Research Article Open Access

Enhanced Amylase Activity by Modulating Abiotic Factors and Enzyme Stability in the Thermophilic Bacterial Isolates

Anthoni Agustien1, Denny Bendrianis1, Feskaharny Alamsyah1, Mufidhatul Muqarramah1 and Mifthahul Jannah1
  • 1 Department of Biology, Faculty of Mathematics and Natural Sciences, Universitas Andalas, Padang, Indonesia

Abstract

Amylase is one of the enzymes that is widely used in bioprocess technology, amylase from different microbial sources also varies in form, so it is suitable for its specific application. The purpose of this study was to determine the optimum temperature, pH, agitation, and stability of the amylase enzyme from two thermophilic bacterial isolates, TUA-07 and TUA-09. This study used a descriptive and an experimental method with a factorial Completely Randomized Design (CRD) with two factors, namely temperature and pH, followed by gradual agitation. The results showed that the optimum temperature, pH, and agitation for isolate TUA-07 was 80°C- pH 6, with the agitation of 125 rpm, while for isolate TUA-09 it was 50°C- pH 7 with the agitation of 125 rpm. Enzyme stability for isolate TUA-07 the amylase activity is 80% stable for 10 h, while for isolate TUA-09 the amylase activity is 80% stable for 8 h.

OnLine Journal of Biological Sciences
Volume 24 No. 2, 2024, 295-301

DOI: https://doi.org/10.3844/ojbsci.2024.295.301

Submitted On: 22 November 2023 Published On: 7 February 2024

How to Cite: Agustien, A., Bendrianis, D., Alamsyah, F., Muqarramah, M. & Jannah, M. (2024). Enhanced Amylase Activity by Modulating Abiotic Factors and Enzyme Stability in the Thermophilic Bacterial Isolates. OnLine Journal of Biological Sciences, 24(2), 295-301. https://doi.org/10.3844/ojbsci.2024.295.301

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Keywords

  • Agitation
  • Enzymes
  • Optimization
  • Stability
  • Thermophilic Bacteria