| dc.creator | Romero, Gabriela | |
| dc.creator | Contreras, Lellys M. | |
| dc.creator | Aguirre Céspedes, Carolina | |
| dc.creator | Wilkesman, Jeff | |
| dc.creator | Clemente Jiménez, Josefa María | |
| dc.creator | Rodríguez Vico, Felipe | |
| dc.creator | Las Heras Vázquez, Francisco Javier | |
| dc.date | 2021-12-27T22:50:47Z | |
| dc.date | 2021-12-27T22:50:47Z | |
| dc.date | 2021 | |
| dc.date.accessioned | 2022-12-20T23:32:16Z | |
| dc.date.available | 2022-12-20T23:32:16Z | |
| dc.identifier | Molecules, Volume 26, Issue 2, 2021, 451 | |
| dc.identifier | 1420-3049 | |
| dc.identifier | http://repositoriodigital.ucsc.cl/handle/25022009/2570 | |
| dc.identifier | 10.3390/molecules26020451 | |
| dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/5429041 | |
| dc.description | Artículo de publicación ISI | |
| dc.description | 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. | |
| dc.language | en | |
| dc.publisher | MDPI | |
| dc.source | https://doi.org/10.3390/molecules26020451 | |
| dc.subject | β-xylosidase | |
| dc.subject | Thermostability | |
| dc.subject | CLEAs | |
| dc.subject | G. stearothermophilus | |
| dc.subject | Xylanase | |
| dc.title | Characterization of cross-linked enzyme aggregates of the Y509E mutant of a glycoside hydrolase family 52 β-xylosidase from G. stearothermophilus | |
| dc.type | Artículos de revistas | |
