{"id":{"repo_id":"vt","oai_identifier":"oai:vtechworks.lib.vt.edu:10919/42889"},"canonical_url":"https://search.dev.ndltd.org/etd/vt/oai:vtechworks.lib.vt.edu:10919/42889","repository":{"repo_id":"vt","name":"Virginia Tech","base_url":"https://vtechworks.lib.vt.edu/oai/request"},"display":{"title":"The nature of sorbital (a primary) and sorbose (a secondary) dehydrogenases of Gluconobacter species","abstract":"The genus <i>Gluconobacter</i> is known to carry out limited oxidations using the NAD(P)-independent membrane-bound dehydrogenases in which the products are released back to the medium. Reports of further limited oxidations of these primary oxidation products by <i>Gluconobacter</i> in single step or sequential oxidations by secondary dehydrogenases are also published. The objective of this project was to evaluate the nature of one primary (sorbitol) dehydrogenase and one secondary (sorbose) dehydrogenase because of their importance in Vitamin C production. My hypotheses were that sorbitol (the primary) dehydrogenase is constitutive, while sorbose (the secondary) dehydrogenase is inducible. Six <i>Gluconobacter</i> strains from three different species grew on plates containing 50/0 sorbose, indicating their ability to oxidize sorbose thus possessing a secondary dehydrogenase. When four strains were tested for their ability to carry out the sequential oxidation of sorbitol and then sorbose on media containing growth-limiting sorbitol concentrations, three strains showed possible biphasic growth. However, thin layer chromatography of culture media did not support sequential sorbitol and sorbose oxidation. F erricyanide assays for sorbitol and sorbose dehydrogenases from membrane fractions isolated from cells grown on glycerol, sorbitol, or sorbose showed that sorbitol dehydrogenase activity in all four strains (three species) tested was always present (constitutive) and its specific activity was always enhanced by growth on sorbose. Membrane fractions showed no or very low constitutive sorbose dehydrogenase activity and no evidence that this secondary dehydrogenase was induced.","abstract_html":"The genus &lt;i&gt;Gluconobacter&lt;/i&gt; is known to carry out limited oxidations using the NAD(P)-independent membrane-bound dehydrogenases in which the products are released back to the medium. Reports of further limited oxidations of these primary oxidation products by &lt;i&gt;Gluconobacter&lt;/i&gt; in single step or sequential oxidations by secondary dehydrogenases are also published. The objective of this project was to evaluate the nature of one primary (sorbitol) dehydrogenase and one secondary (sorbose) dehydrogenase because of their importance in Vitamin C production. My hypotheses were that sorbitol (the primary) dehydrogenase is constitutive, while sorbose (the secondary) dehydrogenase is inducible. Six &lt;i&gt;Gluconobacter&lt;/i&gt; strains from three different species grew on plates containing 50/0 sorbose, indicating their ability to oxidize sorbose thus possessing a secondary dehydrogenase. When four strains were tested for their ability to carry out the sequential oxidation of sorbitol and then sorbose on media containing growth-limiting sorbitol concentrations, three strains showed possible biphasic growth. However, thin layer chromatography of culture media did not support sequential sorbitol and sorbose oxidation. F erricyanide assays for sorbitol and sorbose dehydrogenases from membrane fractions isolated from cells grown on glycerol, sorbitol, or sorbose showed that sorbitol dehydrogenase activity in all four strains (three species) tested was always present (constitutive) and its specific activity was always enhanced by growth on sorbose. Membrane fractions showed no or very low constitutive sorbose dehydrogenase activity and no evidence that this secondary dehydrogenase was induced.","abstract_has_math":false,"creators":["Anriany, Yuda Adha"],"institution":"Virginia Tech","degree_name":"Master of Science","degree_level":"masters","degree_discipline":"Biology","degree_department":"Biology","school":null,"contributors":[],"advisors":[],"committee_chairs":["Claus, George William"],"committee_members":["Yousten, Allan A.","Gregory, Eugene M."],"year":1996,"date_issued":"1996-09-17","date_published":"1996-09-17","updated_at":"2026-07-22T22:19:01Z","subjects":["noninducible","Gluconobacter","sorbital dehydrogenase","sorbase dehydrogenase","biphasic growth","constitutive"],"languages":["en"],"rights":["In Copyright"],"rights_urls":["http://rightsstatements.org/vocab/InC/1.0/"],"identifier_entries":[{"key":"dc:identifier.other","label":"Dc Identifier Other","values":["etd-06082009-170814"],"render_values":[{"text":"etd-06082009-170814","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/10919/42889","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.committeechair","label":"Committee Chair","values":["Claus, George William"]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Yousten, Allan A.","Gregory, Eugene M."]},{"key":"dc:contributor.department","label":"Department","values":["Biology"]},{"key":"dc:creator","label":"Author","values":["Anriany, Yuda Adha"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2014-03-14T21:37:04Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2014-03-14T21:37:04Z","2009-06-08"]},{"key":"dc:date.issued","label":"Date","values":["1996-09-17"]},{"key":"dc:publisher","label":"Institution","values":["Virginia Tech"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"dc:type.dcmitype","label":"Dc Type Dcmitype","values":["Text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["masters"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Virginia Polytechnic Institute and State University"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["noninducible","Gluconobacter","sorbital dehydrogenase","sorbase dehydrogenase","biphasic growth","constitutive"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["In Copyright"]},{"key":"dc:rights.uri","label":"Rights URI","values":["http://rightsstatements.org/vocab/InC/1.0/"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.other","label":"Dc Identifier Other","values":["etd-06082009-170814"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/10919/42889"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["The genus <i>Gluconobacter</i> is known to carry out limited oxidations using the NAD(P)-independent membrane-bound dehydrogenases in which the products are released back to the medium. Reports of further limited oxidations of these primary oxidation products by <i>Gluconobacter</i> in single step or sequential oxidations by secondary dehydrogenases are also published. The objective of this project was to evaluate the nature of one primary (sorbitol) dehydrogenase and one secondary (sorbose) dehydrogenase because of their importance in Vitamin C production. My hypotheses were that sorbitol (the primary) dehydrogenase is constitutive, while sorbose (the secondary) dehydrogenase is inducible. Six <i>Gluconobacter</i> strains from three different species grew on plates containing 50/0 sorbose, indicating their ability to oxidize sorbose thus possessing a secondary dehydrogenase. When four strains were tested for their ability to carry out the sequential oxidation of sorbitol and then sorbose on media containing growth-limiting sorbitol concentrations, three strains showed possible biphasic growth. However, thin layer chromatography of culture media did not support sequential sorbitol and sorbose oxidation. F erricyanide assays for sorbitol and sorbose dehydrogenases from membrane fractions isolated from cells grown on glycerol, sorbitol, or sorbose showed that sorbitol dehydrogenase activity in all four strains (three species) tested was always present (constitutive) and its specific activity was always enhanced by growth on sorbose. Membrane fractions showed no or very low constitutive sorbose dehydrogenase activity and no evidence that this secondary dehydrogenase was induced."]},{"key":"dc:description.degree","label":"Dc Description Degree","values":["Master of Science"]},{"key":"dc:format.medium","label":"Dc Format Medium","values":["BTD"]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["The nature of sorbital (a primary) and sorbose (a secondary) dehydrogenases of Gluconobacter species"]}]}],"canonical_facts":{"dc:contributor.committeechair":["Claus, George William"],"dc:contributor.committeemember":["Yousten, Allan A.","Gregory, Eugene M."],"dc:contributor.department":["Biology"],"dc:creator":["Anriany, Yuda Adha"],"dc:date.accessioned":["2014-03-14T21:37:04Z"],"dc:date.available":["2014-03-14T21:37:04Z","2009-06-08"],"dc:date.issued":["1996-09-17"],"dc:description.abstract":["The genus <i>Gluconobacter</i> is known to carry out limited oxidations using the NAD(P)-independent membrane-bound dehydrogenases in which the products are released back to the medium. Reports of further limited oxidations of these primary oxidation products by <i>Gluconobacter</i> in single step or sequential oxidations by secondary dehydrogenases are also published. The objective of this project was to evaluate the nature of one primary (sorbitol) dehydrogenase and one secondary (sorbose) dehydrogenase because of their importance in Vitamin C production. My hypotheses were that sorbitol (the primary) dehydrogenase is constitutive, while sorbose (the secondary) dehydrogenase is inducible. Six <i>Gluconobacter</i> strains from three different species grew on plates containing 50/0 sorbose, indicating their ability to oxidize sorbose thus possessing a secondary dehydrogenase. When four strains were tested for their ability to carry out the sequential oxidation of sorbitol and then sorbose on media containing growth-limiting sorbitol concentrations, three strains showed possible biphasic growth. However, thin layer chromatography of culture media did not support sequential sorbitol and sorbose oxidation. F erricyanide assays for sorbitol and sorbose dehydrogenases from membrane fractions isolated from cells grown on glycerol, sorbitol, or sorbose showed that sorbitol dehydrogenase activity in all four strains (three species) tested was always present (constitutive) and its specific activity was always enhanced by growth on sorbose. Membrane fractions showed no or very low constitutive sorbose dehydrogenase activity and no evidence that this secondary dehydrogenase was induced."],"dc:description.degree":["Master of Science"],"dc:format.medium":["BTD"],"dc:format.mimetype":["application/pdf"],"dc:identifier.other":["etd-06082009-170814"],"dc:identifier.uri":["http://hdl.handle.net/10919/42889"],"dc:language.iso":["en"],"dc:publisher":["Virginia Tech"],"dc:rights":["In Copyright"],"dc:rights.uri":["http://rightsstatements.org/vocab/InC/1.0/"],"dc:subject":["noninducible","Gluconobacter","sorbital dehydrogenase","sorbase dehydrogenase","biphasic growth","constitutive"],"dc:title":["The nature of sorbital (a primary) and sorbose (a secondary) dehydrogenases of Gluconobacter species"],"dc:type":["Thesis"],"dc:type.dcmitype":["Text"],"thesis:degree_discipline":["Biology"],"thesis:degree_level":["masters"],"thesis:degree_name":["Master of Science"],"thesis:institution_name":["Virginia Polytechnic Institute and State University"]},"updated_at":"2026-07-22T22:19:01Z"}