{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Munoz-Tafalla R"],"funding":["Horizon Europe","Horizon 2020 Framework Programme","Ministerio de Ciencia, Innovación y Universidades","Agencia Estatal de Investigación","European Commission","EU Framework Programme for Research and Innovation Societal Challenges","European Regional Development Fund"],"pagination":["3814-3823"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12454871"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["27"],"pubmed_abstract":["The structural complexity of xylan makes its complete degradation challenging. Strategies to improve its hydrolysis often requires enzyme cocktails with multiple specific activities or proteins harboring multiple catalytic domains. Here, we introduce a novel approach through the design of Xyn11<sub>m1</sub>, a multifunctional enzyme that combines endoxylanase and feruloyl esterase activities, two catalytic functions involved in the hydrolysis of feruloylated xylans. Using the PluriZyme concept, an artificial feruloyl esterase active site was engineered into the scaffold of a thermophilic glycoside hydrolase family 10 xylanase, Xyn11, from <i>Pseudothermotoga thermarum</i>. Computational design, guided by protein energy landscape exploration simulations, revealed a surface cavity that could"],"journal":["Computational and structural biotechnology journal"],"pubmed_title":["Embedding a feruloyl esterase active site into a thermophilic endoxylanase scaffold for the degradation of feruloylated xylans."],"pmcid":["PMC12454871"],"funding_grant_id":["101060625-Nymphe","PID2019-106370RB-I00","MICIU/AEI/10.13039/501100011033","PID2022\\u2013136367OB-C31/C33","101000327"],"pubmed_authors":["Cea-Rama I","Guallar V","Polaina J","Gonzalez-Alfonso JL","Sanz-Aparicio J","Talens-Perales D","Munoz-Tafalla R","Plou FJ","Cervantes FV","Ferrer M"],"additional_accession":[]},"is_claimable":false,"name":"Embedding a feruloyl esterase active site into a thermophilic endoxylanase scaffold for the degradation of feruloylated xylans.","description":"The structural complexity of xylan makes its complete degradation challenging. Strategies to improve its hydrolysis often requires enzyme cocktails with multiple specific activities or proteins harboring multiple catalytic domains. Here, we introduce a novel approach through the design of Xyn11<sub>m1</sub>, a multifunctional enzyme that combines endoxylanase and feruloyl esterase activities, two catalytic functions involved in the hydrolysis of feruloylated xylans. Using the PluriZyme concept, an artificial feruloyl esterase active site was engineered into the scaffold of a thermophilic glycoside hydrolase family 10 xylanase, Xyn11, from <i>Pseudothermotoga thermarum</i>. Computational design, guided by protein energy landscape exploration simulations, revealed a surface cavity that could","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025","modification":"2026-07-15T06:45:30.691Z","creation":"2026-06-30T03:22:17.659Z"},"accession":"S-EPMC12454871","cross_references":{"pubmed":["40994537"],"doi":["10.1016/j.csbj.2025.09.003"]}}