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Characterization of Cross-Linked Enzyme Aggregates of the Y509E Mutant of a Glycoside Hydrolase Family 52 β-xylosidase from G. stearothermoph
dc.contributor.author | Romero, Gabriela | |
dc.contributor.author | Contreras Moyeja, Lellys Mariela | |
dc.contributor.author | Aguirre, Carolina | |
dc.contributor.author | Wilkesman, Jeff | |
dc.contributor.author | Clemente Jiménez, Josefa María | |
dc.contributor.author | Rodríguez Vico, Felipe | |
dc.contributor.author | Las Heras Vázquez, Francisco Javier | |
dc.date.accessioned | 2021-01-18T09:31:20Z | |
dc.date.available | 2021-01-18T09:31:20Z | |
dc.date.issued | 2021-01-16 | |
dc.identifier.issn | 1420-3049 | |
dc.identifier.uri | http://hdl.handle.net/10835/9312 | |
dc.description.abstract | Cross-linked enzyme aggregates (CLEAs) of the Y509E mutant of glycoside hydrolase family 52 β-xylosidase from Geobacillus stearothermophilus with dual activity of β-xylosidase and xylanase (XynB2Y509E) were prepared. Ammonium sulfate was used as the precipitant agent, and glutaraldehyde as cross-linking agent. The optimum conditions were found to be 90% ammonium sulfate, 12.5 mM glutaraldehyde, 3 h of cross-linking reaction at 25 °C, and pH 8.5. Under these (most effective) conditions, XynB2Y509E-CLEAs retained 92.3% of their original β-xylosidase activity. Biochemical characterization of both crude and immobilized enzymes demonstrated that the maximum pH and temperature after immobilization remained unchanged (pH 6.5 and 65 °C). Moreover, an improvement in pH stability and thermostability was also found after immobilization. Analysis of kinetic parameters shows that the Km value of XynB2Y509E-CLEAs obtained was slightly higher than that of free XynB2Y509E (1.2 versus 0.9 mM). Interestingly, the xylanase activity developed by the mutation was also conserved after the immobilization process. | es_ES |
dc.language.iso | en | es_ES |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | β-xylosidase | es_ES |
dc.subject | thermostability | es_ES |
dc.subject | CLEAs | es_ES |
dc.subject | G. stearothermophilus | es_ES |
dc.subject | xylanase | es_ES |
dc.title | Characterization of Cross-Linked Enzyme Aggregates of the Y509E Mutant of a Glycoside Hydrolase Family 52 β-xylosidase from G. stearothermoph | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.relation.publisherversion | https://www.mdpi.com/1420-3049/26/2/451 | es_ES |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es_ES |