Selection of the Compromised Operating Condition of a One-pot Multi-enzymatic Reaction Using Individually Immobilised Enzymes: Production of Lactofructose Syrup

Selection of the Compromised Operating Condition of a One-pot Multi-enzymatic Reaction Using Individually Immobilised Enzymes: Production of Lactofructose Syrup | 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 Selection of the Compromised Operating Condition of a One-pot Multi-enzymatic Reaction Using Individually Immobilised Enzymes: Production of Lactofructose Syrup Camila Clavero, Paulina Urrutia, Raúl Conejeros, Oscar Romero, and 1 more This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-4844667/v1 This work is licensed under a CC BY 4.0 License Status: Under Review Version 1 posted 11 You are reading this latest preprint version Abstract We selected a compromised operating condition (temperature and pH) in a one-pot multienzyme system by considering the stability and initial reaction rate of the catalysts in a single parameter (catalytic potential). The production of lactose-fructose syrup (LFS) was used as model of a multi-enzymatic system. The enzymes used were β-galactosidase (β-gal), extracted from Bifidobacterium bifidum , which was previously immobilised and commercially immobilised glucose isomerase (GI). The compromised catalytic potential for both enzymes was obtained at a temperature of 50 °C and pH of 6.5, with a catalytic potential of 19,034.9 μmol g -1 for β-gal and 1,894.7 μmol g -1 for GI. Under these conditions, the initial reaction rate of β-gal was 100% and GI was 20%, whereas the half-life was 25 h and 300 h for β-gal and GI, respectively. After 20 batches (equivalent to 40 h of operation), no significant productivity losses were detected (less than 10 %). The average productivity of the first five batches was 0.111 g fructose ‧h -1 , whereas that of the last five batches was 0.106 g fructose ‧h -1 . These results showed the applicability of the catalytic potential as a tool for selecting the operating conditions in a process where two or more enzymes work simultaneously. β-galactosidase glucose isomerase one-pot catalytic potential compromise operating conditions. Full Text Additional Declarations No competing interests reported. Supplementary Files SUPPLEMENTARYDATA.docx Cite Share Download PDF Status: Under Review Version 1 posted Editorial decision: Revision requested 26 Aug, 2024 Reviews received at journal 24 Aug, 2024 Reviews received at journal 22 Aug, 2024 Reviewers agreed at journal 14 Aug, 2024 Reviewers agreed at journal 10 Aug, 2024 Reviewers agreed at journal 07 Aug, 2024 Reviewers agreed at journal 07 Aug, 2024 Reviewers invited by journal 07 Aug, 2024 Editor assigned by journal 06 Aug, 2024 Submission checks completed at journal 04 Aug, 2024 First submitted to journal 01 Aug, 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. 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Also discoverable on Platform About Our Team In Review Editorial Policies Advisory Board Help Center Resources Author Services Accessibility API Access RSS feed Manage Cookie Preferences © Research Square 2026 | ISSN 2693-5015 (online) Privacy Policy Terms of Service Do Not Sell My Personal Information {"props":{"pageProps":{"initialData":{"identity":"rs-4844667","acceptedTermsAndConditions":true,"allowDirectSubmit":false,"archivedVersions":[],"articleType":"Research Article","associatedPublications":[],"authors":[{"id":345029220,"identity":"80e294a0-9124-4d98-85ce-e8e791d7485b","order_by":0,"name":"Camila Clavero","email":"","orcid":"","institution":"Pontificial Catholic University of Valparaiso","correspondingAuthor":false,"prefix":"","firstName":"Camila","middleName":"","lastName":"Clavero","suffix":""},{"id":345029221,"identity":"d7836dff-1a2d-4ac7-bed7-3ac6f888ab4c","order_by":1,"name":"Paulina Urrutia","email":"","orcid":"","institution":"Pontificial Catholic University of 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The production of lactose-fructose syrup (LFS) was used as model of a multi-enzymatic system. The enzymes used were β-galactosidase (β-gal), extracted from \u003cem\u003eBifidobacterium bifidum\u003c/em\u003e, which was previously immobilised and commercially immobilised glucose isomerase (GI).\u003c/p\u003e\n\u003cp\u003eThe compromised catalytic potential for both enzymes was obtained at a temperature of 50 °C and pH of 6.5, with a catalytic potential of 19,034.9 μmol g\u003csup\u003e-1\u003c/sup\u003e for β-gal and 1,894.7 μmol g\u003csup\u003e-1\u003c/sup\u003e for GI. Under these conditions, the initial reaction rate of β-gal was 100% and GI was 20%, whereas the half-life was 25 h and 300 h for β-gal and GI, respectively. After 20 batches (equivalent to 40 h of operation), no significant productivity losses were detected (less than 10 %). 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