Proceedings of the 4th International Conference on Informatics, Technology and Engineering 2023 (InCITE 2023)

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

Authors
Lieke Riadi1, *, Yuana Elly Agustin1, Lu Ki Ong1, Ferrent Auryn Hadiwijaya1, Amelia Winoto1, Edrea Adelia Gunawan1, Jessica Tambatjong1, Tjie Kok1
1University of Surabaya, Surabaya, 60284, Indonesia
*Corresponding author. Email: lieke@staff.ubaya.ac.id
Corresponding Author
Lieke Riadi
Available Online 19 November 2023.
DOI
10.2991/978-94-6463-288-0_7How to use a DOI?
Keywords
Xylanase; Immobilization; Kinetic
Abstract

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.

Copyright
© 2023 The Author(s)
Open Access
Open Access This chapter is licensed under the terms of the Creative Commons Attribution-NonCommercial 4.0 International License (http://creativecommons.org/licenses/by-nc/4.0/), which permits any noncommercial use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license and indicate if changes were made.

Download article (PDF)

Volume Title
Proceedings of the 4th International Conference on Informatics, Technology and Engineering 2023 (InCITE 2023)
Series
Atlantis Highlights in Engineering
Publication Date
19 November 2023
ISBN
978-94-6463-288-0
ISSN
2589-4943
DOI
10.2991/978-94-6463-288-0_7How to use a DOI?
Copyright
© 2023 The Author(s)
Open Access
Open Access This chapter is licensed under the terms of the Creative Commons Attribution-NonCommercial 4.0 International License (http://creativecommons.org/licenses/by-nc/4.0/), which permits any noncommercial use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license and indicate if changes were made.

Cite this article

TY  - CONF
AU  - Lieke Riadi
AU  - Yuana Elly Agustin
AU  - Lu Ki Ong
AU  - Ferrent Auryn Hadiwijaya
AU  - Amelia Winoto
AU  - Edrea Adelia Gunawan
AU  - Jessica Tambatjong
AU  - Tjie Kok
PY  - 2023
DA  - 2023/11/19
TI  - Performance and Kinetic Study of Xylan Hydrolysis by Free and Immobilized Trichoderma Xylanase
BT  - Proceedings of the 4th International Conference on Informatics, Technology and Engineering 2023 (InCITE 2023)
PB  - Atlantis Press
SP  - 62
EP  - 68
SN  - 2589-4943
UR  - https://doi.org/10.2991/978-94-6463-288-0_7
DO  - 10.2991/978-94-6463-288-0_7
ID  - Riadi2023
ER  -