ArticleBioprocess and biosystems engineering2021
Immobilization of endoglucanase on kaolin by adsorption and covalent bonding.
Article in Bioprocess and biosystems engineering, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 16 citations in OpenAlex.
- Enhanced kinetic performance and stability of catalase immobilized on epoxy-functionalized kaolinite.Scientific reports · 2026Article
- Transcriptome and co-expression network analysis reveal the genetic basis of cell wall components in maize stalks.BMC genomics · 2025Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
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.
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