Advanced HKUST/MWCNT/Cellulose Acetate Hybrid Support for β-Glucosidase Immobilization: Enhanced Stability, Catalytic Performance, and Reusability
5 affiliations
- 1Department of Biochemistry, King Abdulaziz University, Jeddah 21589, Saudi Arabia
- 2Experimental Biochemistry Unit, King Fahad Medical Research Centre, King Abdulaziz University, Jeddah 21589, Saudi Arabia
- 3Department of Biological Sciences, College of Science, University of Jeddah, Jeddah 23445, Saudi Arabia
- 4Department of Biochemistry, Faculty of Science, University of Tabuk, Tabuk 71491, Saudi Arabia
- 5Chemistry Department, Faculty of Applied Science, Taiz University, P.O. Box 17021, Taiz 3191 Taiz, Yemen
Abstract
This study reports the fabrication of a ternary HKUST/MWCNT/CA hybrid support for the immobilization of β-glucosidase and the evaluation of its catalytic and stability properties. The support was prepared by integrating HKUST with multi-walled carbon nanotubes (MWCNTs) and cellulose acetate (CA), followed by enzyme immobilization through glutaraldehyde-mediated coupling. Structural and surface characterization by XRD, FTIR, SEM/EDX, BET, and zeta potential confirmed the successful formation of the hybrid matrix and subsequent enzyme loading. The immobilization yield reached 88%, indicating efficient enzyme attachment onto the support. Nonlinear Michaelis–Menten analysis showed an increase in apparent Km after immobilization, whereas the apparent Vmax remained comparable to that of the free enzyme, indicating preservation of substantial catalytic performance. The immobilized β-glucosidase exhibited enhanced tolerance toward non-optimal conditions, retaining higher activity over broader pH and temperature ranges than the free enzyme. Notably, the optimum temperature shifted from 50 °C for the free enzyme to 60 °C after immobilization. The immobilized preparation also demonstrated good operational stability, preserving about 74% of its initial activity after 10 cycles, and excellent storage stability, retaining nearly 79% activity after 30 days at 4 °C. These findings demonstrate that HKUST/MWCNT/CA is a promising support for developing robust and reusable β-glucosidase biocatalysts.
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BibTeX
@article{almalki2026advanced,
title = {{Advanced HKUST/MWCNT/Cellulose Acetate Hybrid Support for β-Glucosidase Immobilization: Enhanced Stability, Catalytic Performance, and Reusability}},
author = {Naif Abdullah R. Almalki and Hamed Alsufyani and Hayam A. Alwabsi and Yaaser Q. Almulaiky},
journal = {Catalysts},
year = {2026},
month = oct,
doi = {10.3390/catal16110948},
url = {https://www.mdpi.com/2073-4344/16/11/948},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Advanced HKUST/MWCNT/Cellulose Acetate Hybrid Support for β-Glucosidase Immobilization: Enhanced Stability, Catalytic Performance, and Reusability
AU - Naif Abdullah R. Almalki
AU - Hamed Alsufyani
AU - Hayam A. Alwabsi
AU - Yaaser Q. Almulaiky
PY - 2026
DA - 2026/10/24
JO - Catalysts
DO - 10.3390/catal16110948
UR - https://www.mdpi.com/2073-4344/16/11/948
AB - This study reports the fabrication of a ternary HKUST/MWCNT/CA hybrid support for the immobilization of β-glucosidase and the evaluation of its catalytic and stability properties. The support was prepared by integrating HKUST with multi-walled carbon nanotubes (MWCNTs) and cellulose acetate (CA), followed by enzyme immobilization through glutaraldehyde-mediated coupling. Structural and surface characterization by XRD, FTIR, SEM/EDX, BET, and zeta potential confirmed the successful formation of the hybrid matrix and subsequent enzyme loading. The immobilization yield reached 88%, indicating efficient enzyme attachment onto the support. Nonlinear Michaelis–Menten analysis showed an increase in apparent Km after immobilization, whereas the apparent Vmax remained comparable to that of the free enzyme, indicating preservation of substantial catalytic performance. The immobilized β-glucosidase exhibited enhanced tolerance toward non-optimal conditions, retaining higher activity over broader pH and temperature ranges than the free enzyme. Notably, the optimum temperature shifted from 50 °C for the free enzyme to 60 °C after immobilization. The immobilized preparation also demonstrated good operational stability, preserving about 74% of its initial activity after 10 cycles, and excellent storage stability, retaining nearly 79% activity after 30 days at 4 °C. These findings demonstrate that HKUST/MWCNT/CA is a promising support for developing robust and reusable β-glucosidase biocatalysts.
SN - 2073-4344
ER -