TY - JOUR
T1 - Screening of supports for the immobilization of β-glucosidase
AU - De Alencar Figueira, Joelise
AU - Dias, Fernanda Furlan Gonçalves
AU - Sato, Hélia Harumi
AU - Fernandes, Pedro
PY - 2011
Y1 - 2011
N2 - A set of supports were screened for the immobilization of a partially purified extract of β-glucosidase from Aspergillus sp. These supports, namely, Eupergit, Amberlite, alginate, gelatin, polyvinyl alcohol- (PVA-) based matrices (Lentikats), and sol-gel, have proved effective for the implementation of some other enzyme-based processes. The initial criterion for selection of promising supports prior to further characterization relied on the retention of the catalytic activity following immobilization. Based on such criterion, where immobilization in sol-gel and in Lentikats outmatched the remaining approaches, those two systems were further characterized. Immobilization did not alter the pH/activity profile, whereas the temperature/activity profile was improved when sol-gel support was assayed. Both thermal and pH stability were improved as a result of immobilization. An increase in the apparent KM (Michaelis constant) was observed following immobilization, suggesting diffusion limitations.
AB - A set of supports were screened for the immobilization of a partially purified extract of β-glucosidase from Aspergillus sp. These supports, namely, Eupergit, Amberlite, alginate, gelatin, polyvinyl alcohol- (PVA-) based matrices (Lentikats), and sol-gel, have proved effective for the implementation of some other enzyme-based processes. The initial criterion for selection of promising supports prior to further characterization relied on the retention of the catalytic activity following immobilization. Based on such criterion, where immobilization in sol-gel and in Lentikats outmatched the remaining approaches, those two systems were further characterized. Immobilization did not alter the pH/activity profile, whereas the temperature/activity profile was improved when sol-gel support was assayed. Both thermal and pH stability were improved as a result of immobilization. An increase in the apparent KM (Michaelis constant) was observed following immobilization, suggesting diffusion limitations.
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U2 - 10.4061/2011/642460
DO - 10.4061/2011/642460
M3 - Article
AN - SCOPUS:84869034577
SN - 2090-0406
VL - 2011
JO - Enzyme Research
JF - Enzyme Research
IS - 1
M1 - 642460
ER -