Enzymology of butanol formation in Clostridium Beijerinckii

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dc.contributor.authorYan, Run-Taoen
dc.contributor.committeechairChen, Jiann-Shinen
dc.contributor.committeememberDean, Dennis R.en
dc.contributor.committeememberJohnson, John L.en
dc.contributor.committeememberGregory, Eugene M.en
dc.contributor.committeememberKrieg, Noel R.en
dc.contributor.departmentAnaerobic Microbiologyen
dc.date.accessioned2014-03-14T21:15:03Zen
dc.date.adate2006-06-19en
dc.date.available2014-03-14T21:15:03Zen
dc.date.issued1991en
dc.date.rdate2006-06-19en
dc.date.sdate2006-06-19en
dc.description.abstractThe present study encompasses an investigation of the expression of solvent forming enzymes and purification and characterization of butanol-forming enzymes. More sensitive and accurate procedures for the determination of acids and solvents in cultures have been developed, which led to the recognition of the onset of solvent production at the mid-exponential phase, about two h earlier than previously reported. Activities of solvent-forming enzymes started to increase about one h before the onset of measurable solvent production and the activities of solvent-forming enzymes did not increase simultaneously. CoA-acylating aldehyde dehydrogenase (ALDH) was purified to near homogeneity. The ALDH showed a native M.. of 100,000, and a subunit Mr of 55,000. ALDH could use either NAD(H) or NADP(H) as the coenzyme. ALDH was oxygenlabile. The O₂-inactivated enzyme could be reactivated by incubating the enzyme with CoA. Both NADH- and NADPH-dependent alcohol dehydrogenase activities were present in crude extracts. The ratio of NADPH-dependent activity to NADH-dependent activity (the PID ratio) varied in crude extracts. The PID ratio was affected by O~ ionic strength, pH, growth stage of cell, Fe in culture medium and temperature. Two ADHs have been identified in crude extracts. The NADPH-dependent ADH (P-ADH) could be separated from the NADH/NADPH-dependent ADH (D/P-ADH). The D/P-ADH has been extensively purified. The D/P-ADH showed a native Mr of 70,000 and subunits with Mr of 45,300 and 40,000. The D/P-ADH activity could be inactivated by a,a' -dipyridyl and restored by Fe2+.en
dc.description.degreePh. D.en
dc.format.extentxi, 141 leavesen
dc.format.mediumBTDen
dc.format.mimetypeapplication/pdfen
dc.identifier.otheretd-06192006-125711en
dc.identifier.sourceurlhttp://scholar.lib.vt.edu/theses/available/etd-06192006-125711/en
dc.identifier.urihttp://hdl.handle.net/10919/38617en
dc.language.isoenen
dc.publisherVirginia Techen
dc.relation.haspartLD5655.V856_1991.Y36.pdfen
dc.relation.isformatofOCLC# 24367453en
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subject.lccLD5655.V856 1991.Y36en
dc.subject.lcshButanol -- Researchen
dc.subject.lcshClostridium -- Researchen
dc.titleEnzymology of butanol formation in Clostridium Beijerinckiien
dc.typeDissertationen
dc.type.dcmitypeTexten
thesis.degree.disciplineAnaerobic Microbiologyen
thesis.degree.grantorVirginia Polytechnic Institute and State Universityen
thesis.degree.leveldoctoralen
thesis.degree.namePh. D.en

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