Biocatalyst immobilization : foundations and applications /

Biocatalyst Immobilization: Foundations and Applications provides a comprehensive overview of biocatalytic immobilization processes, as well as methods for study, characterization and application. Early chapters discuss current progress in enzyme immobilization and methods for selecting and pretreat...

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Bibliographic Details
Corporate Author:	ScienceDirect (Online service)
Other Authors:	Ferreira, María Luján
Format:	eBook
Language:	English
Published:	London, United Kingdom : Academic Press, [2023].
Series:	Foundations and frontiers in enzymology series.
Subjects:	Biocatalysis. Immobilized enzymes. Biocatalysis Enzymes, Immobilized Biocatalyse. Enzymes immobilisées. Immobilized enzymes Electronic books.
Online Access:	Connect to the full text of this electronic book

Table of Contents:

Intro
Biocatalyst Immobilization: Foundations and Applications
Copyright
Dedication
Contents
Contributors
Preface
Acknowledgments
Chapter 1: The enzyme, the support, and the immobilization strategy: The key findings to a desirable biocatalyst
1.1. Introduction
1.2. Enzyme immobilization: Enzyme, support, or hybrid biocatalyst?
1.3. Immobilization methodologies and immobilization chemistry
1.4. Supports for enzyme immobilization
1.5. Enzyme engineering for enzyme immobilization
1.6. Improve enzyme performance: Just an immobilization question? The immobilized biocatalyst engineering (IBE) approach
1.7. Conclusions and perspectives
References
Chapter 2: Selection and modification of enzymes prior to immobilization
2.1. Introduction
2.2. Selection of enzymes for various applications
2.2.1. Classification of enzymes
2.2.2. Industrial applications of enzymes
2.2.3. Selection of enzymes based on process considerations
2.3. Enzyme modification technologies
2.3.1. Protein engineering
2.3.2. Enzyme engineering to improve catalytic activity
2.3.2.1. Directed evolution
2.3.2.2. Site-directed mutagenesis (SDM)
2.3.2.3. Fusion protein linkers
2.3.2.4. Unnatural amino acids
2.3.2.5. Surface display technology (SDT)
References
Chapter 3: Enzyme immobilization approaches
3.1. Introduction
3.1.1. Immobilized enzymes
3.1.2. Immobilization techniques
3.2. Methods of carrier binding
3.2.1. Covalent binding method
3.2.2. Noncovalent adsorption and deposition
3.2.2.1. Adsorption technique
3.2.3. Cross-linking approach
3.2.4. Entrapping method
3.2.4.1. Matrix entrapment
3.2.4.2. Microencapsulation
3.2.5. Immobilization via ionic interactions
3.2.6. Covalent fastening (tethering).
3.3. Factors that should be taken into consideration before planning immobilization techniques
3.4. Immobilized enzyme bioanalytical potential
3.5. Advantages and disadvantages of immobilization
3.5.1. Advantages of immobilized enzymes
3.5.2. Disadvantages of enzyme immobilization
3.6. Some applications of immobilized enzymes
3.6.1. Industrial production
3.6.2. Biomedical applications
3.6.3. Food industry
3.6.4. Wastewater management
3.7. Conclusions
Acknowledgment
References
Further reading
Chapter 4: Postimmobilization treatments before applications
4.1. Introduction
4.2. Enzyme immobilization on/in insoluble carriers
4.2.1. Polyethylenimine in postimmobilization treatments
4.2.2. Dextran aldehyde in postimmobilization treatments
4.2.3. Glutaraldehyde in postimmobilization treatments
4.2.4. Other active agents used in postimmobilization treatments
4.3. Enzyme immobilization in membrane reactors
4.3.1. The membrane as a selective barrier
4.3.2. The membrane as a carrier
4.4. Summary
References
Chapter 5: Support-free immobilization
5.1. Introduction
5.2. Enzyme immobilization
5.2.1. Adsorption techniques
5.2.2. Entrapment
5.2.3. Covalent attachment
5.2.4. Cross-linked enzymes
5.3. Preparation of cross-linked enzyme aggregate (CLEA)
5.3.1. Selection of the precipitant agent
5.3.2. Cofeeders in the preparation of CLEAs
5.3.3. Chemical amination of the enzyme
5.3.4. Preparation of magnetic CLEAs
5.4. Preparation of coimmobilization of enzymes in combi-CLEAs
5.5. Preparation of magnetic CLEA (m-CLEAs) and m-Combi-CLEAs
5.5.1. Reactional equations
5.5.2. Chemical reactions
5.5.3. Reactional equations
5.5.4. Reactional equations
5.6. Cross-linked enzyme crystals (CLECs)
5.7. Future trends and conclusion
References.
Chapter 6: Measuring and reporting enzyme's immobilization efficiency
6.1. General topics about protein quantification in biocatalysts
6.1.1. An important issue: How much protein does my biocatalyst have?
6.1.2. Definitions and protein quantification methods
6.2. Free and immobilized enzymes: Important issues in protein quantification methods
6.2.1. Protein quantification in liquid media: Influence of the nature of the enzyme and the solvent
6.2.2. Strategies for the quantification of immobilized proteins in commercial biocatalysts
6.2.3. A complete analysis of the use of spectrophotometric methods to quantify proteins in biocatalysts and in general
6.2.3.1. CALB
6.2.3.2. Other enzymes
6.2.3.3. Other proteins
6.2.3.4. Biocatalyst stability: Evaluation of protein leaching in unconventional media
6.3. Strategies to avoid mistakes in protein quantification
6.3.1. Recognizing interferences
6.3.2. Stirring and aggregation
6.3.3. A new method in protein quantification in the field of immobilized enzymes: Determination of sulfur using AE-ICP
6.3.4. Quantification of the immobilized protein through electron microprobe analysis
6.4. Other considerations in enzyme immobilization: Unexpected sources of error
6.4.1. Spectrophotometric methods
6.4.2. Mass balance of support and total protein, role of adsorbed water, and the drying procedure
6.4.3. Reproducibility of protein quantification and loss of proteins at the washing, filtration, and separation steps
6.5. CLEAs: A challenge for protein quantification and free and immobilized enzymatic activity comparison
6.5.1. Quantification of protein in commercial and lab CLEA preparations
6.5.2. Free and immobilized enzymatic activity comparisons: How to select conditions and a frequent cause of mistake.
6.6. A constructive criticism: The need for systematization
6.6.1. Best procedures to report efficiency of protein immobilization in biotechnology: The search of the parameters for ...
6.7. Conclusions and recommendations
Acknowledgments
References
Chapter 7: Some recent innovations related to enzyme immobilization
7.1. Introduction
7.2. Selection and synthesis of novel support systems for enzyme immobilization
7.2.1. Synthetic materials as supports
7.2.1.1. Zeolites
7.2.1.2. Ceramics
7.2.1.3. Celite
7.2.1.4. Silica
7.2.1.5. Glass
7.2.1.6. Activated carbon
7.2.2. Inorganic supports
7.2.3. Nano-carrier immobilized enzymes
7.2.3.1. Carbon nanotubes
7.2.3.2. Graphene
7.2.3.3. Metal nanomaterials
7.2.3.4. Metal oxide nanomaterials
7.2.4. Agricultural wastes
7.2.4.1. Lignocellulosic wastes
7.2.4.2. Rice straw
7.2.4.3. Coconut fibers
7.2.4.4. Spent coffee grounds
7.2.4.5. Eggshell
7.2.5. DNA: A promising support for multienzymatic cascades
7.2.6. Metal-organic frameworks: An enzyme immobilization platform with large surface area and tunable ultrahigh porosity
7.2.7. Matter-tag: An adhesion-promoting peptide-based universal enzyme immobilization platform
7.2.8. Tunable 3D-printed enzyme immobilization carriers: Meeting the demands of biocatalytic industry
7.3. Methods of immobilization
7.3.1. Methods of irreversible enzyme immobilization
7.3.1.1. Formation of covalent bonds
7.3.1.2. Entrapment and cross-linking
7.3.2. Methods of reversible immobilization
7.4. In silico toolbox for tools and optimization of rational design for novel approaches of enzyme immobilization
7.5. Integration of enzyme immobilization and protein engineering
7.6. Conclusions
Acknowledgments
References.
Chapter 8: Enzyme immobilization for use in nonconventional media
8.1. Enzyme immobilization for nonconventional media: Why and for what
8.1.1. Biocatalysis in nonconventional media
8.1.2. Use of immobilized enzymes in nonconventional media
8.2. Impact of additives in the aqueous media, nonaqueous media, and multiphasic media: Bioimprinting, surfactants, polym ...
8.2.1. Bioimprinting for use in organic reaction media
8.2.2. Surfactants for protein stabilization and disaggregation
8.2.3. Neutral polymers and polyions to stabilize enzymes
8.2.4. Biodegradable polymers
8.3. Ionic liquids: It is interesting but would it be rentable? Differences with other reaction media
8.4. Some considerations for reactions performed in nonconventional biphasic liquid systems
8.5. Dont forget the supports: What happens in nonconventional media vs water?
8.6. The drawbacks of different additives in the nonconventional reaction media of immobilized enzymes: Adsorbents for pr ...
8.6.1. A polar compound as a product in a nonpolar reaction media
8.6.2. A polar compound as a substrate in a nonpolar reaction media
8.7. Adequate drying of the immobilized enzyme: Is lyophilization the solution?
8.8. Enzyme leaching in nonconventional media
8.8.1. Aggregation
8.8.2. Interaction with the surface
8.8.3. Protection from desorption and the nonconventional reaction media
8.9. Achieving a high enzymatic activity in CLEAs and its measurement: An example of a complex task
8.9.1. Determination of the protein content of commercial enzyme preparations in the context of comparison with CLEAs
8.9.2. Determination of measurement intervals that guarantee constant specific activity values
8.9.3. Determination of PP content in CLEAs from activity measurements of supernatant and washings.