Immobilization of Purified α-Amylase from Aspergillus fumigatus on a Chitosan–Silica Gel 60 Hybrid: Enhanced Thermal Stability and Reusability

Santalum Alba; Yandri Yandri; Tati Suhartati; Bambang Irawan; Stevenson Waruwu

doi:10.9767/bcrec.20874

DOI: https://doi.org/10.9767/bcrec.20874

Immobilization of Purified α-Amylase from Aspergillus fumigatus on a Chitosan–Silica Gel 60 Hybrid: Enhanced Thermal Stability and Reusability

Santalum Alba¹

, Yandri Yandri²

, Tati Suhartati²

, Bambang Irawan³

, Stevenson Waruwu⁴

¹Department of Cosmetic Engineering, Faculty of Industrial Technology, Institut Teknologi Sumatera, South Lampung 35365, 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

⁴ Postgraduate Program in Chemistry, Faculty of Mathematics and Natural Sciences, University of Lampung, Bandar Lampung 35145, Indonesia

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Received: 2 Oct 2026; Revised: 2 Nov 2026; Accepted: 2 Nov 2026; Available online: 6 Nov 2026; Published: 30 Apr 2027.

Editor(s): Istadi Istadi

This work is licensed under a Creative Commons Attribution-ShareAlike 4.0 International License.

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@article{BCREC20874,
    author = {Santalum Alba and Yandri Yandri and Tati Suhartati and Bambang Irawan and Stevenson Waruwu},
    title = {Immobilization of Purified α-Amylase from Aspergillus fumigatus on a Chitosan–Silica Gel 60 Hybrid: Enhanced Thermal Stability and Reusability},
    journal = {Bulletin of Chemical Reaction Engineering & Catalysis},
  volume = {22},
    number = {1},
    year = {2027},
    keywords = {α-Amylase; Aspergillus fumigatus; chitosan–silica gel hybrid; immobilization; thermal stability},
    abstract = {Free α-amylase is readily inactivated at high temperatures and cannot be recovered after starch hydrolysis, which limits its industrial use. Hybrid supports can combine the advantages of their components, but a chitosan–silica gel 60 hybrid has not been reported for  Aspergillus fumigatus  α-amylase. This study aimed to compare the catalytic properties, thermal inactivation kinetics, and reusability of  A. fumigatus  α-amylase immobilized on silica gel 60, chitosan, and a chitosan–silica gel 60 hybrid. The enzyme was purified by (30–90)% ammonium sulfate fractionation and dialysis, increasing its specific activity from 702.23 to 3449.43 U/mg (4.9-fold). The hybrid, synthesized with glutaraldehyde as a cross-linker, showed the FT-IR bands of both components with wavenumber shifts, indicating their interaction. The enzyme was immobilized by physical adsorption at an optimum binding pH of 5.0 on all matrices. Immobilization raised the optimum temperature from 50 to 55 °C, increased  K  M  from 3.48 to 4.62–5.80 mg mL −1 , and decreased  V  max  from 12.97 to 2.72–3.73 μmol mL −1  min −1 . After 80 min at 60 °C, the purified enzyme retained 24.8% of its activity, whereas the enzyme immobilized on silica gel 60, chitosan, and the hybrid retained 77.3, 55.1, and 81.1%, respectively. The enzyme–hybrid had the longest half-life (260.85 min; a 6.5-fold increase), the highest free energy of inactivation (109.62 kJ mol −1 ), and the highest residual activity after six reuse cycles (57%). The chitosan–silica gel 60 hybrid is therefore a more effective support than either of its components for stabilizing and reusing α-amylase.},
   issn = {1978-2993},   pages = {55--68}  doi = {10.9767/bcrec.20874},
    url = {https://journal.bcrec.id/index.php/bcrec/article/view/20874}
}

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Abstract

Free α-amylase is readily inactivated at high temperatures and cannot be recovered after starch hydrolysis, which limits its industrial use. Hybrid supports can combine the advantages of their components, but a chitosan–silica gel 60 hybrid has not been reported for Aspergillus fumigatus α-amylase. This study aimed to compare the catalytic properties, thermal inactivation kinetics, and reusability of A. fumigatus α-amylase immobilized on silica gel 60, chitosan, and a chitosan–silica gel 60 hybrid. The enzyme was purified by (30–90)% ammonium sulfate fractionation and dialysis, increasing its specific activity from 702.23 to 3449.43 U/mg (4.9-fold). The hybrid, synthesized with glutaraldehyde as a cross-linker, showed the FT-IR bands of both components with wavenumber shifts, indicating their interaction. The enzyme was immobilized by physical adsorption at an optimum binding pH of 5.0 on all matrices. Immobilization raised the optimum temperature from 50 to 55 °C, increased K_M from 3.48 to 4.62–5.80 mg mL⁻¹, and decreased V_max from 12.97 to 2.72–3.73 μmol mL⁻¹ min⁻¹. After 80 min at 60 °C, the purified enzyme retained 24.8% of its activity, whereas the enzyme immobilized on silica gel 60, chitosan, and the hybrid retained 77.3, 55.1, and 81.1%, respectively. The enzyme–hybrid had the longest half-life (260.85 min; a 6.5-fold increase), the highest free energy of inactivation (109.62 kJ mol⁻¹), and the highest residual activity after six reuse cycles (57%). The chitosan–silica gel 60 hybrid is therefore a more effective support than either of its components for stabilizing and reusing α-amylase.

Supporting Information (SI) PDF

Keywords: α-Amylase; Aspergillus fumigatus; chitosan–silica gel hybrid; immobilization; thermal stability

Funding: The authors are grateful to the Ministry of Education, Culture, Research and Technology of the Republic of Indonesia for funding this study under the Basic Research 2023 scheme (contract nos. 027/E5/PG.02.00.PL/2023, dated 12 April 2023, and 2192/UN26.21/

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In 2027: BCREC Volume 22 Issue 1 Year 2027 (April 2027) (Issue in Progress)

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