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Immobilized B-galactosidase-mediated...

Gonawan, Fadzil Noor.

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Immobilized B-galactosidase-mediated conversion of lactose = process, kinetics and modeling studies /

Record Type:	Electronic resources : Monograph/item
Title/Author:	Immobilized B-galactosidase-mediated conversion of lactose/ by Fadzil Noor Gonawan.
Reminder of title:	process, kinetics and modeling studies /
Author:	Gonawan, Fadzil Noor.
Published:	Singapore :Springer Singapore : : 2019.,
Description:	xxi, 171 p. :ill., digital ;24 cm.
[NT 15003449]:	Introduction -- Literature Review -- Research Methodology -- Results and Discussion -- Conclusions and Recommendations.
Contained By:	Springer eBooks
Subject:	Enzyme kinetics. -
Online resource:	https://doi.org/10.1007/978-981-13-3468-9
ISBN:	9789811334689

Immobilized B-galactosidase-mediated conversion of lactose = process, kinetics and modeling studies /
Gonawan, Fadzil Noor.

Immobilized B-galactosidase-mediated conversion of lactoseprocess, kinetics and modeling studies /[electronic resource] :by Fadzil Noor Gonawan. - Singapore :Springer Singapore :2019. - xxi, 171 p. :ill., digital ;24 cm. - Springer theses,2190-5053. - Springer theses..

Introduction -- Literature Review -- Research Methodology -- Results and Discussion -- Conclusions and Recommendations.

This book describes the reaction rate profiles of the B-galactosidase-catalyzed conversion of lactose on the inner surface of a hollow fiber membrane, which is employed as an enzymatic reactor system. The reaction rate profiles were obtained by solving the mass transfer and kinetics of reaction in a 2-dimensional model of the system. The primary challenge of this research was to develop the kinetic model of the reaction to describe the kinetic behavior as the reaction occurred on the membrane surface. Despite the difficulties, the proposed model can reliably replicate the actual process, as validation procedures have confirmed. The reaction rates obtained analyze the performance of the immobilized enzyme on the membrane surface. Previously, an increase in performance of 'B-galactosidase-catalyzed conversion of lactose assisted by ultrafiltration was suggested due to inhibitor removal.However, as the analysis presented here shows, the concentration profile of the substrate on the membrane surface also affects the reaction performance.

ISBN: 9789811334689

Standard No.: 10.1007/978-981-13-3468-9doiSubjects--Topical Terms:

536022
Enzyme kinetics.

LC Class. No.: QP601.3 / .G663 2019

Dewey Class. No.: 572.744

Immobilized B-galactosidase-mediated conversion of lactose = process, kinetics and modeling studies /
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245 1 0 $a Immobilized B-galactosidase-mediated conversion of lactose $h [electronic resource] : $b process, kinetics and modeling studies / $c by Fadzil Noor Gonawan.
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300 $a xxi, 171 p. : $b ill., digital ; $c 24 cm.
490 1 $a Springer theses, $x 2190-5053
505 0 $a Introduction -- Literature Review -- Research Methodology -- Results and Discussion -- Conclusions and Recommendations.
520 $a This book describes the reaction rate profiles of the B-galactosidase-catalyzed conversion of lactose on the inner surface of a hollow fiber membrane, which is employed as an enzymatic reactor system. The reaction rate profiles were obtained by solving the mass transfer and kinetics of reaction in a 2-dimensional model of the system. The primary challenge of this research was to develop the kinetic model of the reaction to describe the kinetic behavior as the reaction occurred on the membrane surface. Despite the difficulties, the proposed model can reliably replicate the actual process, as validation procedures have confirmed. The reaction rates obtained analyze the performance of the immobilized enzyme on the membrane surface. Previously, an increase in performance of 'B-galactosidase-catalyzed conversion of lactose assisted by ultrafiltration was suggested due to inhibitor removal.However, as the analysis presented here shows, the concentration profile of the substrate on the membrane surface also affects the reaction performance.
650 0 $a Enzyme kinetics. $3 536022
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