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Please use this identifier to cite or link to this item: http://eprint.iitd.ac.in/handle/2074/660

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dc.contributor.authorBhattacharya, Sumana-
dc.contributor.authorSchiavone, Marc-
dc.contributor.authorGomes, James-
dc.contributor.authorBhattacharya, Sanjoy K-
dc.date.accessioned2005-08-02T06:38:34Z-
dc.date.available2005-08-02T06:38:34Z-
dc.date.issued2004-
dc.identifier.citationJournal of Biotechnology, 111(2), 203–217en
dc.identifier.urihttp://eprint.iitd.ac.in/dspace/handle/2074/660-
dc.description.abstractA novel scheme employing enzymatic catalysts is described enabling conversion of d-ribulose-1,5-bisphosphate (RuBP) from 3-phospho-d-glycerate (3-PGA) without loss of carbon. Bioreactors harboring immobilized enzymes namely, phosphoglycerate kinase (PGK), glycerate phosphate dehydrogenase, triose phosphate isomerase (TIM), aldolase, transketolase (TKL), phosphatase (PTASE/FP), epimerase (EMR) and phosphoribulokinase (PRK), in accordance with this novel scheme were employed. These reactors were designed and constructed based on simulations carried out to study their performance under various operational conditions and allowed production of about 56±3%RuBP from 3-PGA. This method of synthesis of RuBP from 3-PGA employing immobilized enzyme bioreactors may be used for continuous regeneration of RuBP in biocatalytic carbon dioxide fixation processes from emissions where RuBP acts as acceptor of carbon dioxide to produce 3-PGA, rendering the fixation process continuous.en
dc.format.extent3167552 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoenen
dc.subjectEnzymesen
dc.subjectRuBPen
dc.subject3-PGAen
dc.titleCascade of bioreactors in series for conversion of 3-phospho-d-glycerate into d-ribulose-1,5-bisphosphate: kinetic parameters of enzymes and operation variablesen
dc.typeArticleen
Appears in Collections:Biochemical Engg. and Biotechnology

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