Proceedings of selected papers of International Conference on Health, Science, and Environment (ICHSE 2023)

The Improvement of α-Amylase Enzyme Stability from Aspergillus fumigatus through Immobilization Method Using Hybrid Zeolite/Chitin Matrix

Authors
Ella Gita Silviana1, Yandri Yandri2, *, Tati Suhartati2, Bambang Irawan3, Sutopo Hadi2
1Postgraduate Student of Chemistry, Faculty of Mathematics and Natural Sciences, University of Lampung, Bandar Lampung, 35145, Indonesia
2Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Lampung, Bandar Lampung, 35145, Indonesia
3Department of Biology, Faculty of Mathematics and Natural Sciences, University of Lampung, Bandar Lampung, 35145, Indonesia
*Corresponding author. Email: yandri.as@fmipa.unila.ac.id
Corresponding Author
Yandri Yandri
Available Online 30 May 2024.
DOI
10.2991/978-94-6463-431-0_16How to use a DOI?
Keywords
Immobilization; α-amylase enzyme; Aspergillus fumigatus; hybrid zeolite/chitin matrix
Abstract

The stability of enzymes against pH and temperature is an important factor in the industry. Generally, enzymes can work on physiological conditions and unresistant to extreme pH and temperature conditions. To be used in industry, it is necessary to enhance enzyme stability. This research aims to enhance the stability of the α-amylase enzyme from Aspergillus fumigatus through immobilization using a hybrid matrix of zeolite and chitin. The α-amylase enzyme was isolated by centrifugation and purified using ammonium sulfate precipitation and dialysis. The purified α-amylase has an optimum temperature of 50℃ and an optimum pH of 6, while the immobilized α-amylase has an optimum temperature of 60℃ and an optimum pH of 5. The residual activity of the purified α-amylase after being incubated for 100 minutes at 50℃ was 17.08%, whereas the immobilized α-amylase after being incubated at 60℃ retained a residual activity of 67.30%. The purified α-amylase has a half-life (t½) of 37.067 minutes ± 0.000, while the immobilized α-amylase has a t½ of 173.287 minutes ± 0.000. The immobilized α-amylase from A. fumigatus using the hybrid zeolite/chitin matrix has better stability compared to the purified α-amylase; this is proved by a 4.68-fold increase in t½ compared to the purified enzyme. The immobilized enzyme still retained 47.54% residual activity after being used for six repeated cycles.

Copyright
© 2024 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.

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Volume Title
Proceedings of selected papers of International Conference on Health, Science, and Environment (ICHSE 2023)
Series
Advances in Biological Sciences Research
Publication Date
30 May 2024
ISBN
978-94-6463-431-0
ISSN
2468-5747
DOI
10.2991/978-94-6463-431-0_16How to use a DOI?
Copyright
© 2024 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  - Ella Gita Silviana
AU  - Yandri Yandri
AU  - Tati Suhartati
AU  - Bambang Irawan
AU  - Sutopo Hadi
PY  - 2024
DA  - 2024/05/30
TI  - The Improvement of α-Amylase Enzyme Stability from Aspergillus fumigatus through Immobilization Method Using Hybrid Zeolite/Chitin Matrix
BT  - Proceedings of selected papers of International Conference on Health, Science, and Environment (ICHSE 2023)
PB  - Atlantis Press
SP  - 147
EP  - 162
SN  - 2468-5747
UR  - https://doi.org/10.2991/978-94-6463-431-0_16
DO  - 10.2991/978-94-6463-431-0_16
ID  - Silviana2024
ER  -