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<p>The exploration of extreme environments offers significant potential for discovering enzymes that may be suitable for demanding industrial conditions. In this study, we characterized the crude cellulase produced by the <i>Bacillus licheniformis</i> OE-1 strain, isolated from the thermal springs of Diyadin (Ağrı Province, Turkey). The inherent adaptation of this strain to extreme habitats suggests a potential for enzymatic stability. The enzyme exhibited its optimal activity at 60&#xa0;°C and pH 9.0, indicating its potential for application in certain high temperature and alkaline based processes. Using carboxymethyl cellulose as a substrate, the enzyme displayed a Vmax of 2.29 U mL⁻¹ and a Km of 0.1691&#xa0;mg/mL. The effects of various compounds on the enzyme were investigated; IC<sub>50</sub> values were calculated from dose-response curves, and inhibition types were preliminarily identified using Lineweaver-Burk plots. EDTA, MgSO<sub>4</sub> and KI were found to be uncompetitive inhibitors, while KCl and SDS exhibited non-competitive inhibition. This research highlights the potential of the Diyadin geothermal ecosystem as a candidate source for biocatalysts that may contribute to industrial sustainability.</p>

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Characterization of crude cellulase produced by Bacillus licheniformis OE-1 from the Diyadin hot springs, Ağrı Province

  • 期刊论文

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  • 发表日期：

    2026年4月10日

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  • Osman Eren,
  • Halis Sakiroglu

摘要

The exploration of extreme environments offers significant potential for discovering enzymes that may be suitable for demanding industrial conditions. In this study, we characterized the crude cellulase produced by the Bacillus licheniformis OE-1 strain, isolated from the thermal springs of Diyadin (Ağrı Province, Turkey). The inherent adaptation of this strain to extreme habitats suggests a potential for enzymatic stability. The enzyme exhibited its optimal activity at 60 °C and pH 9.0, indicating its potential for application in certain high temperature and alkaline based processes. Using carboxymethyl cellulose as a substrate, the enzyme displayed a Vmax of 2.29 U mL⁻¹ and a Km of 0.1691 mg/mL. The effects of various compounds on the enzyme were investigated; IC50 values were calculated from dose-response curves, and inhibition types were preliminarily identified using Lineweaver-Burk plots. EDTA, MgSO4 and KI were found to be uncompetitive inhibitors, while KCl and SDS exhibited non-competitive inhibition. This research highlights the potential of the Diyadin geothermal ecosystem as a candidate source for biocatalysts that may contribute to industrial sustainability.