Teuku M. Iqbalsyah, Frida Oesman, Nurlaila, Febriani
The search for novel enzymes from bacterial origin has always been in demand to discover those with better attributes for various industrial applications. A thermostable alkaline protease from newly isolated Geobacillus jabois was purified using ammonium sulfate precipitation and gel exclusion chromatography*producing a-50a kDa enzyme with 20-fold purity and 27% yield. The enzyme showed optimum activity at 70°C and pH 10 and was reasonably stable for 2a h at 70°C with the addition of 5a mM Ca2+. Inhibition by PSMF and EDTA indicated that the enzyme was a serine protease. The KM and Vmax of the enzyme were 9.8 x 10-1 mM and 6.8 x 10-1 mM/s, respectively. The calculated Kcat and Kcat/KM were 1.4 x 102 /s and 1.5 x 102 /mM.s, respectively. A comparison with other Kcat/KM values in the Braunschweig Enzyme Database (BRENDA) indicated that the enzyme is more efficient than most subtilisin family members. Further studies to increase the stability would make the protease from G. jabois a distinct enzyme with application in industries that require high temperature and alkaline conditions. © 2023 Author(s).
Biomolecules Application Research Group, Chemistry Department, Faculty of Mathematics and Natural Sciences, Universitas Syiah Kuala, Banda Aceh, 23111, Indonesia
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