Immobilization of endoglucanase on kaolin by adsorption and covalent bonding.
Adsorption
Biotechnology
/ methods
Catalysis
Cellulase
/ chemistry
Enzyme Stability
Enzymes, Immobilized
/ metabolism
Glutaral
/ chemistry
Hydrogen-Ion Concentration
Hydrolysis
Kaolin
/ chemistry
Microscopy, Electron, Scanning
Particle Size
Propylamines
/ chemistry
Silanes
/ chemistry
Temperature
X-Ray Diffraction
Adsorption
Cellulases immobilization
Covalent bonding
Kaolin
Reusability
Journal
Bioprocess and biosystems engineering
ISSN: 1615-7605
Titre abrégé: Bioprocess Biosyst Eng
Pays: Germany
ID NLM: 101088505
Informations de publication
Date de publication:
Aug 2021
Aug 2021
Historique:
received:
10
12
2020
accepted:
26
02
2021
pubmed:
10
3
2021
medline:
21
12
2021
entrez:
9
3
2021
Statut:
ppublish
Résumé
In the current research, endoglucanase, one of the enzymes of the cellulolytic complex, was immobilized on kaolin by two different techniques, adsorption, and covalent bonding. A comparative study was conducted between free, adsorbed, and covalently immobilized endoglucanase. For the covalent bonding, the kaolin particles were functionalized with 3-aminopropyltriethoxysilane (APTES) and activated with glutaraldehyde. Immobilization by adsorption was performed using the kaolin without any treatment. Recovered activities after the endoglucanase immobilization by adsorption and covalent bonding were found to be 60 ± 2.5 and 65 ± 3.5%, respectively. The studies of optima pH and temperature, as well as thermal stability, showed that the catalytic characteristic of the enzyme was maintained after the immobilization by both adsorption and covalent bonding. Even after 8 cycles of use, the endoglucanase immobilized by the two techniques retained about 86% of its initial activity. The results showed that the adsorption was as effective as covalent bonding for the immobilization of endoglucanase on kaolin. However, the adsorption technique seems to have a greater potential for use in future studies, as it is simpler, cheaper, and faster than covalent immobilization. Therefore, in this work it was demonstrated that endoglucanases can be immobilized efficiently on kaolin through a very simple immobilization protocol, offering a promising strategy for performing repeated enzymatic hydrolysis reactions.
Identifiants
pubmed: 33686500
doi: 10.1007/s00449-021-02545-3
pii: 10.1007/s00449-021-02545-3
doi:
Substances chimiques
Enzymes, Immobilized
0
Propylamines
0
Silanes
0
Kaolin
24H4NWX5CO
Cellulase
EC 3.2.1.4
amino-propyl-triethoxysilane
L8S6UBW552
Glutaral
T3C89M417N
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1627-1637Subventions
Organisme : Coordenação de Aperfeiçoamento de Pessoal de Nível Superior
ID : 88887.310560/2018-00
Organisme : Coordenação de Aperfeiçoamento de Pessoal de Nível Superior
ID : 88887.310727/2018-00
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