{"id":{"repo_id":"etsu","oai_identifier":"oai:dc.etsu.edu:etd-2401"},"canonical_url":"https://search.dev.ndltd.org/etd/etsu/oai:dc.etsu.edu:etd-2401","repository":{"repo_id":"etsu","name":"East Tennessee State University","base_url":"https://dc.etsu.edu/do/oai/"},"display":{"title":"Cloning, Expression, and Biochemical Characterization of Recombinant Putative Glucosyltransferases Clone 3 and 8 from Grapefruit (Citrus paradisi)","abstract":"<p>The grapefruit plant, <em>Citrus paradisi</em>, tends to accumulate high levels of flavonoid glycosides such as flavanones and flavones. Flavonoids have a vast array of important functions in plants and also in humans. Glucosyltransferases (GTs) are enzymes responsible for glucosylation reactions. In our pursuit to study the structure and function of flavonoid GTs, we have used molecular approaches to identify, clone, express, and functionally characterize the enzymes. This research was designed to test the hypothesis that PGT3 is a flavonoid glucosyltransferase and is subject to biochemical regulation. PGT3 has been tested for GT activity with compounds representing subclasses of flavonoids as well as some simple phenolics. Results indicate GT activity with 6 substrates, p-hydroxybenzoic acid, vanillin, vanillic acid, p-hydroxyphenylpyruvate, gentisic acid, and catechol. A second project designed to clone putative PGT8 into the Pichia expression system has been completed.</p>","abstract_html":"&lt;p&gt;The grapefruit plant, &lt;em&gt;Citrus paradisi&lt;/em&gt;, tends to accumulate high levels of flavonoid glycosides such as flavanones and flavones. Flavonoids have a vast array of important functions in plants and also in humans. Glucosyltransferases (GTs) are enzymes responsible for glucosylation reactions. In our pursuit to study the structure and function of flavonoid GTs, we have used molecular approaches to identify, clone, express, and functionally characterize the enzymes. This research was designed to test the hypothesis that PGT3 is a flavonoid glucosyltransferase and is subject to biochemical regulation. PGT3 has been tested for GT activity with compounds representing subclasses of flavonoids as well as some simple phenolics. Results indicate GT activity with 6 substrates, p-hydroxybenzoic acid, vanillin, vanillic acid, p-hydroxyphenylpyruvate, gentisic acid, and catechol. A second project designed to clone putative PGT8 into the Pichia expression system has been completed.&lt;/p&gt;","abstract_has_math":false,"creators":["Hayford, Deborah"],"institution":null,"degree_name":"MS (Master of Science)","degree_level":"Thesis - unrestricted","degree_discipline":"Biology","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2012,"date_issued":"2012-05-01T07:00:00Z","date_published":"2012-05-01T07:00:00Z","updated_at":"2026-07-24T02:20:06Z","subjects":["Glucosyltransferase","Flavonoids","Citrus paradisi","Phenolics","Inclusion Bodies","Biology","Life Sciences"],"languages":[],"rights":["Copyright by the authors."],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://dc.etsu.edu/etd/1215","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Hayford, Deborah"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2014-07-01T07:00:00Z"]},{"key":"dc:date.issued","label":"Date","values":["2012-05-01T07:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis - unrestricted"]},{"key":"thesis:degree_name","label":"Degree Name","values":["MS (Master of Science)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Glucosyltransferase","Flavonoids","Citrus paradisi","Phenolics","Inclusion Bodies","Biology","Life Sciences"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:rights","label":"Dc Rights","values":["Copyright by the authors."]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://dc.etsu.edu/context/etd/article/2401/viewcontent/HayfordD041212f.pdf","https://dc.etsu.edu/etd/1215"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["<p>The grapefruit plant, <em>Citrus paradisi</em>, tends to accumulate high levels of flavonoid glycosides such as flavanones and flavones. Flavonoids have a vast array of important functions in plants and also in humans. Glucosyltransferases (GTs) are enzymes responsible for glucosylation reactions. In our pursuit to study the structure and function of flavonoid GTs, we have used molecular approaches to identify, clone, express, and functionally characterize the enzymes. This research was designed to test the hypothesis that PGT3 is a flavonoid glucosyltransferase and is subject to biochemical regulation. PGT3 has been tested for GT activity with compounds representing subclasses of flavonoids as well as some simple phenolics. Results indicate GT activity with 6 substrates, p-hydroxybenzoic acid, vanillin, vanillic acid, p-hydroxyphenylpyruvate, gentisic acid, and catechol. A second project designed to clone putative PGT8 into the Pichia expression system has been completed.</p>"]},{"key":"dc:title","label":"Title","values":["Cloning, Expression, and Biochemical Characterization of Recombinant Putative Glucosyltransferases Clone 3 and 8 from Grapefruit (Citrus paradisi)"]}]}],"canonical_facts":{"dc:creator":["Hayford, Deborah"],"dc:date.available":["2014-07-01T07:00:00Z"],"dc:date.issued":["2012-05-01T07:00:00Z"],"dc:description.abstract":["<p>The grapefruit plant, <em>Citrus paradisi</em>, tends to accumulate high levels of flavonoid glycosides such as flavanones and flavones. Flavonoids have a vast array of important functions in plants and also in humans. Glucosyltransferases (GTs) are enzymes responsible for glucosylation reactions. In our pursuit to study the structure and function of flavonoid GTs, we have used molecular approaches to identify, clone, express, and functionally characterize the enzymes. This research was designed to test the hypothesis that PGT3 is a flavonoid glucosyltransferase and is subject to biochemical regulation. PGT3 has been tested for GT activity with compounds representing subclasses of flavonoids as well as some simple phenolics. Results indicate GT activity with 6 substrates, p-hydroxybenzoic acid, vanillin, vanillic acid, p-hydroxyphenylpyruvate, gentisic acid, and catechol. A second project designed to clone putative PGT8 into the Pichia expression system has been completed.</p>"],"dc:identifier":["https://dc.etsu.edu/context/etd/article/2401/viewcontent/HayfordD041212f.pdf","https://dc.etsu.edu/etd/1215"],"dc:rights":["Copyright by the authors."],"dc:subject":["Glucosyltransferase","Flavonoids","Citrus paradisi","Phenolics","Inclusion Bodies","Biology","Life Sciences"],"dc:title":["Cloning, Expression, and Biochemical Characterization of Recombinant Putative Glucosyltransferases Clone 3 and 8 from Grapefruit (Citrus paradisi)"],"thesis:degree_discipline":["Biology"],"thesis:degree_level":["Thesis - unrestricted"],"thesis:degree_name":["MS (Master of Science)"]},"updated_at":"2026-07-24T02:20:06Z"}