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.
| Original language | English |
|---|---|
| Pages (from-to) | 883-892 |
| Number of pages | 10 |
| Journal | Brazilian Journal of Chemical Engineering |
| Volume | 42 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 11 Jul 2024 |
Bibliographical note
Publisher Copyright:© The Author(s) under exclusive licence to Associação Brasileira de Engenharia Química 2024.
Funding
The authors would like to thank the Fundação de Amparo à Pesquisa do Estado da Bahia (FAPESB), the Coordenação de Aperfeiçoamento Pessoal de Nível Superior (CAPES) by doctoral scholarship [88882.447813/2019-01], CNPq, and the Postgraduate Program in Biotechnology—UEFS—for financial support and scholarships.
| Funders | Funder number |
|---|---|
| Postgraduate Program in Biotechnology | |
| Fundação de Amparo à Pesquisa do Estado da Bahia | |
| Coordenação de Aperfeiçoamento de Pessoal de Nível Superior | 88882.447813/2019-01 |
Keywords
- Celite
- Enzyme extract
- Immobilization
- Optimization
- Thermal stability
- β-Glucosidase