Nanomaterials for Biocatalysis

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Nanomaterials for Biocatalysis explains the fundamental design concepts and emerging applications of nanoscale biocatalysts, such as bioconversions, bioelectronics, biosensors, biocomputing and therapeutic applications. Nano-biocatalysts refers to the incorporation of enzymes into nanomaterials. These enzyme-enhanced nanocarriers have many advantages, including low mass transfer limitation, high enzyme capacity, better stabilization, and the formation of single-enzyme nanoparticles. Smart nanocontainers have been developed for the smart release of their embedded active substances. These smart releases can be obtained by using smart coatings as their outer nanoshells.

In addition, these nanocontainers could protect the enzymes from chemical or metabolic alterations on their delivering pathways towards the target. This is an important reference source for materials scientists and chemical engineers who want to know more about how nanomaterials are being used for biocatalysis applications.

Author(s): Guillermo R. Castro, Ashok Kumar Nadda, Tuan Anh Nguyen, Xianghui Qi, Ghulam Yasin
Series: Micro and Nano Technologies
Publisher: Elsevier
Year: 2021

Language: English
Pages: 753
City: Amsterdam

Front Cover
Nanomaterials for Biocatalysis
Copyright Page
Contents
List of contributors
1 Basic Principles
1 Nanobiocatalysis: an introduction
1.1 Introduction
1.2 Metallic nanomaterials
1.2.1 Metal nanomaterials
1.2.2 Metal-oxide based nanomaterials
1.3 Carbonaceous nanomaterial
1.3.1 Graphene and graphene oxide
1.3.2 Carbon nanotube
1.4 Other nanomaterials
1.5 Conclusion
Acknowledgment
References
2 Enzyme immobilized nanomaterials
2.1 Introduction
2.2 Components of the “nano-enzyme conjugates”
2.2.1 Nanomaterial
2.2.1.1 Magnetic NPs
2.2.1.2 Other metal NPs
2.2.1.3 Carbon based NPs
2.2.1.4 Mesoporous silica NPs
2.2.1.5 Polymeric NPs
2.2.2 Synthesis of nanoparticles
2.2.3 Functionalization of NPs
2.3 Enzymes immobilized on nanomaterials
2.3.1 Lipases
2.3.2 α-amylases
2.3.3 Glucose oxidase
2.3.4 Laccases
2.3.5 Multi enzyme systems
2.4 Characterization of enzyme-nano conjugates
2.4.1 Transmission Electron Microscopy and Scanning Electron Microscopy
2.4.2 Fourier transformation infrared spectroscopy
2.4.3 Energy dispersive X-ray
2.4.4 X-ray Diffraction
2.4.5 Thermogravimetric analysis
2.5 Applications of nano-enzyme bioconjugates
2.6 Conclusions and future perspectives
Acknowledgments
References
3 Electrochemical functionalization of carbon nanomaterials and their application in immobilization of enzymes
3.1 Introduction
3.2 Methods of enzyme immobilization
3.2.1 Physical methods
3.2.1.1 Adsorption
3.2.1.2 Entrapment
3.2.2 Chemical methods
3.3 Nanostructured carbon materials
3.4 Functionalization of nanostructured carbon materials for bioelectrocatalysis applications
3.4.1 Noncovalent functionalization
3.4.2 Covalent functionalization
3.5 Some selected examples of electrochemical functionalization and enzyme immobilization
3.6 Conclusions
Acknowledgment
References
4 Mechanisms of interaction among enzymes and supports
4.1 Introduction
4.2 Fundamental aspects of protein structure for enzyme-support interaction
4.2.1 The relationship between enzyme structure and function
4.2.2 Features and properties of the enzymes relevant for interaction with materials
4.2.2.1 Size and shape
4.2.2.2 Isoelectric point
4.2.3 Amino acids involved in enzyme immobilization
4.2.3.1 Noncovalent attachment
4.2.3.2 Covalent attachment
4.2.3.3 Bioaffinity
4.3 Porous materials as effective enzyme supports
4.3.1 Selection of the material
4.3.1.1 SiO2 (Silica)
4.3.1.2 TiO2 (Titania)
4.3.1.3 ZnO (Zinc oxide)
4.3.1.4 Al2O3 (Alumina)
4.3.1.5 Zeolite
4.3.1.6 Metal-organic frameworks
4.3.2 Addressing enzyme requirements tuning materials peculiarities
4.3.2.1 Tailor-made pore size
4.3.2.2 Adjustable synthesis pathway
4.3.2.3 Surface chemistry modification
4.3.2.4 Design of composite systems
4.3.2.5 Postimmobilization strategies
4.3.3 Support characterizations
4.3.3.1 Surface properties
4.3.3.2 Material morphology
4.3.3.3 Bulk structure
4.4 Characterization of immobilized enzymes
4.4.1 Basic characterization: quantification, catalytic performances, and stability
4.4.2 Advanced characterizations: distribution, orientation, and conformational changes of immobilized enzymes
4.5 Conclusions
References
5 The impact of nanoparticles-based enzyme immobilization in biocatalysis
5.1 Introduction
5.2 Magnetic nanoparticles
5.3 Characteristic properties of magnetic nanoparticles
5.3.1 Large surface areas
5.3.2 Magnetic properties
5.3.3 Biocompatibility and nontoxicity
5.4 Structural chemistry of magnetic nanoparticles
5.5 Functionalization and stabilization of magnetic nanoparticles
5.5.1 Inorganic coating
5.5.1.1 Silica coating
5.5.1.2 Metal coating
5.5.2 Organic coating
5.5.2.1 Polymer coating
5.5.2.2 Surfactant coating
5.6 Biocatalysis via enzyme immobilization on nanostructures
5.7 Applications of nanoparticles in enzyme technology and their industrial relevance
5.8 Conclusion and future directions
Acknowledgments
Conflict of interest
References
Further reading
2 Nanomaterlals in Biocatalysts
6 Silica-based nanomaterials in biocatalysis
6.1 Catalytic reactions and biocatalysts
6.1.1 Enzyme biocatalysis
6.1.2 Nanomaterials as biocatalysts
6.1.3 Silica-based nanomaterials
6.1.4 Synthesis and modification of silica nanomaterials
6.1.4.1 Synthesis of biomolecules and enzyme-modified silica nanomaterials for biocatalysis
6.1.4.2 Synthesis of organosilica nanomaterials for biocatalysis
6.1.4.3 Synthesis of metals incorporated silica nanomaterials for biocatalysis
6.1.4.4 Synthesis of polymer-based silica nanomaterials for biocatalysis
6.1.5 Applications of silica nanomaterials as biocatalyst
6.2 Conclusion
Acknowledgments
Declaration of interests
References
7 Enzyme-metal nanobiohybrids in chemobiocatalytic cascade processes
7.1 Introduction
7.2 Synthesis of enzyme–metal hybrid catalysts
7.2.1 Coimmobilization of enzymes and metal nanoparticles on a supporting carrier
7.2.2 Biomimetic synthesis of enzyme-metal nanoparticles catalytic nanobiohybrids
7.3 Classification of enzyme–metal hybrid catalysts (E-MNPs) by metal nano particles
7.3.1 Gold nanoparticle-based enzyme hybrid
7.3.2 Palladium and platinum nanoparticle-based enzyme-metal hybrids
7.3.3 Other metals used for metal-enzyme hybrid catalysts
7.4 Application of enzyme-metal nanoparticle hybrid catalysts in cascade reactions
7.5 Conclusion
Acknowledgments
References
8 Nanostructured organic supports
8.1 Introduction
8.2 Polymeric nanofibers
8.2.1 Fabrication of nanofibers using electrospinning
8.2.2 Immobilization of enzyme on the nanofiber surface
8.3 Polymeric nanoparticles
8.4 Polymeric nanogels
8.5 Polymeric micelles
8.6 Inorganic-organic hybrid nanostructures
8.6.1 Magnetic nanoparticles-polymers hybrid nanostructures
8.6.2 Other inorganic nanoparticles-polymers nanostructures
8.7 Conclusion
References
9 Recent developments of iron-based nanosystems as enzyme-mimicking surrogates of interest in tumor microenvironment treatment
9.1 Introduction
9.2 Biocatalytic activity of FexOy nanomaterials
9.2.1 Catalase mechanism: natural enzymes versus Fe3O4 nanoparticles
9.2.2 Peroxidase mechanism: natural enzymes versus Fe3O4 nanoparticles
9.2.3 Comparison of catalase and peroxidase activity involving Fe3O4 nanoparticles
9.3 Role of Fe-based nanoparticles in tumor cell microenvironments: interaction with hydrogen peroxide and glutathione
9.3.1 Role of ionic Fe species in biological processes
9.3.2 Catalase biomimetic activity of Fe-based nanocatalysts against tumor hypoxia
9.3.3 Peroxidase-like biocatalytic activity of Fe nanosystem for enhanced reacting oxygen species production
9.4 New trends in nanozyme materials: single atom catalysts
9.5 Conclusions and outlook
References
10 Metal organic frameworks for biocatalysis
10.1 Introduction
10.2 Synthesis of enzyme-metal-organic frameworks composites
10.2.1 Surface attachment
10.2.2 Covalent conjugation
10.2.3 Pore/channel infiltration
10.2.4 In situ encapsulation
10.3 Application of enzyme-metal-organic frameworks composites
10.3.1 Biological manufacturing
10.3.2 Environmental protection
10.3.3 Disease diagnosis and therapy
10.4 Summary and outlook
References
11 Enzyme immobilization on magnetic nanoparticle supports for enhanced separation and recycling of catalysts
11.1 Introduction
11.1.1 Covalent binding
11.1.2 Physical adsorption
11.1.3 Encapsulation
11.1.4 Crosslinking
11.2 Magnetic support materials for enzyme immobilization
11.2.1 Magnetism and magnetic materials
11.2.2 Iron oxide nanoparticles as magnetic supports
11.3 Immobilization methods on magnetic supports
11.4 Single enzyme systems
11.5 Multi-enzyme cascade systems
11.6 Cofactor-dependent systems
11.7 Conclusion and future outlooks
References
12 Polymers and metal−organic frameworks as supports in biocatalysis: applications and future trend
12.1 Introduction to biocatalysis
12.2 Enzyme immobilization on polymers, biopolymers, and metal−organic frameworks
12.2.1 Enzyme immobilization techniques
12.2.1.1 Surface immobilization
12.2.1.2 Covalent linkage
12.2.1.3 Entrapment
12.2.1.4 Cross-linked enzyme aggregates
12.3 Applications of immobilized biocatalyst
12.3.1 Biodiesel production
12.3.2 Synthesis of flavor ester
12.3.3 Pharmaceutical applications
12.3.4 Biosensors
12.3.5 Protein digestion and chemical degradation
12.4 Limitations and challenges in the application of organic materials as enzyme supports
References
13 Carbon nanotubes/nanorods in biocatalysis
13.1 Introduction
13.2 Carbon nanotubes in biocatalysis
13.3 Multi-walled carbon nanotubes in biocatalysis
13.4 Non-covalent immobilization of enzymes on multi-walled carbon nanotubes
13.5 Covalent immobilization of enzymes on multi-walled carbon nanotubes
13.6 Single-walled carbon nanotubes in biocatalysis
13.7 Hybrid materials based on carbon nanotubes in biocatalysis
13.8 Other carbon nanoshapes in biocatalysis
13.9 Conclusions
Acknowledgment
References
14 Gold nanoparticles for biocatalysis
14.1 Introduction
14.2 Gold as catalyst for chemical and biochemical reactions
14.2.1 Gold nanoclusters as a catalyst
14.2.2 Gold nanoparticles in catalysis
14.2.3 Anisotropic gold particles in catalysis
14.2.3.1 Gold nanorods (AuNR)
14.2.3.2 Gold nanostars (AuNS)
14.2.3.3 Biotemplated gold catalysts
14.3 Gold as support of biocatalytic compounds (enzymes)
14.3.1 Properties of gold nanoparticles
14.3.2 Enzyme immobilization onto gold nanoparticles
14.3.3 Enzyme-gold nanoparticles as biosensors
14.3.4 Enzymes in biofuel cells
14.4 Synthesis approaches of gold nanoparticles
14.4.1 Colloidal synthesis of gold nanoparticles
14.4.2 Synthesis methods and capping agents
14.5 Advanced techniques for the characterization of gold nanoparticles used as enzymes support
14.5.1 Transmission electron microscopy and scanning transmission electron microscopy
14.5.2 X-ray energy dispersive spectroscopy
14.5.3 Raman spectroscopy
14.5.4 Dynamic light scattering
Acknowledgments
References
3 Emerging Applications
15 Nanobiocatalyst for drug delivery
15.1 Introduction
15.2 Therapeutic enzymes
15.3 Strategies for therapeutic enzyme delivery
15.3.1 Stabilization of carrier-free enzymes
15.3.1.1 Bioconjugation
15.3.1.2 Cross-linked biocatalyst
15.3.2 Enzyme stabilization with carriers
15.3.2.1 Biocatalyst entrapment and microencapsulation
15.4 Nanocarriers for biocatalysis
15.4.1 Metal nanoparticles
15.4.2 Polymeric nanoparticles
15.4.3 Solid lipid carriers
15.4.4 Protein cages
15.4.5 Single-enzyme nanoparticles
15.5 Conclusions and future prospects
Acknowledgments
References
16 Enzymatic biosensors for the detection of water pollutants
16.1 Introduction
16.2 Aacetylcholinesterase-based biosensors
16.3 Electrochemical biosensors
16.4 Optical biosensors
16.5 Polyphenol oxidases-based biosensors
16.6 Biosensors based on zinc-oxide nanoparticles
16.7 Biosensors based on gold nanoparticles
16.8 Biosensor based on α-Fe2O3 nanocrystals
16.9 Biosensors based on polypyrrole nanotubes
16.10 Biosensors based on carbon nanomaterials
16.11 Biosensor based on poly(3,4-ethylenedioxythiophene)-iridium oxide
16.12 Peroxidase-based biosensors
16.13 General characteristics of peroxidases
16.14 Nanomaterial-peroxidase-based biosensors
16.15 Biosensors for H2O2 detection
16.16 Biosensors for phenolic and amine compounds detection
16.17 Biosensors for pesticides detection
16.18 Conclusion
References
17 Biocatalytic nanomaterials as an alternative to peroxidase enzymes
17.1 Introduction
17.2 Overview of peroxidase enzyme
17.3 Peroxidase-like activity of nanoparticles
17.3.1 Nanosized metal particles
17.3.2 Nanosized metal oxide particles
17.3.3 Nanosized carbon-based particles
17.3.4 Nanosized polymeric particles
17.3.5 Nanosized composites
17.4 Applications of biocatalytic nanomaterials with peroxidase-like activity
17.4.1 Biosensor application
17.4.1.1 Detection of biomolecules
17.4.1.2 Detection of heavy metal ions
17.4.1.3 Detection of proteins
17.4.1.4 Detection of nucleic acids
17.4.1.5 Detection of cancer cells
17.4.2 Wastewater treatment
17.4.3 Antibacterial agents
17.4.4 Other novel applications
17.4.4.1 Bioimaging
17.4.4.2 Therapeutic agents
17.4.4.3 Bioremediation
17.5 Future perspective
17.6 Conclusion
References
18 Lignin peroxidase–a robust tool for biocatalysis
18.1 Introduction
18.2 Ligninolytic system of white-rot fungi
18.3 Lignocellulosic wastes
18.4 Production, purification, and characterization of lignin peroxidase
18.5 Enzyme immobilization–advantages and disadvantages
18.6 Selection of best immobilization carrier
18.7 Methods for enzyme immobilization
18.7.1 Physical adsorption
18.7.2 Covalent binding
18.7.3 Cross-linking
18.7.4 Entrapment
18.7.5 Microencapsulation
18.8 Selection of appropriate immobilization method
18.9 Natural polymers for enzyme immobilization
18.9.1 Alginate
18.9.2 Chitosan
18.9.3 Gelatin
18.10 Synthetic polymers as supports for enzyme immobilization
18.10.1 Nylon membrane
18.10.2 Polyvinyl alcohol
18.11 Industrial applications of lignin peroxidase
18.11.1 Dye decolorization
18.11.2 Delignification of plant biomass
18.12 Conclusion and future perspectives
18.13 Competing interests
References
19 Laccases: catalytic and functional attributes for robust biocatalysis
19.1 Introduction
19.2 Laccase and their general properties
19.3 Laccase structure and active site
19.4 Catalytic mechanism of laccase
19.5 Difference of laccase with other oxidases
19.6 Laccase substrates and inhibitors
19.7 Occurrence of laccase
19.7.1 Plant laccase
19.7.2 Bacterial laccase
19.7.3 Fungal laccases
19.8 Production of laccase
19.9 Purification and characterization of laccase
19.10 Immobilization of laccase
19.10.1 Adsorption
19.10.2 Entrapment
19.10.3 Covalent binding
19.10.4 Cross-linking of enzyme aggregates
19.11 Environmental bioremediation by laccase
19.12 Conclusion and directions
References
Further reading
20 Microbial exo-polygalacturonase—a versatile enzyme with multiindustrial applications
20.1 Pectinases
20.2 Substrate for pectinase enzymes
20.2.1 Homogalacturonan
20.2.2 Rhamnogalacturonan I
20.2.3 Rhamnogalacturonan II
20.3 History of pectinases
20.4 Sources of pectinases
20.5 Structural topology of pectinase
20.6 Modern classification of pectinases
20.6.1 Glucosidases
20.6.2 Esterases
20.6.3 Pectin lyases
20.7 Production of exo-polygalacturonase
20.7.1 Solid-state fermentation and submerged state fermentation
20.7.2 Factors affecting solid-state fermentation (SSF) for polygalaturonase production
20.7.2.1 Spore size
20.7.2.2 Moisture level
20.7.2.3 Substrate selection
20.7.2.4 Glucose level
20.7.2.5 Production temperature
20.7.3 Solid-state fermentation versus submerged state fermentation
20.8 Biochemical characterization
20.8.1 Purification
20.8.2 Effect of pH
20.8.3 Metal ion effect
20.8.4 Carbon and nitrogen sources
20.8.5 Phenolic contents
20.8.6 pH and thermal stability profiles of pectinases
20.8.7 Viscosity, turbidity and juice yield
20.9 Industrial applications of pectinases
20.9.1 Juice and wine industry
20.9.2 Pulp and paper industry
20.9.3 Pectic wastewater pretreatment
20.9.4 Plant bast fibers degumming
20.9.5 Retting of plant fibers
20.9.6 Bioscouring of cotton fibers and textile processing
20.9.7 Coffee and tea fermentations
20.9.8 Plant disease control
20.9.9 Oil extraction
20.9.10 Pectinase and dietary fibers
20.9.11 Clarification and viscosity reduction of fruit juices
20.9.12 Phenolic contents
Acknowledgments
Declaration of interests
References
21 Therapeutic applications
21.1 Introduction
21.2 Enzyme-immobilized nanomaterials
21.2.1 Enzyme-immobilized nanomaterials for antithrombotic therapy
21.2.2 Enzyme-immobilized nanomaterials for Gaucher’s disease treatment
21.2.3 Enzyme-immobilized nanomaterials for the treatment of Pseudomonas aeruginosa infections in patients with cystic fibrosis
21.2.4 Enzyme-immobilized nanomaterials for phenylketonuria treatment
21.2.5 Enzyme-immobilized nanomaterials for neonatal jaundice treatment
21.2.6 Enzyme-immobilized nanomaterials for the treatment of bone regeneration and hypophosphatasia
21.3 Nanomaterials displaying enzyme-like activities
21.3.1 Iron-based nanozymes for therapy
21.3.1.1 Iron-based nanozymes for tumor therapy
21.3.2 Carbon-based nanozymes
21.3.3 Carbon-based nanozymes for therapy
21.4 Multifunctional nanozymes
21.4.1 Multifunctional nanozymes with antioxidant activity
21.4.2 Multifunctional nanozymes for neurodegenerative diseases treatment
21.4.2.1 Multifunctional nanozymes for Parkinson’s disease therapy
21.4.2.2 Multifunctional nanozymes for Alzheimer’s disease therapy
21.4.3 Multifunctional nanozymes for antibacterial applications
21.4.4 Multifunctional nanozymes for hyperuricemia treatment
21.5 Single-atom catalysts
21.5.1 Carbon-supported single-atom catalysts
21.5.2 Single-atom catalysts for cancer treatment
21.5.3 Single-atom catalysts for antibacterial applications and wound healing
21.5.4 Single-atom catalysts as scavengers for oxidative stress cytoprotection
21.5.5 Single-atom catalysts for photodynamic therapy
21.6 New nanodevices for therapy: nanomotors based on gated enzyme-powered Janus nanoparticles
21.7 Concluding remarks
Acknowledgments
References
22 Nanosupport immobilized β-galactosidases, their stabilization, and applications
22.1 Introduction
22.2 Sources of β-galactosidase
22.3 Immobilization of enzymes
22.3.1 Factors considered prior to enzyme immobilization
22.3.1.1 Choice of supports
22.3.2 Factors influencing the biochemical activity of the immobilized enzyme
22.3.2.1 Immobilization methods
22.3.2.2 Concentration gradient
22.3.2.3 Size of the carrier
22.3.2.4 Diffusion
22.3.2.5 Diffusion limitations
22.3.3 Nanoimmobilization
22.3.4 Methods of enzyme immobilization on nanomaterial
22.3.4.1 Electrostatic adsorption
22.3.4.2 Covalent binding
22.3.4.3 Bioaffinity based binding
22.3.4.4 Microencapsulation
22.4 Applications of nanoimmobilized β-galactosidase
22.4.1 Production of lactose free dairy products
22.4.2 Application in whey utilization
22.4.3 Biosensor applications
22.4.4 Food technology
22.4.5 Environmental remediation
22.4.6 Medical applications
22.4.7 Production of galctooligosaccharide
22.5 Conclusion and future outlook
Acknowledgments
References
23 Nanocarbon for bioelectronics and biosensing
23.1 Introduction
23.2 Properties and biocompatibility of nanocarbon
23.2.1 Nanocarbon
23.2.2 Biocompatibility of nanocarbon
23.3 Nanocarbon for bioelectronic applications
23.3.1 Gene therapy and nanocarrier
23.4 Soft nanocarbon bioelectronics for precision therapy
23.5 Nanocarbon bioelectronics for tissue engineering
23.5.1 Graphene-based nanoelectronics for tissue engineering
23.6 Carbon nanotubes-based nanoelectronics for tissue engineering
23.7 Applications of nanocarbon-based biosensors
23.7.1 Biophysical biosensor and monitoring
23.7.1.1 Biopotential monitoring
23.8 Skin temperature monitoring
23.9 Broad range human body movement monitoring
23.10 Electrochemical biosensor
23.10.1 Enzymatic biosensor
23.10.2 DNA biosensor
23.10.3 Protein biosensor
23.10.4 Immunobiosensors
23.11 Conclusion
References
Index
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