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181204s2018 enka ob 001 0 eng d |
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|a GBB8N9426
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|a 019171294
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|a 9780128163610
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|a (OCoLC)1077292081
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|a TP248.E5
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|a SCI
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|a 660.634
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|a Enzymes of energy technology /
|c edited by Fraser Armstrong.
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|a First edition.
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|a United Kingdom :
|b Academic Press,
|c 2018.
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|a 1 online resource :
|b color illustrations
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|a text
|b txt
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|a computer
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|a online resource
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|a data file
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|a Methods in enzymology ;
|v volume 613
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|a Online resource; title from PDF title page (EBSCO, viewed December 5, 2018).
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|a Includes bibliographical references and index.
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|a Front Cover; Enzymes of Energy Technology; Copyright; Contents; Contributors; Preface; Chapter One: Purification of fully active and crystallizable photosystem II from thermophilic cyanobacteria; 1. Introduction; 2. Growth and harvest of cells; 3. Isolation of thylakoid membranes; 4. Isolation of crude PSII particles; 5. Purification of PSII dimers; 6. Characterization of the purified PSII core dimers; 7. Crystallization of purified PSII dimers; Acknowledgments; References; Chapter Two: Production and manipulation of blue copper oxidases for technological applications; 1. Introduction
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|a 2. Heterologous production of fungal laccases2.1. Cloning; 2.1.1. Site-directed mutagenesis; 2.1.2. Yeast recombination; 2.2. Transformations; 2.2.1. S. cerevisiae; 2.2.2. A. niger; 2.3. Screening for laccase secreting transformants in S. cerevisiae and A. niger; 2.3.1. Screening of clones from deep-well or microtiter plate cultures; 2.3.2. Screening of laccase producing transformants on petri dish plates; 2.3.3. Screening of activity on 96-well plate; 2.3.4. ELISA screening; 2.4. Fermentation in A. niger; 2.4.1. Preparation of spore inoculum and storage
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|a 2.4.2. Production in bioreactor and growth parameters3. General purification procedure and characterization; 3.1. Purification procedure; 3.1.1. Assay procedures; 3.1.2. Laccase purification procedure; 4. Applications; 4.1. General procedure for an oriented covalent grafting of the laccase surface; 4.1.1. Preparation of laccase variants for single-site anchoring; 4.1.2. Reductive amination of lysine; 4.1.3. Evaluation of the grafting; 4.2. Hybridization with materials; 5. Conclusions; Acknowledgment; References; Further reading
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|a Chapter Three: Production and spectroscopic characterization of lytic polysaccharide monooxygenases1. Introduction; 2. Expression and purification of LPMOs; 2.1. Recombinant expression and purification from the E. coli periplasm; 2.2. Recombinant expression and purification from the E. coli cytoplasm; 2.3. Recombinant expression and purification from yeast; 2.4. Recombinant expression and purification from fungi; 3. EPR spectroscopy; 3.1. EPR sample preparation for LPMOs; 3.2. Multifrequency collection; 3.3. Simulation procedures; Acknowledgments; References; Further reading
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|a Chapter Four: A novel overproduction system for the structural determination of a proton-pumping hydrogen-producing [NiFe ... 1. Introduction; 1.1. Hydrogen catalysis in nature; 1.2. Escherichia coli hydrogenase-2 genetic and structural arrangement; 1.3. First approaches to overexpression of a [NiFe]-hydrogenase; 2. Overproduction of fully formed holo-Hyd-2; 2.1. Molecular biology strategies for the overproduction of Hyd-2; 2.1.1. Design of overexpression plasmid pO; 2.1.1.1. Equipment; 2.1.1.2. Reagents and buffers; 2.1.1.3. Procedures; 2.1.2. Design of overexpression strain HJ001-hyp
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|a Enzymes of Energy Technology, Volume 613 in the Methods in Enzymology series, highlights new advances in the field, with this updated volume presenting interesting chapters written by an international board of authors. Chapters include Purification of fully active and crystallizable photosystem II from thermophilic cyanobacteria, Production and manipulation of [NiFeSe]-hydrogenases for renewable hydrogen research, Hydrogen production by [FeFe]-hydrogenases, Production and properties of enzymes that activate and produce carbon monoxide, Recombinant [NiFe]-hydrogenases from E. coli, Working with nitrogenase, Oxygen--tolerant [NiFe]-hydrogenases, Cytoplasmic and Membrane Bound Hydrogenases from the hyperthermophile Pyrococcus furiosus, and more. Additional sections cover Enzymatic conversion of methane into useful chemicals, Production and investigations of trans-membrane electron transfer protein, Characterization of post-translational modifications in methyl-coenzyme M reductase in diverse methanogens by mass-spectrometry, Reductive activation of carbon dioxide by formate dehydrogenases, and Lytic polysaccharide monooxygenases in biofuel processing. 14. Production and manipulation of blue copper oxidases for technological applications Yasmina Mekmouche.
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|a Enzymes
|x Industrial applications.
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| 650 |
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|a SCIENCE
|x Chemistry
|x Industrial & Technical.
|2 bisacsh
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|a TECHNOLOGY & ENGINEERING
|x Chemical & Biochemical.
|2 bisacsh
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| 650 |
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|a Enzymes
|x Industrial applications.
|2 fast
|0 (OCoLC)fst00913615
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| 655 |
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|a Electronic books.
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| 700 |
1 |
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|a Armstrong, Fraser.,
|e editor.
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|a Methods in enzymology ;
|v v. 613.
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|3 ScienceDirect
|u https://www.sciencedirect.com/science/bookseries/00766879/613
|z Full Text via HEAL-Link
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