Enhanced Amylase Activity by Modulating Abiotic Factors and Enzyme Stability in the Thermophilic Bacterial Isolates
- 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.
DOI: https://doi.org/10.3844/ojbsci.2024.295.301
Copyright: © 2024 Anthoni Agustien, Denny Bendrianis, Feskaharny Alamsyah, Mufidhatul Muqarramah and Mifthahul Jannah. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Keywords
- Agitation
- Enzymes
- Optimization
- Stability
- Thermophilic Bacteria