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Article: NADPH-dependent D-aldose reductases and xylose fermentation in Fusarium oxysporum

TitleNADPH-dependent D-aldose reductases and xylose fermentation in Fusarium oxysporum
Authors
KeywordsAcetoin
Fusarium Oxysporum
Xylose
Xylose Reductases
Issue Date2004
PublisherSociety for Biotechnology, Japan. The Journal's web site is located at http://www.jstage.jst.go.jp/browse/jbb/_vols/-char/en
Citation
Journal Of Bioscience And Bioengineering, 2004, v. 97 n. 5, p. 299-304 How to Cite?
AbstractTwo aldose (xylose) reductases (ARI and ARII) from Fusarium oxysporum were purified and characterized. The native ARI was a monomer with Mr 41000, pI 5.2 and showed a 52-fold preference for NADPH over NADH, while ARII was homodimeric with a subunit of Mr 37000, pI 3.6 and a 60-fold preference for NADPH over NADH. In this study, the influence of aeration and the response to the addition of electron acceptors on xylose fermentation by F. oxysporum were also studied. The batch cultivation of F. oxysporum on xylose was performed under aerobic, anaerobic and oxygen-limited conditions in stirred tank reactors. Oxygen limitation had considerable influence on xylose metabolism. Under anaerobic conditions (0 vvm), xylitol was the main product with a maximum yield of 0.34 mole of xylitol/mole of xylose while the maximum ethanol yield (1.02 moles of ethanol/mole of xylose) was obtained under aerobic conditions (0.3 vvm). When the artificial electron acceptor acetoin was added to an anaerobic batch fermentation of xylose by F. oxysporum, the ethanol yield increased while xylitol excretion was also decreased.
Persistent Identifierhttp://hdl.handle.net/10722/181240
ISSN
2015 Impact Factor: 1.964
2015 SCImago Journal Rankings: 0.709
References

 

DC FieldValueLanguage
dc.contributor.authorPanagiotou, Gen_US
dc.contributor.authorChristakopoulos, Pen_US
dc.date.accessioned2013-02-21T02:03:26Z-
dc.date.available2013-02-21T02:03:26Z-
dc.date.issued2004en_US
dc.identifier.citationJournal Of Bioscience And Bioengineering, 2004, v. 97 n. 5, p. 299-304en_US
dc.identifier.issn1389-1723en_US
dc.identifier.urihttp://hdl.handle.net/10722/181240-
dc.description.abstractTwo aldose (xylose) reductases (ARI and ARII) from Fusarium oxysporum were purified and characterized. The native ARI was a monomer with Mr 41000, pI 5.2 and showed a 52-fold preference for NADPH over NADH, while ARII was homodimeric with a subunit of Mr 37000, pI 3.6 and a 60-fold preference for NADPH over NADH. In this study, the influence of aeration and the response to the addition of electron acceptors on xylose fermentation by F. oxysporum were also studied. The batch cultivation of F. oxysporum on xylose was performed under aerobic, anaerobic and oxygen-limited conditions in stirred tank reactors. Oxygen limitation had considerable influence on xylose metabolism. Under anaerobic conditions (0 vvm), xylitol was the main product with a maximum yield of 0.34 mole of xylitol/mole of xylose while the maximum ethanol yield (1.02 moles of ethanol/mole of xylose) was obtained under aerobic conditions (0.3 vvm). When the artificial electron acceptor acetoin was added to an anaerobic batch fermentation of xylose by F. oxysporum, the ethanol yield increased while xylitol excretion was also decreased.en_US
dc.languageengen_US
dc.publisherSociety for Biotechnology, Japan. The Journal's web site is located at http://www.jstage.jst.go.jp/browse/jbb/_vols/-char/enen_US
dc.relation.ispartofJournal of Bioscience and Bioengineeringen_US
dc.subjectAcetoinen_US
dc.subjectFusarium Oxysporumen_US
dc.subjectXyloseen_US
dc.subjectXylose Reductasesen_US
dc.titleNADPH-dependent D-aldose reductases and xylose fermentation in Fusarium oxysporumen_US
dc.typeArticleen_US
dc.identifier.emailPanagiotou, G: gipa@hku.hken_US
dc.identifier.authorityPanagiotou, G=rp01725en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.scopuseid_2-s2.0-2942626136en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-2942626136&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume97en_US
dc.identifier.issue5en_US
dc.identifier.spage299en_US
dc.identifier.epage304en_US
dc.publisher.placeJapanen_US
dc.identifier.scopusauthoridPanagiotou, G=8566179700en_US
dc.identifier.scopusauthoridChristakopoulos, P=7006479823en_US

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