Efficiency Assessment between Entrapment and Covalent Bond Immobilization of Mutant -Xylosidase onto Chitosan Support
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Romero, G; Contreras Moyeja, Lellys Mariela![Autoridad Universidad de Almería Autoridad Universidad de Almería](/themes/Mirage2/images/autoridades/autoridad.png)
![Autoridad Universidad de Almería Autoridad Universidad de Almería](/themes/Mirage2/images/autoridades/autoridad.png)
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2023Resumen
The Y509E mutant of -xylosidase from Geobacillus stearothermophilus (XynB2Y509E) (which
also bears xylanase activity) has been immobilized in chitosan spheres through either entrapment or
covalent bond formation methods. The maximum immobilization yield by entrapment was achieved
by chitosan beads developed using a 2% chitosan solution after 1 h of maturation time in CFG buffer
with ethanol. On the other hand, the highest value in covalent bond immobilization was observed
when employing chitosan beads that were prepared from a 2% chitosan solution after 4 h of activation
in 1% glutaraldehyde solution at pH 8. The activity expressed after immobilization by covalent
bonding was 23% higher compared to the activity expressed following entrapment immobilization,
with values of 122.3 and 99.4 IU.g1, respectively. Kinetic data revealed that catalytic turnover values
were decreased as compared to a free counterpart. Both biocatalysts showed increased thermal
and pH stability, alon...
Palabra/s clave
-xylosidase
chitosan
enzyme immobilization
G. stearothermophilus
xylanase