| Document Type
|
:
|
BL
|
| Record Number
|
:
|
891341
|
| Main Entry
|
:
|
Gonawan, Fadzil Noor.
|
| Title & Author
|
:
|
Immobilized [beta]-Galactosidase-Mediated Conversion of Lactose : : Process, Kinetics and Modeling Studies /\ Fadzil Noor Gonawan.
|
| Publication Statement
|
:
|
[Place of publication not identified] :: Springer,, 2019.
|
| Series Statement
|
:
|
Springer theses
|
| Page. NO
|
:
|
1 online resource
|
| ISBN
|
:
|
9789811334689
|
|
|
:
|
: 9811334684
|
|
|
:
|
9789811334672
|
| Contents
|
:
|
Intro; Supervisors' Foreword; Parts of this thesis have been published in the following journal articles:; Acknowledgements; Contents; Abbreviations; Symbols; 1 Introduction; 1.1 Concerns and Issues Regarding Lactose; 1.2?-Galactosidase-Catalyzed Conversion of Lactose; 1.3 Problem Statement; 1.4 Research Objectives; References; 2 Literature Review; 2.1 Enzymatic Production of GOS; 2.1.1 Substrate; 2.1.2 Type of Enzyme; 2.1.3 Reaction Parameters; 2.2 The Kinetic of?-Gal-Catalyzed Reaction of Lactose; 2.2.1 The Hydrolysis and Transgalactosylation Reaction Mechanism
|
|
|
:
|
2.2.2 The Inhibition of?-Gal2.2.3 The Kinetic Model of Hydrolysis and Transgalactosylation Reactions; 2.3 Reactors for?-Gal-Catalyzed Lactose Conversion; 2.4 The Preparation of EMR; 2.4.1 Type of Membrane; 2.4.2 The Characteristic of the Membrane; 2.4.3 The Immobilization of?-Gal on the Membrane; 2.5?-Gal-Catalyzed Conversion of Lactose in EMR; 2.6 The Mass Transfer of Solutes Through the Membrane; 2.6.1 Diffusivities in Liquids; 2.6.2 Concentration Polarization; 2.6.3 Hindrance Factors; 2.6.4 Mass Transfer Model in Enzymatic HFMR; 2.7 Summary; References; 3 Research Methodology
|
|
|
:
|
3.1 Research Flowchart3.2 Materials and Chemicals; 3.3 Determination of?-Gal Activity; 3.4 Chemical Analysis of the Saccharides Compound; 3.5 Preliminary Study on?-Gal-Catalyzed Conversion of Lactose; 3.5.1 Study on the Hydrolysis and Transgalactosylation Reactions; 3.5.2 Inhibition Study; 3.6 The Immobilization of?-Gal on the Polysulfone Membrane; 3.7 The Development and Operation of HFMR Experimental Rig; 3.7.1 Hydrodynamic Study of the HFMR; 3.7.2 Immobilization of?-Gal on the EMR Module; 3.7.3 Development and Operation of the HFMR; 3.7.4 Shutdown and Cleaning Procedure
|
|
|
:
|
3.10.2 The Effect of Gel Layer3.10.3 Determination of the Mass Transfer Parameters; 3.10.4 Coupled Model of Mass Transfer and Rate of Reaction; 3.10.5 Effect of TMP on the Mass Transfer and Reaction Rate; 3.11 Scope of Study; References; 4 Results and Discussion; 4.1 Preliminaries Study of?-Gal-Catalyzed Conversion of Lactose; 4.1.1 Effect of?-Gal Activity; 4.1.2 Effect of Lactose Concentration; 4.1.3 Inhibition Study of Galactose and Glucose; 4.2 The Preparation of?-Gal Immobilized in the HFMR; 4.2.1 Hydrodynamic Study in the HFMR; 4.2.1.1 The Effect of Mesh Size on the Response
|
|
|
:
|
3.8 Operational Parameters Study of the EMR3.8.1 Determination of Permeation Flux; 3.8.2 Determination of Separation Factor (Sf, i); 3.8.3 Determination of Membrane Resistance Coefficient; 3.8.4 The Effect of TMP on?-Gal-Catalyzed Reaction; 3.8.5 The Effect of Feed Concentration on?-Gal-Catalyzed Reaction; 3.8.6 The Effect of Feed Flow Rate on?-Gal-Catalyzed Reaction; 3.9 Kinetic Modeling of?-Gal-Catalyzed Reaction of Lactose; 3.9.1 Kinetic Model Development; 3.9.2 Determination of the Kinetic Parameters; 3.10 Study on the Mass Transfer Characteristic; 3.10.1 Mass Transfer Model
|
| Abstract
|
:
|
This book describes the reaction rate profiles of the?-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 '?-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.
|
| Subject
|
:
|
Biochemical engineering.
|
| Subject
|
:
|
Enzyme kinetics.
|
| Subject
|
:
|
Biochemical engineering.
|
| Subject
|
:
|
Enzyme kinetics.
|
| Subject
|
:
|
SCIENCE-- Life Sciences-- Biochemistry.
|
| Dewey Classification
|
:
|
572.744
|
| LC Classification
|
:
|
QP601.3
|