Tiarsa, Ezra Rheinsky and Yandri, Yandri and Suhartati, Tati and Satria, Heri and Irawan, Bambang and Hadi, Sutopo (2022) The Stability Improvement of Aspergillus fumigatus α-Amylase by Immobilization onto Chitin-Bentonite Hybrid. Biochemistry Research International, 2022.

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13. The Stability Improvement of Aspergillus fumigatus α-Amylase by__Immobilization onto Chitin-Bentonite Hybrid.pdf

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Official URL: https://www.hindawi.com/journals/bri/2022/5692438/


Enzyme immobilization is a powerful method to improve the stability, reuse, and enzymatic properties of enzymes. *e im- mobilization of the α-amylase enzyme from Aspergillus fumigatus on a chitin-bentonite (CB) hybrid has been studied to improve its stability. *erefore, this study aims to obtain the higher stability of α-amylase enzyme to reduce industrial costs. *e procedures were performed as follows: production, isolation, partial purification, immobilization, and characterization of the free and immobilized enzymes. *e CB hybrid was synthesized by bentonite, chitin, and glutaraldehyde as a cross-linker. *e free enzyme was immobilized onto CB hybrid using 0.1 M phosphate buffer pH 7.5. *e free and immobilized enzymes were characterized by optimum temperature, Michaelis constant (KM), maximum velocity (Vmax), thermal inactivation rate constant (ki), half-life (t1/2), and transformation of free energy because of denaturation (ΔGi). *e free enzyme has optimum temperature of 55°C, KM= 3.04 mg mL−1 substrate, Vmax = 10.90 μmolemL− 1 min− 1, ki = 0.0171 min−1, t1/2 = 40.53 min, and ΔGi= 104.47 kJ mole−1. Meanwhile, the immobilized enzyme has optimum temperature of 60°C, KM= 11.57 mg mL−1 substrate, Vmax= 3.37 μmolemL− 1 min− 1, ki= 0.0045 min−1, t1/2= 154.00 min, and ΔGi= 108.17 kJ mole−1. After sixth cycle of reuse, the residual activity of the immobilized enzyme was 38%. *e improvement in the stability of α-amylase immobilized on the CB hybrid based on the increase in half-life was four times of the free enzyme.

Item Type: Article
Subjects: Q Science > QD Chemistry
Divisions: Fakultas Matematika dan Ilmu Pengetahuan Alam (FMIPA) > Prodi Biologi
Depositing User: BAMBANG IR
Date Deposited: 06 Oct 2022 05:22
Last Modified: 06 Oct 2022 05:22
URI: http://repository.lppm.unila.ac.id/id/eprint/45551

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