Partial Purification and Characterization of Pectinase From Actinomycete : Nocardiopsis Dasnonivelli Isolated From Marine Samples

Partial Purification and Characterization of Pectinase From Actinomycete : Nocardiopsis Dasnonivelli Isolated From Marine Samples | 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 Partial Purification and Characterization of Pectinase From Actinomycete : Nocardiopsis Dasnonivelli Isolated From Marine Samples Vaddadi Suman, N. M Yugandhar This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-3922915/v1 This work is licensed under a CC BY 4.0 License Status: Under Review Version 1 posted 3 You are reading this latest preprint version Abstract Biocatalysis, one of the oldest technologies, is becoming a favorable alternative to chemical processes and a vital part of green technology. This study was to purification and characterization of the pectinase. The extracted enzyme was subjected to partial purification which include ammonium sulphate precipitation, dialysis, sephadex G-100 column chromatography. The cell free supernatant pectinase activity was found to be in the 20% salt saturation fraction. Enzyme activity of pectinase increased from 75.9 ± 0.15U/mL to 81.08 ± 1.06 U/mL at 20% salt saturation fraction. As a result, the 20% ammonium sulphate fraction of crude enzyme extract was further analysed for purification of potential pectinase. Pectinase from the 20% ammonium sulphate crude enzyme fraction was purified by using sephadex-G-100 gel chromatography. From these results, the purified pectinase exhibited 85.83 ± 16 U/ml of enzyme activity. It was observed that the purification of pectinase by sephadex-G-100 gel chromatography increased its activity by 11.51%. The purified pectinase when subjected to SDS PAGE appeared as a single homogenous band with a molecular weight of 40 kDa. Partially purified enzyme was characterized, the enzyme was stable 50C upto 80 min at pH 9. Later the purified 40KDa protein spot of Nocardiopsis dassonvillei S10 was identified as pectinase by Peptide mass fingerprinting. PMF results of the protein spot was matched with Bacillus subtilis Mutant which is having highest score i.e. 63.4.Protein 3D structure models were predicted and validated by the Ramchandran plot assessment and the functional prediction was done by I-TASSER server. Enzymes ammonium sulphate precipitation dialysis sephadex G-100 column chromatography Full Text Additional Declarations No competing interests reported. Cite Share Download PDF Status: Under Review Version 1 posted Editor assigned by journal 06 Feb, 2024 Submission checks completed at journal 06 Feb, 2024 First submitted to journal 03 Feb, 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. 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-3922915","acceptedTermsAndConditions":true,"allowDirectSubmit":false,"archivedVersions":[],"articleType":"Research Article","associatedPublications":[],"authors":[{"id":271394934,"identity":"665689d9-c9ec-44e5-86b8-e7e821faaa63","order_by":0,"name":"Vaddadi Suman","email":"data:image/png;base64,iVBORw0KGgoAAAANSUhEUgAAAZAAAAAyAQMAAABI0h/eAAAABlBMVEX///8AAABVwtN+AAAACXBIWXMAAA7EAAAOxAGVKw4bAAAA7ElEQVRIiWNgGAWjYHACAwkGNgkI8wMQs7GTooVxBkgLM3FaICxmHjBJSP3xwxtv/CizsDe4dvjZY5tf2+T5mBkYP3zMwaPlTFqxZc85icQNt9PMjXP7bhu2MTMwS87chluLZEOOmQRvm0SCwe0EM+ncntuMQC1szLz4tPS/MZP82yZhb3A7/Zu0Zc9te4Ja+CVyzKSBtjBuuA1kMPy4nUiElmfF1jJAv8y8nVMm2dtwO7mNmbEZr1/Y+JM33nxTVmfPdzt9m8SPP7dt57c3H/zwEY8WVMDYBiYbiFUPAn9IUTwKRsEoGAUjBQAADqBM3Q82+EIAAAAASUVORK5CYII=","orcid":"","institution":"Andhra University","correspondingAuthor":true,"prefix":"","firstName":"Vaddadi","middleName":"","lastName":"Suman","suffix":""},{"id":271394935,"identity":"91e544a3-ec66-4655-8d13-16c1721f8799","order_by":1,"name":"N. 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