Assessment of Diffusion Limitations on the Performance of Immobilised Acid Urease Derivatives

In this work, the specific activity of acid urease immobilised on Eupergit® C250L at different enzyme loadings YP/B in the range of 48-170.5 mg BSAE/g dry support (ds) was satisfactorily reconstructed by using the simultaneous film and intraparticle diffusion and Michaelis-Menten kinetic reaction mo...

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Main Authors: N. Bortone, M. Fidaleo, M. Moresi
Format: Article
Language:English
Published: AIDIC Servizi S.r.l. 2013-06-01
Series:Chemical Engineering Transactions
Online Access:https://www.cetjournal.it/index.php/cet/article/view/6583
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author N. Bortone
M. Fidaleo
M. Moresi
author_facet N. Bortone
M. Fidaleo
M. Moresi
author_sort N. Bortone
collection DOAJ
description In this work, the specific activity of acid urease immobilised on Eupergit® C250L at different enzyme loadings YP/B in the range of 48-170.5 mg BSAE/g dry support (ds) was satisfactorily reconstructed by using the simultaneous film and intraparticle diffusion and Michaelis-Menten kinetic reaction model. By referring to the intrinsic kinetic parameters of free acid urease, the statistically significant change in the apparent affinity of immobilised enzyme for urea was attributed to diffusion limitations only. When operating in a stirred bioreactor in the pseudo-first order regime, the specific activity of the biocatalyst was mainly restricted by its internal resistance, the corresponding effectiveness factor (?) reducing from 0.9 to 0.28 as YP/B increased from 12.5 to 400.0 mg BSAE/g ds. The combined effect of internal and external mass-transfer resistances limited the advantages of using biocatalysts with enzyme loadings greater than 150 mg BSAE/g ds.
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spelling doaj.art-d33cdc323340466ab13d9968f8e3260d2022-12-21T23:03:57ZengAIDIC Servizi S.r.l.Chemical Engineering Transactions2283-92162013-06-013210.3303/CET1332189Assessment of Diffusion Limitations on the Performance of Immobilised Acid Urease DerivativesN. BortoneM. FidaleoM. MoresiIn this work, the specific activity of acid urease immobilised on Eupergit® C250L at different enzyme loadings YP/B in the range of 48-170.5 mg BSAE/g dry support (ds) was satisfactorily reconstructed by using the simultaneous film and intraparticle diffusion and Michaelis-Menten kinetic reaction model. By referring to the intrinsic kinetic parameters of free acid urease, the statistically significant change in the apparent affinity of immobilised enzyme for urea was attributed to diffusion limitations only. When operating in a stirred bioreactor in the pseudo-first order regime, the specific activity of the biocatalyst was mainly restricted by its internal resistance, the corresponding effectiveness factor (?) reducing from 0.9 to 0.28 as YP/B increased from 12.5 to 400.0 mg BSAE/g ds. The combined effect of internal and external mass-transfer resistances limited the advantages of using biocatalysts with enzyme loadings greater than 150 mg BSAE/g ds.https://www.cetjournal.it/index.php/cet/article/view/6583
spellingShingle N. Bortone
M. Fidaleo
M. Moresi
Assessment of Diffusion Limitations on the Performance of Immobilised Acid Urease Derivatives
Chemical Engineering Transactions
title Assessment of Diffusion Limitations on the Performance of Immobilised Acid Urease Derivatives
title_full Assessment of Diffusion Limitations on the Performance of Immobilised Acid Urease Derivatives
title_fullStr Assessment of Diffusion Limitations on the Performance of Immobilised Acid Urease Derivatives
title_full_unstemmed Assessment of Diffusion Limitations on the Performance of Immobilised Acid Urease Derivatives
title_short Assessment of Diffusion Limitations on the Performance of Immobilised Acid Urease Derivatives
title_sort assessment of diffusion limitations on the performance of immobilised acid urease derivatives
url https://www.cetjournal.it/index.php/cet/article/view/6583
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