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Rational design of enzyme-nanomaterials / edited by Chalia Vijaya Kumar.

Contributor(s): Material type: TextTextSeries: Methods in enzymology ; v. 571.Publisher: Cambridge, MA : Academic Press is an imprint of Elsevier, 2016Description: 1 online resource : illustrations (chiefly color)Content type:
  • text
Media type:
  • computer
Carrier type:
  • online resource
ISBN:
  • 9780128048337
  • 0128048336
Subject(s): Genre/Form: Additional physical formats: Print version:: Rational Design of Enzyme-Nanomaterials.DDC classification:
  • 660.6 23
LOC classification:
  • TP248.65.E59
NLM classification:
  • QT 36.5
Online resources:
Contents:
Front Cover; Rational Design of Enzyme-Nanomaterials; Copyright; Contents; Contributors; Preface; Acknowledgments; Chapter One: Preparation of Biocatalytic Microparticles by Interfacial Self-Assembly of Enzyme-Nanoparticle Conjugates Aro ... ; 1. Theory; 2. Equipment; 3. Materials; 3.1. Buffer Preparation; 4. Protocol; 4.1. Duration; 4.2. Preparation; 5. Step 1: Nanoparticle Synthesis; 5.1. Overview; 5.2. Duration; 5.3. Tip; 5.4. Tip; 5.5. Tip; 5.6. Tip; 5.7. Tip; 6. Step 2: Purification of Enzyme; 6.1. Overview; 6.2. Duration; 6.3. Tip; 6.4. Tip.
7. Step 3: Preparation of the Aqueous Phase and Oil Phase7.1. Overview; 7.2. Duration; 7.3. Tip; 7.4. Tip; 7.5. Tip; 7.6. Tip; 7.7. Tip; 7.8. Tip; 7.9. Tip; 8. Step 4: Microparticle Assembly; 8.1. Overview; 8.2. Duration; 8.3. Tip; 8.4. Tip; 8.5. Tip; 9. Step 5: Microparticle Washing; 9.1. Overview; 9.2. Duration; 9.3. Tip; 9.4. Tip; 10. Conclusions; References; Chapter Two: Monitoring Enzymatic Proteolysis Using Either Enzyme- or Substrate-Bioconjugated Quantum Dots; 1. Introduction; 1.1. Enzyme-Nanoparticle Constructs.
1.2. Quantification Assay for Observing Modified Kinetics with Enzyme-QD Conjugates1.3. Enzyme Activity Sensors Based on Transient QD-Enzyme Interactions; 2. Quantification Assay for Observing Modified Kinetics with Enzyme-QD Conjugates; 2.1. Materials; 2.1.1. Equipment; 2.1.2. Reagents; 2.2. Enzyme Assembly onto QDs; 2.3. Obtaining Kinetic Data of QD-Enzyme Constructs; 2.4. Analyzing the Data; 3. Enzyme Activity Sensors Based on Transient QD-Enzyme Interactions; 3.1. Materials; 3.1.1. General Equipment; 3.1.2. Peptide Labeling; 3.1.2.1. Equipment; 3.1.2.2. Reagents.
3.1.3. Peptide Precleaving3.1.3.1. Equipment; 3.1.3.2. Reagents; 3.1.4. QD-Peptide Construct; 3.1.4.1. Equipment; 3.1.4.2. Reagents; 3.1.5. Spectral Characterization and Kinetics Measurements; 3.1.5.1. Equipment; 3.1.5.2. Reagents; 3.2. Peptide Labeling; 3.2.1. Single Cysteine Labeling; 3.2.2. Dual Labeling for Control Experiments; 3.2.3. Peptide Purification, Quantification, and Storage; 3.3. Peptide Precleaving; 3.4. QD-Peptide Construct; 3.4.1. Formation; 3.4.2. Characterization; 3.5. Spectral Characterization; 3.6. Fixed Enzyme Experiments; 3.7. Fixed Substrate Experiments.
Summary: Rational Design of Enzyme-Nanomaterials, the new volume in the Methods in Enzymology series, continues the legacy of this premier serial with quality chapters authored by leaders in the field. This volume covers research methods in rational design of enzyme-nanomaterials, and includes sections on such topics as conjugation of enzymes and dextran-aldehyde polymers, improved activity of enzymes bound to titanate nanosheet, nano-layered 'stable-on-the-table' biocatalysts and nanoparticle-based enzyme sensors.
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Rational Design of Enzyme-Nanomaterials, the new volume in the Methods in Enzymology series, continues the legacy of this premier serial with quality chapters authored by leaders in the field. This volume covers research methods in rational design of enzyme-nanomaterials, and includes sections on such topics as conjugation of enzymes and dextran-aldehyde polymers, improved activity of enzymes bound to titanate nanosheet, nano-layered 'stable-on-the-table' biocatalysts and nanoparticle-based enzyme sensors.

Includes indexes.

Online resource; title from title details screen (ScienceDirect, viewed April 28, 2016).

880-01 Front Cover; Rational Design of Enzyme-Nanomaterials; Copyright; Contents; Contributors; Preface; Acknowledgments; Chapter One: Preparation of Biocatalytic Microparticles by Interfacial Self-Assembly of Enzyme-Nanoparticle Conjugates Aro ... ; 1. Theory; 2. Equipment; 3. Materials; 3.1. Buffer Preparation; 4. Protocol; 4.1. Duration; 4.2. Preparation; 5. Step 1: Nanoparticle Synthesis; 5.1. Overview; 5.2. Duration; 5.3. Tip; 5.4. Tip; 5.5. Tip; 5.6. Tip; 5.7. Tip; 6. Step 2: Purification of Enzyme; 6.1. Overview; 6.2. Duration; 6.3. Tip; 6.4. Tip.

7. Step 3: Preparation of the Aqueous Phase and Oil Phase7.1. Overview; 7.2. Duration; 7.3. Tip; 7.4. Tip; 7.5. Tip; 7.6. Tip; 7.7. Tip; 7.8. Tip; 7.9. Tip; 8. Step 4: Microparticle Assembly; 8.1. Overview; 8.2. Duration; 8.3. Tip; 8.4. Tip; 8.5. Tip; 9. Step 5: Microparticle Washing; 9.1. Overview; 9.2. Duration; 9.3. Tip; 9.4. Tip; 10. Conclusions; References; Chapter Two: Monitoring Enzymatic Proteolysis Using Either Enzyme- or Substrate-Bioconjugated Quantum Dots; 1. Introduction; 1.1. Enzyme-Nanoparticle Constructs.

1.2. Quantification Assay for Observing Modified Kinetics with Enzyme-QD Conjugates1.3. Enzyme Activity Sensors Based on Transient QD-Enzyme Interactions; 2. Quantification Assay for Observing Modified Kinetics with Enzyme-QD Conjugates; 2.1. Materials; 2.1.1. Equipment; 2.1.2. Reagents; 2.2. Enzyme Assembly onto QDs; 2.3. Obtaining Kinetic Data of QD-Enzyme Constructs; 2.4. Analyzing the Data; 3. Enzyme Activity Sensors Based on Transient QD-Enzyme Interactions; 3.1. Materials; 3.1.1. General Equipment; 3.1.2. Peptide Labeling; 3.1.2.1. Equipment; 3.1.2.2. Reagents.

3.1.3. Peptide Precleaving3.1.3.1. Equipment; 3.1.3.2. Reagents; 3.1.4. QD-Peptide Construct; 3.1.4.1. Equipment; 3.1.4.2. Reagents; 3.1.5. Spectral Characterization and Kinetics Measurements; 3.1.5.1. Equipment; 3.1.5.2. Reagents; 3.2. Peptide Labeling; 3.2.1. Single Cysteine Labeling; 3.2.2. Dual Labeling for Control Experiments; 3.2.3. Peptide Purification, Quantification, and Storage; 3.3. Peptide Precleaving; 3.4. QD-Peptide Construct; 3.4.1. Formation; 3.4.2. Characterization; 3.5. Spectral Characterization; 3.6. Fixed Enzyme Experiments; 3.7. Fixed Substrate Experiments.

Includes bibliographical references and indexes.

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