Performance and Kinetic Study of Xylan Hydrolysis by Free and Immobilized Trichoderma Xylanase

Riadi, Lieke and Agustin, Yuana Elly and Ong, Lu ki and Hadiwijaya, Ferrent Auryn and Winot, Amelia and Gunawan, Edrea Adelia and Tambatjong, Jessica and Kok, Tjie (2023) Performance and Kinetic Study of Xylan Hydrolysis by Free and Immobilized Trichoderma Xylanase. In: Proceedings of the 4th International Conference on Informatics, Technology and Engineering 2023 (InCITE 2023), 14-15 September 2023, Yogyakarta.

[thumbnail of 125994422.pdf] PDF

Download (375kB)
Official URL / DOI:


Enzyme immobilization is essential for enhancing the stability and reusability of enzymes in various industrial processes. To improve its feasibility, efficient yet simple immobilization techniques were required to be explored with respect to enhance overall catalytic efficiency and/or operational performance. This study investigates the enzymatic hydrolysis of beechwood xylan using free and immobilized xylanase in a batch reaction system at 60°C, which was considered as damaging temperature for most enzymatic protein. Xylanase immobilization was carried out by direct adsorption of xylanase onto dry zeolite, which resulted in 92.70% efficiency. The experimental variables used in this study include pH levels (pH 5.0 and 6.0) and xylan concentrations at 1.00% (w/v), 1.50% (w/v), 2.00% (w/v), and 2.50% (w/v). The optimal process variables for xylan hydrolysis by free enzyme and immobilized enzyme were found to be at pH of 5.0 and xylan concentration of 2.50% (w/v). At the optimum condition, the concentration of xylose obtained at 40 min of hydrolysis was 4.82 mg/mL and 5.68 mg/mL for free and immobilized enzymes, respectively. The saturation constants (Km) were determined to be 19.12 mg/mL and 42.03 mg/mL for free and immobilized enzymes, respectively, while the maximum rates (vmax) were 1.92 mg/(mL.min) and 1.21 mg/(mL.min) for free and immobilized enzymes, respectively. The results of this study suggest that xylanase immobilization could improve enzyme stability at higher processing temperatures without changing its response to surrounding pH.

Item Type: Conference or Workshop Item (Paper)
Uncontrolled Keywords: Xylanase; Immobilization; Kinetic
Subjects: Q Science > QD Chemistry
Divisions: Faculty of Engineering > Department of Chemical Engineering
Depositing User: Eko Setiawan 194014
Date Deposited: 24 Apr 2024 06:35
Last Modified: 25 Apr 2024 02:01

Actions (login required)

View Item View Item