Recombinant Esterase (BaCEm) Immobilized on Polyethyleneimine-Loaded Mesoporous Silica SBA-15 Exhibits Outstanding Catalytic Performance

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Recombinant Esterase (BaCEm) Immobilized on Polyethyleneimine-Loaded Mesoporous Silica SBA-15 Exhibits Outstanding Catalytic Performance | 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 Recombinant Esterase (BaCEm) Immobilized on Polyethyleneimine-Loaded Mesoporous Silica SBA-15 Exhibits Outstanding Catalytic Performance Hongjun Zhang, Yichao Li, Litian Wei, Zhao Wang, Yinjun zhang This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-4477121/v1 This work is licensed under a CC BY 4.0 License Status: Published Journal Publication published 02 Sep, 2024 Read the published version in Applied Biochemistry and Biotechnology → Version 1 posted 5 You are reading this latest preprint version Abstract A recombinant esterase, BaCE m , derived from Bacillus aryabhattai and heterologously expressed in Escherichia coli , was successfully immobilized on polyethyleneimine-impregnated mesoporous silica SBA-15. This immobilization utilized glutaraldehyde as a crosslinker. Optimal conditions were established with a PEI/SBA-15 ratio of 25% (w/w), a pH of 7.5, and a glutaraldehyde concentration of 0.5% (w/w), resulting in a loading capacity of 76.4 mg/g, a recovery activity of 43.5%, and a specific activity of 7917 U/g for BaCE m . The immobilized BaCE m demonstrated high enantioselectivity, with an 'E' value of 203.92, in the resolution assay of ( R , S )-ethyl indoline-2-carboxylate. Notably, the immobilized enzyme, compared to its free counterpart, exhibited enhanced thermostability, maintaining 95.4% of its activity after 3 hours at 30°C. It also showed significant tolerance to organic solvents, retaining 48.4% and 28.7% residual activity in 10% v/v acetonitrile and acetone, respectively. Moreover, its storage stability was confirmed, with 68.5% residual activity preserved after 30 days at 4°C. Remarkably, the immobilized BaCE m retained 58.1% of its activity after 10 reuse cycles, underscoring the potential of polyethyleneimine-impregnated mesoporous silica SBA-15 as an effective support for enzyme immobilization, promising for industrial applications. Esterase Immobilization Mesoporous silica SBA-15 Polyethyleneimine Biocatalysis Full Text Cite Share Download PDF Status: Published Journal Publication published 02 Sep, 2024 Read the published version in Applied Biochemistry and Biotechnology → Version 1 posted Editorial decision: Accept with revisions 15 Jul, 2024 Reviewers agreed at journal 27 Jun, 2024 Reviewers invited by journal 21 Jun, 2024 Editor invited by journal 28 May, 2024 First submitted to journal 27 May, 2024 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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