005"},{"key":"e_1_2_10_49_1","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1186\/1472-6807-9-50","article-title":"CRYSTALP2: sequence\u2010based protein crystallization propensity prediction","volume":"9","author":"Kurgan L","year":"2009","journal-title":"BMC Struct Biol"},{"key":"e_1_2_10_50_1","doi-asserted-by":"crossref","first-page":"W521","DOI":"10.1093\/nar\/gkae241","article-title":"The EMBL\u2010EBI job dispatcher sequence analysis tools framework in 2024","volume":"52","author":"Madeira F","year":"2024","journal-title":"Nucleic Acids Res"},{"key":"e_1_2_10_51_1","doi-asserted-by":"crossref","first-page":"W389","DOI":"10.1093\/nar\/gkv332","article-title":"JPred4: a protein secondary structure prediction server","volume":"43","author":"Drozdetskiy A","year":"2015","journal-title":"Nucleic Acids Res"},{"key":"e_1_2_10_52_1","doi-asserted-by":"crossref","DOI":"10.1093\/molbev\/msae263","article-title":"MEGA12: molecular evolutionary genetic analysis version 12 for adaptive and green computing","volume":"41","author":"Kumar S","year":"2024","journal-title":"Mol Biol Evol"},{"key":"e_1_2_10_53_1","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1002\/pro.3290","article-title":"Clustal omega for making accurate alignments of many protein sequences","volume":"27","author":"Sievers F","year":"2018","journal-title":"Protein Sci"},{"key":"e_1_2_10_54_1","doi-asserted-by":"crossref","first-page":"W344","DOI":"10.1093\/nar\/gkw408","article-title":"ConSurf 2016: an improved methodology to estimate and visualize evolutionary conservation in macromolecules","volume":"44","author":"Ashkenazy H","year":"2016","journal-title":"Nucleic Acids Res"},{"key":"e_1_2_10_55_1","doi-asserted-by":"crossref","DOI":"10.1016\/j.pep.2021.105862","article-title":"Purification and characterization of an FeII\u2010 and \u03b1\u2010ketoglutarate\u2010dependent xanthine hydroxylase from Aspergillus oryzae","volume":"183","author":"Bocanegra\u2010Jim\u00e9nez FY","year":"2021","journal-title":"Protein Expr Purif"},{"key":"e_1_2_10_56_1","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the Head of bacteriophage T4","volume":"227","author":"Laemmli UK","year":"1970","journal-title":"Nature"},{"key":"e_1_2_10_57_1","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1002\/bmb.20644","article-title":"Protein analysis by dynamic light scattering: methods and techniques for students","volume":"40","author":"Lorber B","year":"2012","journal-title":"Biochem Mol Biol Educ"},{"key":"e_1_2_10_58_1","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1007\/s11745-017-4265-y","article-title":"Identification and characterization of a novel thermophilic, organic solvent stable lipase of Bacillus from a hot spring","volume":"52","author":"Li J","year":"2017","journal-title":"Lipids"},{"key":"e_1_2_10_59_1","doi-asserted-by":"crossref","first-page":"4836","DOI":"10.1128\/jb.173.15.4836-4841.1991","article-title":"Extracellular lipase of Pseudomonas sp. strain ATCC 21808: purification, characterization, crystallization, and preliminary X\u2010ray diffraction data","volume":"173","author":"Kordel M","year":"1991","journal-title":"J Bacteriol"},{"key":"e_1_2_10_60_1","doi-asserted-by":"crossref","first-page":"1042","DOI":"10.1016\/j.enzmictec.2006.02.005","article-title":"Lipase from the thermotolerant fungus Rhizopus homothallicus is more thermostable when produced using solid state fermentation than liquid fermentation procedures","volume":"39","author":"Mateos Diaz JC","year":"2006","journal-title":"Enzym Microb Technol"},{"key":"e_1_2_10_61_1","doi-asserted-by":"crossref","DOI":"10.3389\/fmicb.2022.855658","article-title":"Characterization of a novel esterase Est33 from an Antarctic bacterium: a representative of a new esterase family","volume":"13","author":"Liu X","year":"2022","journal-title":"Front Microbiol"},{"key":"e_1_2_10_62_1","doi-asserted-by":"crossref","first-page":"782","DOI":"10.1016\/j.biotechadv.2009.06.001","article-title":"Methods for detection and characterization of lipases: a comprehensive review","volume":"27","author":"Hasan F","year":"2009","journal-title":"Biotechnol Adv"},{"key":"e_1_2_10_63_1","first-page":"13139","article-title":"Production and characterization of lipase from Bacillus stearothermophilus","volume":"10","author":"Massadeh M","year":"2011","journal-title":"Afr J Biotechnol"},{"key":"e_1_2_10_64_1","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/S0076-6879(82)87025-0","article-title":"Buffers of constant ionic strength for studying pH\u2010dependent processes","volume":"87","author":"Ellis KJ","year":"1982","journal-title":"Methods Enzymol"},{"key":"e_1_2_10_65_1","doi-asserted-by":"crossref","first-page":"31","DOI":"10.15359\/ru.34-2.2","article-title":"Revisiting the fundamentals of p\u2010nitrophenol analysis for its application in the quantification of lipases activity. A graphical update","volume":"34","author":"Syedd\u2010Le\u00f3n R","year":"2020","journal-title":"Uniciencia"},{"key":"e_1_2_10_66_1","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1107\/S0907444906019949","article-title":"HKL\u20103000: the integration of data reduction and structure solution \u2013 from diffraction images to an initial model in minutes","volume":"62","author":"Minor W","year":"2006","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"issue":"2","key":"e_1_2_10_67_1","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive python\u2010based system for macromolecular structure solution","volume":"66","author":"Adams P","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_2_10_68_1","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy AJ","year":"2007","journal-title":"J Appl Crystallogr"},{"key":"e_1_2_10_69_1","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model\u2010building tools for molecular graphics","volume":"60","author":"Emsley P","year":"2005","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_2_10_70_1","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all\u2010atom structure validation for macromolecular crystallography","volume":"66","author":"Chen V","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_2_10_71_1","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1002\/pro.3280","article-title":"Improvements to the APBS biomolecular solvation software suite","volume":"27","author":"Jurrus E","year":"2018","journal-title":"Protein Sci"},{"key":"e_1_2_10_72_1","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF chimera\u2014a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen EF","year":"2004","journal-title":"J Comput Chem"},{"key":"e_1_2_10_73_1","doi-asserted-by":"crossref","DOI":"10.1002\/pro.4473","article-title":"PDBsum1: a standalone program for generating PDBsum analyses","volume":"31","author":"Laskowski RA","year":"2022","journal-title":"Protein Sci"},{"key":"e_1_2_10_74_1","doi-asserted-by":"crossref","first-page":"W194","DOI":"10.1093\/nar\/gkae415","article-title":"CASTpFold: computed atlas of surface topography of the universe of protein folds","volume":"52","author":"Ye B","year":"2024","journal-title":"Nucleic Acids Res"},{"key":"e_1_2_10_75_1","unstructured":"Schr\u00f6dinger LLCThe PyMOL Molecular Graphics System Version 3.1."},{"key":"e_1_2_10_76_1","doi-asserted-by":"crossref","first-page":"W559","DOI":"10.1093\/nar\/gkab375","article-title":"ProteinTools: a toolkit to analyze protein structures","volume":"49","author":"Ferruz N","year":"2021","journal-title":"Nucleic Acids Res"},{"key":"e_1_2_10_77_1","doi-asserted-by":"crossref","first-page":"33387","DOI":"10.1074\/jbc.M505030200","article-title":"X\u2010ray snapshots of peptide processing in mutants of tricorn\u2010interacting factor F1 from Thermoplasma acidophilum*","volume":"280","author":"Goettig P","year":"2005","journal-title":"J Biol Chem"},{"key":"e_1_2_10_78_1","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1007\/978-1-61779-600-5_2","volume-title":"Lipases and Phospholipases: Methods and Protocols","author":"Ali YB","year":"2012"},{"key":"e_1_2_10_79_1","doi-asserted-by":"crossref","DOI":"10.7717\/peerj.7249","article-title":"A proposed update for the classification and description of bacterial lipolytic enzymes","volume":"7","author":"Hitch TCA","year":"2019","journal-title":"PeerJ"},{"key":"e_1_2_10_80_1","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1016\/S0006-291X(03)00375-9","article-title":"Crystal structure of a histidine\u2010tagged serine hydrolase involved in the carbazole degradation (CarC enzyme)","volume":"303","author":"Habe H","year":"2003","journal-title":"Biochem Biophys Res Commun"},{"key":"e_1_2_10_81_1","doi-asserted-by":"crossref","first-page":"1079","DOI":"10.1021\/acs.jafc.0c06338","article-title":"Structural insights into a novel esterase from the East Pacific rise and its improved thermostability by a semirational design","volume":"69","author":"Zhu C","year":"2021","journal-title":"J Agric Food Chem"},{"key":"e_1_2_10_82_1","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1002\/pro.3289","article-title":"PDBsum: structural summaries of PDB entries","volume":"27","author":"Laskowski RA","year":"2018","journal-title":"Protein Sci"},{"key":"e_1_2_10_83_1","doi-asserted-by":"crossref","first-page":"W210","DOI":"10.1093\/nar\/gkac387","article-title":"Dali server: structural unification of protein families","volume":"50","author":"Holm L","year":"2022","journal-title":"Nucleic Acids Res"},{"key":"e_1_2_10_84_1","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1038\/ng0595-111","article-title":"A candidate genetic risk factor for vascular disease: a common mutation in methylenetetrahydrofolate reductase","volume":"10","author":"Frosst P","year":"1995","journal-title":"Nat Genet"},{"key":"e_1_2_10_85_1","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1002\/pro.2860","article-title":"Clusters of isoleucine, leucine, and valine side chains define cores of stability in high\u2010energy states of globular proteins: sequence determinants of structure and stability","volume":"25","author":"Kathuria SV","year":"2016","journal-title":"Protein Sci"},{"key":"e_1_2_10_86_1","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1002\/prot.24232","article-title":"Hydrophobic environment is a key factor for the stability of thermophilic proteins","volume":"81","author":"Gromiha MM","year":"2013","journal-title":"Proteins"},{"key":"e_1_2_10_87_1","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1110\/ps.37401","article-title":"Stabilization of hen egg white lysozyme by a cavity\u2010filling mutation","volume":"10","author":"Ohmura T","year":"2001","journal-title":"Protein Sci"},{"key":"e_1_2_10_88_1","doi-asserted-by":"crossref","DOI":"10.1186\/1472-6807-11-42","article-title":"Comparative void\u2010volume analysis of psychrophilic and mesophilic enzymes: structural bioinformatics of psychrophilic enzymes reveals sources of core flexibility","volume":"11","author":"Paredes DI","year":"2011","journal-title":"BMC Struct Biol"},{"key":"e_1_2_10_89_1","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0145848","article-title":"Comparing residue clusters from thermophilic and mesophilic enzymes reveals adaptive mechanisms","volume":"11","author":"Sammond DW","year":"2016","journal-title":"PLoS One"},{"key":"e_1_2_10_90_1","doi-asserted-by":"crossref","first-page":"6064","DOI":"10.1021\/acs.jafc.1c00940","article-title":"The \u03b1\u2010helical cap domain of a novel esterase from gut Alistipes shahii shaping the substrate\u2010binding pocket","volume":"69","author":"Wei X","year":"2021","journal-title":"J Agric Food Chem"},{"key":"e_1_2_10_91_1","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1007\/s11802-024-5664-3","article-title":"Characterization of a novel esterase belonging to family V from Marinobacter flavimaris","volume":"23","author":"He J","year":"2024","journal-title":"J Ocean Univ China"},{"key":"e_1_2_10_92_1","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1016\/0304-4165(76)90278-6","article-title":"Thermoplasma acidophilum: intracellular pH and potassium concentration","volume":"451","author":"Searcy DG","year":"1976","journal-title":"Biochim Biophys Acta Gen Subj"},{"key":"e_1_2_10_93_1","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0169540","article-title":"Crystal structure and functional characterization of an esterase (EaEST) from Exiguobacterium antarcticum","volume":"12","author":"Lee CW","year":"2017","journal-title":"PLoS One"},{"key":"e_1_2_10_94_1","doi-asserted-by":"crossref","first-page":"1426","DOI":"10.1016\/j.jmb.2007.12.062","article-title":"High\u2010resolution structure of ybfF from Escherichia coli K12: a unique substrate\u2010binding crevice generated by domain arrangement","volume":"376","author":"Park SY","year":"2008","journal-title":"J Mol Biol"},{"key":"e_1_2_10_95_1","doi-asserted-by":"crossref","first-page":"2622","DOI":"10.1039\/C5CY00085H","article-title":"Substrate channel evolution of an esterase for the synthesis of cilastatin","volume":"5","author":"Luan Z\u2010J","year":"2015","journal-title":"Cat Sci Technol"},{"key":"e_1_2_10_96_1","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0020506","article-title":"Crystal structure of a novel esterase Rv0045c from Mycobacterium tuberculosis","volume":"6","author":"Zheng X","year":"2011","journal-title":"PLoS One"},{"key":"e_1_2_10_97_1","doi-asserted-by":"crossref","DOI":"10.3389\/fmicb.2015.01294","article-title":"The structure of a novel thermophilic esterase from the planctomycetes species, Thermogutta terrifontis reveals an open active site due to a minimal \u2018cap\u2019 domain","volume":"6","author":"Sayer C","year":"2015","journal-title":"Front Microbiol"}],"container-title":["FEBS Open Bio"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/2211-5463.70327","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/full-xml\/10.1002\/2211-5463.70327","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/2211-5463.70327","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,22]],"date-time":"2026-08-22T05:52:33Z","timestamp":1787377953000},"score":1,"resource":{"primary":{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/10.1002\/2211-5463.70327"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,21]]},"references-count":96,"alternative-id":["10.1002\/2211-5463.70327"],"URL":"https:\/\/doi.org\/10.1002\/2211-5463.70327","archive":["Portico"],"relation":{},"ISSN":["2211-5463","2211-5463"],"issn-type":[{"value":"2211-5463","type":"print"},{"value":"2211-5463","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,21]]},"assertion":[{"value":"2026-06-05","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2026-08-07","order":2,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2026-08-21","order":3,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}],"article-number":"2211-5463.70327"}}