Characterization of Crude Cellulase Produced by Bacillus licheniformis OE-1 from the Diyadin Hot Springs, Ağrı Province

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Abstract In this study, we characterized the crude cellulase produced by Bacillus licheniformis OE-1, a strain isolated from the thermal springs of Diyadin District (Ağrı Province, Turkey) and examined the effects of various compounds on its activity. The enzyme exhibited an optimum activity at 60 °C and pH 9.0. Using carboxymethyl cellulose (CMC) as the substrate, the enzyme displayed a Vmax of 2.33 U mL⁻¹ and a Km of 0.0348 mM. When the effects of EDTA, KCl, MgSO 4 , KI, and SDS compounds on the cellulase enzyme were investigated, it was observed that these compounds inhibit the enzyme. By plotting a Lineweaver-Burk graph, the IC 50 values of these compounds were calculated, and the inhibition types were determined.
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Characterization of Crude Cellulase Produced by Bacillus licheniformis OE-1 from the Diyadin Hot Springs, Ağrı Province | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Research Article Characterization of Crude Cellulase Produced by Bacillus licheniformis OE-1 from the Diyadin Hot Springs, Ağrı Province Osman Eren, Halis Şakiroğlu This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-8729286/v1 This work is licensed under a CC BY 4.0 License Status: Published Journal Publication published 09 Apr, 2026 Read the published version in International Microbiology → Version 1 posted 10 You are reading this latest preprint version Abstract In this study, we characterized the crude cellulase produced by Bacillus licheniformis OE-1, a strain isolated from the thermal springs of Diyadin District (Ağrı Province, Turkey) and examined the effects of various compounds on its activity. The enzyme exhibited an optimum activity at 60 °C and pH 9.0. Using carboxymethyl cellulose (CMC) as the substrate, the enzyme displayed a Vmax of 2.33 U mL⁻¹ and a Km of 0.0348 mM. When the effects of EDTA, KCl, MgSO 4 , KI, and SDS compounds on the cellulase enzyme were investigated, it was observed that these compounds inhibit the enzyme. By plotting a Lineweaver-Burk graph, the IC 50 values of these compounds were calculated, and the inhibition types were determined. Full Text Additional Declarations No competing interests reported. Cite Share Download PDF Status: Published Journal Publication published 09 Apr, 2026 Read the published version in International Microbiology → Version 1 posted Editorial decision: Revision requested 04 Mar, 2026 Reviews received at journal 17 Feb, 2026 Reviewers agreed at journal 13 Feb, 2026 Reviewers agreed at journal 13 Feb, 2026 Reviews received at journal 12 Feb, 2026 Reviewers agreed at journal 11 Feb, 2026 Reviewers invited by journal 11 Feb, 2026 Editor assigned by journal 11 Feb, 2026 Submission checks completed at journal 05 Feb, 2026 First submitted to journal 29 Jan, 2026 You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. We do this by developing innovative software and high quality services for the global research community. Our growing team is made up of researchers and industry professionals working together to solve the most critical problems facing scientific publishing. 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