Febriani, Rayyana, Mildatul Ulya, F. Oesman, Akhmaloka, Teuku M. Iqbalsyah
Industrial demands for enzymes that are stable in a broad range of conditions are increasing. Such enzymes, one of which is α-amylase, could be produced by extremophiles. This study reports a thermostable α-amylase produced by a newly isolated Geobacillus sp. nov. from a geothermal area. The phylogenetic analysis of the 16S rRNA gene showed that the isolate formed a separate branch with 95% homology to Geobacillus sp. After precipitation using ammonium sulphate followed by ion-exchange chromatography, the enzyme produced a specific activity of 25.1 (U/mg) with a purity of 6.5-fold of the crude extract. The molecular weight of the enzyme was approximately 12.2 kDa. The optimum activity was observed at 75 °C and pH 8. The activity increased in the presence of Ba2+ and Fe2+ but decreased in the presence of K+ and Mg2+. Ca2+ and Mn2+ increased the activity slightly. The activity completely diminished with the addition of Cu2+. EDTA and PMSF also sharply reduced enzyme activity. Although the stability was moderate, the low molecular weight could be an important feature for its future applications. © 2019
Biomolecules Application Research Group, Chemistry Department, Faculty of Mathematics and Natural Sciences, Universitas Syiah Kuala, Banda Aceh, 23111, Indonesia; Biochemistry Research Group, Faculty of Mathematics and Natural Sciences, Institut Teknologi Bandung, Ganesha 10 Bandung, Indonesia
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