The nature of sorbital (a primary) and sorbose (a secondary) dehydrogenases of Gluconobacter species

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dc.contributor.authorAnriany, Yuda Adhaen
dc.contributor.committeechairClaus, George Williamen
dc.contributor.committeememberYousten, Allan A.en
dc.contributor.committeememberGregory, Eugene M.en
dc.contributor.departmentBiologyen
dc.date.accessioned2014-03-14T21:37:04Zen
dc.date.adate2009-06-08en
dc.date.available2014-03-14T21:37:04Zen
dc.date.issued1996-09-17en
dc.date.rdate2009-06-08en
dc.date.sdate2009-06-08en
dc.description.abstractThe 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.en
dc.description.degreeMaster of Scienceen
dc.format.extentx, 89 leavesen
dc.format.mediumBTDen
dc.format.mimetypeapplication/pdfen
dc.identifier.otheretd-06082009-170814en
dc.identifier.sourceurlhttp://scholar.lib.vt.edu/theses/available/etd-06082009-170814/en
dc.identifier.urihttp://hdl.handle.net/10919/42889en
dc.language.isoenen
dc.publisherVirginia Techen
dc.relation.haspartLD5655.V855_1996.A575.pdfen
dc.relation.isformatofOCLC# 36113980en
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subjectnoninducibleen
dc.subjectGluconobacteren
dc.subjectsorbital dehydrogenaseen
dc.subjectsorbase dehydrogenaseen
dc.subjectbiphasic growthen
dc.subjectconstitutiveen
dc.subject.lccLD5655.V855 1996.A575en
dc.titleThe nature of sorbital (a primary) and sorbose (a secondary) dehydrogenases of Gluconobacter speciesen
dc.typeThesisen
dc.type.dcmitypeTexten
thesis.degree.disciplineBiologyen
thesis.degree.grantorVirginia Polytechnic Institute and State Universityen
thesis.degree.levelmastersen
thesis.degree.nameMaster of Scienceen

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