Immobilization of β-glucosidase from Moniliophthora perniciosa on different supports by adsorption

Abstract

Enzyme immobilization allows the reuse of the biocatalyst more than once without excessive loss of its catalytic activity and conveys operational and storage stability. In this work, β-glucosidase produced extracellularly by the filamentous fungus Moniliophthora perniciosa was immobilized by adsorption on Celite, silica, and chitosan. Celite was the chosen carrier for immobilization due to the high activity yield and maintenance of 65% ± 1.9 of its initial activity after seven reuses. The activity of the immobilized β-glucosidase peaked at pH 4 at a temperature of 60 °C. Moreover, the immobilized enzyme retained 23.7% ± 4.85 of the initial activity when incubated at a temperature of 90 °C during 60 min. Additionally, it retained more than 70% of the initial activity after 20 min of incubation at 50–70 °C.