Potential of Calophyllum Inophyllum Shell as Activated Carbon for Cellulase Immobilization
Year: 2025
Type: conference-paper
Abstract: Immobilized enzymes have higher resistance to environmental changes and can be easily obtained/re-recovered/reusable compared with their free form after use in the biocatalysis process. The main benefit of immobilization is that it protects the enzyme from harsh environmental conditions (e.g. high temperatures, extreme pH values, etc.). However, the enzyme immobilization process is not easy and cheap. Most cellulases used in Indonesia are single-use enzymes and are unstable. This causes the use of cellulase on an industrial scale to be expensive and difficult to store for a long time. Therefore, a solution is needed to mobilize cellulase with a simple and inexpensive process, namely by utilizing activated carbon from the shell of a Calophylluminophyllum seed. This study aimed to investigate the potential of activated carbon made from C. inophyllum shell as an immobilizer for the production of cellulase. An optimal, easy, and simple enzyme immobilization method is required to ensure sufficient cellulase quality and quantity for industrial scale. In general, the four stages of research were as follows: a) the synthesis of activated carbon made from C. inophyllum shell; b) cellular immobilization synthesis; c) stability test of immobilized cellulase against pH and temperature; and d) reusability analysis of immobilized enzymes. This study examined the effect of carbon particle size (60 and 100 mesh) and concentration of ZnCl2 activator (1, 2, and 3 M). The results indicate that the optimal manufacturing of C. inophyllum shell activated carbon is by using a size of 100 Mesh with a concentration of ZnCl2 activator of 2 M, which has an enzyme activity in the range of ±0.25 units/mL, and the immobilized cellulase remains effective for up to 5 reuse cycles.
Source: Engineering headway
DOI: 10.4028/p-6zbddf
Institutions: Institut Teknologi Sepuluh Nopember, Universitas Jember
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
OpenAlex ID: W4412951147