Experimental modelling of thermal inactivation of urease

Illeová, Viera; Polakovič, Milan; Štefuca, Vladimı́r; Ačai, Pavel; Juma, M.

doi:10.1016/j.jbiotec.2003.07.005

Cited by 43 publications

(30 citation statements)

References 17 publications

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“…The thermostability of ureases of different origin either in free or immobilized forms has often been a subject of investigation. There are several studies for jack been urease where the inactivation curve was measured at high temperatures [12,13].…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Estimation of the overall kinetic parameters of enzyme inactivation using an isoconversional method

Oancea

Stuparu

Nita

et al. 2008

Biophysical Chemistry

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Please cite this article as: D. Oancea, Alexandrina Stuparu, Madalina Nita, Mihaela Puiu, Adina Raducan, Estimation of the overall kinetic parameters of enzyme inactivation using an isoconversional method, Biophysical Chemistry (2008Chemistry ( ), doi: 10.1016Chemistry ( /j.bpc.2008 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT ABSTRACTAn isoconversional method is proposed in order to calculate the kinetic parameters of enzyme inactivation. The method provides an efficient and low-cost procedure to describe both operational and thermal inactivation. Unlike the ordinary kinetic assays performed at constant enzyme concentration and at various substrate concentrations, the isoconversional method requires several extended kinetic curves for constant initial substrate concentration and different enzyme concentrations. The procedure was tested and validated using simulated data obtained for several kinetic models frequently discussed in the literature. After the validation, the isoconversional method was used for the investigation of the thermoinactivation of urease during urea hydrolysis in self buffered medium and the operational inactivation (destructive oxidation by excess peroxide) of catalase at high concentration of hydrogen peroxide. The results showed that the isoconversional method gives good results of global inactivation constant for both simple and more complex models.

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Section: Accepted Manuscriptmentioning

confidence: 99%

Estimation of the overall kinetic parameters of enzyme inactivation using an isoconversional method

Oancea

Stuparu

Nita

et al. 2008

Biophysical Chemistry

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“…On the other hand, simple models are available, which can provide valuable insight about the underlying mechanism, as well as quantitative indications about the system behavior with only a few, but meaningful, parameters. The simplest model proposed for the evaluation of enzymatic deactivation consists of a single step first-order kinetics (Illeova et al, 2003;Borda et al, 2004;Ladero et al 2006), where the enzyme evolves from its original active state (ε 1 ) to a deactivated state (ε 2 ) according to Equation (3):…”

Section: Effect Of Temperature and Water On The Conversion Of The Reamentioning

confidence: 99%

Stability of immobilized Rhizomucor miehei lipase for the synthesis of pentyl octanoate in a continuous packed bed bioreactor

Skoronski

Padoin

Soares

et al. 2014

Braz. J. Chem. Eng.

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-The enzymatic synthesis of organic compounds in continuous bioreactors is an efficient way to obtain industrially important chemicals. However, few works have focused on the study of the operational conditions and the bioprocess performance. In this work, the aliphatic ester pentyl octanoate was obtained by direct esterification using a continuous packed bed bioreactor containing the immobilized enzyme Lipozyme ® RM IM as catalyst. Enzymatic deactivation was evaluated under different conditions for the operational parameters substrate/enzyme ratio (5.00, 1.67, 0.83 and 0.55 mmol substrate ·min -1 ·g -1 enzyme ) and temperature (30, 40, 50 and 60 °C). The optimal condition was observed at 30 ºC, which gave the minimum enzymatic deactivation rate and the maximum conversion to the desired product, yielding approximately 60 mmols of ester for an enzyme loading of 0.5 g into the bioreactor. A first-order deactivation model showed good agreement with the experimental data.

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“…2 International Journal of Engineering Mathematics Table 1: Range of parameters used in Illeova et al [1] and this work.…”

Section: Mathematical Formulation Of Analysis and Problemsmentioning

confidence: 99%

“…Several excellent techniques are available to assess urease activity [1,2]. In 1926, urease was isolated by Summner from the seeds of jack bean as a pure, crystalline enzyme [3].…”

Section: Introductionmentioning

confidence: 99%

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Mathematical Modeling and Analysis of the Kinetics of Thermal Inactivation of Enzyme

Ananthi¹,

Manimozhi²,

Praveen³

et al. 2013

International Journal of Engineering Mathematics

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A theoretical model of Illeova et al. (2003) thermal inactivation of urease is discussed. Analytical expressions pertaining to the molar concentrations of the native and denatured enzyme are obtained in terms of second-order reaction rate constant. Simple and closed form of theoretical expression pertains to the temperature are also derived. In this paper, homotopy analysis method (HAM) is used to obtain approximate solutions for a nonlinear ordinary differential equation. The obtained approximate result in comparison with the numerical ones is found to be in satisfactory agreement.

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Experimental modelling of thermal inactivation of urease

Cited by 43 publications

References 17 publications

Estimation of the overall kinetic parameters of enzyme inactivation using an isoconversional method

Estimation of the overall kinetic parameters of enzyme inactivation using an isoconversional method

Stability of immobilized Rhizomucor miehei lipase for the synthesis of pentyl octanoate in a continuous packed bed bioreactor

Mathematical Modeling and Analysis of the Kinetics of Thermal Inactivation of Enzyme

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