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Enzyme reaction engineering for the conversion of emulsified di-rhamnolipid by free and immobilized Naringinase

dc.contributor.authorMagario, Ivana*
dc.date.accessioned2021-02-11T12:46:10Z
dc.date.available2021-02-11T12:46:10Z
dc.date.issued2009*
dc.date.submitted2019-07-30 20:02:00*
dc.identifier35218*
dc.identifier.urihttps://directory.doabooks.org/handle/20.500.12854/46649
dc.description.abstractProcess optimization was conducted for the conversion of the aggragate-building substrate di-rhamnolipid to mono-rhamnolipid by Alpha-L-rhamnosidase from Penicillium decumbens and resulting in: (I) selection of optimal reaction conditions for enzyme activity and stability, (II) modeling of the reaction time course assuming mixed aggregates as a second phase, and (III) high mass diffusion resistances were completely overcome by the use of non-porous magnetic enzyme micro-carriers.*
dc.languageEnglish*
dc.subjectTP155-156*
dc.subject.classificationthema EDItEUR::T Technology, Engineering, Agriculture, Industrial processes::TC Biochemical engineering::TCB Biotechnologyen_US
dc.subject.othermixed aggregates*
dc.subject.otheraggregate-building substrate*
dc.subject.otherNaringinase*
dc.subject.othermagnetic microbeads*
dc.subject.otherrhamnolipids*
dc.titleEnzyme reaction engineering for the conversion of emulsified di-rhamnolipid by free and immobilized Naringinase*
dc.typebook
oapen.identifier.doi10.5445/KSP/1000010067*
oapen.relation.isPublishedBy68fffc18-8f7b-44fa-ac7e-0b7d7d979bd2*
oapen.relation.isbn9783866443297*
oapen.pages131 p.*
peerreview.review.typeFull text
peerreview.anonymityAll identities known
peerreview.reviewer.typeInternal editor
peerreview.reviewer.typeExternal peer reviewer
peerreview.review.stagePre-publication
peerreview.open.reviewNo
peerreview.publish.responsibilityScientific or Editorial Board
peerreview.id8ad5c235-9810-49eb-b358-27c8675324d9
peerreview.titleDissertations (Dissertationen)


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