Enzyme Microfluidics | Buch | 978-0-443-52054-9 | www.sack.de

Buch, Englisch, Format (B × H): 152 mm x 229 mm

Enzyme Microfluidics


Erscheinungsjahr 2026
ISBN: 978-0-443-52054-9
Verlag: Elsevier Science & Technology

Buch, Englisch, Format (B × H): 152 mm x 229 mm

ISBN: 978-0-443-52054-9
Verlag: Elsevier Science & Technology


Enzyme Microfluidics, Volume 737 in the Methods in Enzymology series, presents detailed methodological descriptions and protocols that cover a wide range of microfluidics-based approaches for mechanistic enzymology, high-throughput screening, and enzyme engineering campaigns. The volume includes both established methods as well as advances in the field. Sections in this new release cover four unique sections, including Chips and Reagents, Enzyme Characterization, Enzyme Engineering, and Moving Beyond Microfluidics (from micro to nanoscale). Specific chapters delve into Joint Methods for Fabricating Microfluidic Chips, A liquid handling robotic workflow for quantifying the activity of antibiotic resistance genes (ARGs) in cell-free protein synthesis, and much more.

Additional chapters cover Preparation of uniform microcrystals by droplet microfluidics for time-resolved serial crystallography, Droplet microfluidic HDX for investigating highly dynamic proteins, An Accessible, Low-Cost Platform for High-Throughput Microfluidic Enzyme Kinetics, High-Throughput Data Processing, DA-MEK, Mass Spectrometry of Droplets, Digital Bioassay Using a Femtoliter Reactor Array Device, Confocal absorbance droplet sorting, Sequence-Function Data Analysis from Microfluidics Screening, and much more.

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Weitere Infos & Material


Section 1: Chips and Reagents
1. Joint Methods for Fabricating Microfluidic Chips
2. A liquid handling robotic workflow for quantifying the activity of antibiotic resistance genes (ARGs) in cell-free protein synthesis
Simon Moore

Section 2: Enzyme Characterisation
3. Preparation of uniform microcrystals by droplet microfluidics for time-resolved serial crystallography
Jonathan West
4. Droplet microfluidic HDX for investigating highly dynamic proteins
Jonathan West
5. An Accessible, Low-Cost Platform for High-Throughput Microfluidic Enzyme Kinetics
Craig Markin
6. High-Throughput Data Processing
Margaux Pinney
7. DA-MEK
Polly Fordyce
8. Mass Spectrometry of Droplets
Perdita Elizabeth Barran
9. Digital Bioassay Using a Femtoliter Reactor Array Device
Hiroyuki Noji

Section 3: Enzyme Engineering
10. Confocal absorbance droplet sorting
Jean-Christophe Baret
11. Sequence-Function Data Analysis from Microfluidics Screening
Maximilian Gantz
12. Passive microfluidic system for droplet sorting based on proteolytic activity
Tomasz Kaminski
13. Directed Evolution of computationally designed enzymes on integrated devices
Richard Obexer
14. TBD
Miriam Rosenbaum
15. TBD
Guangyu Yang
16. TBD
Fuqiang Ma

Section 4: Moving beyond microfluidics (from micro to nanoscale)
17. Lithographic patterning of nanoscale enzyme arrays
Lu Shin Wong


Markin, Craig
Craig Markin is a Fellow jointly appointed in the Manchester Institute of Biotechnology and the Division of Molecular and Cellular Function in the Faculty of Biology, Medicine, and Health at The University of Manchester. He received his PhD in 2013 from the University of Alberta, where he worked with Prof Leo Spyracopoulos studying the synthesis and recognition of K63-linked polyubiquitin chains in the DNA damage response. This was followed by postdoctoral work at Stanford University, in the labs of Prof Polly Fordyce and Prof Dan Herschlag, which spurred his interest in high-throughput enzymology and microfluidic technologies. He started his independent group in 2023 with a focus on developing and applying high-throughput technologies to map and better understand the sequence-structure-function relationships governing enzyme function and regulation.

Allen, Karen N.
Dr. Karen N. Allen works at the Department of Chemistry of the Boston University, the Metcalf Center for Science and Engineering

Christianson, David
After completing studies for the A.B., A.M., and Ph.D. degrees in chemistry at Harvard University, David W. Christianson joined the faculty of the University of Pennsylvania, where he is currently the Roy and Diana Vagelos Professor in Chemistry and Chemical Biology. At Penn, Christianson’s research focuses on the structural and chemical biology of the zinc-dependent histone deacetylases as well as enzymes of terpene biosynthesis. His research accomplishments have been recognized by several awards, including the Pfizer Award in Enzyme Chemistry and the Repligen Award in Chemistry of Biological Processes from the American Chemical Society, a Guggenheim Fellowship, and the Elizabeth S. and Richard M. Cashin Fellowship from the Radcliffe Institute for Advanced Study at Harvard University. Christianson is also a dedicated classroom teacher, and his accomplishments in this regard have been recognized by the Lindback Award for Distinguished Teaching at Penn and a Rhodes Trust Inspirational Educator Award from Oxford University. Christianson has also held visiting professorships in the Department of Biochemistry at Cambridge University and the Department of Chemistry and Chemical Biology at Harvard University. Christianson has served with Prof. Anna Pyle as Co-Editor-in-Chief of Methods in Enzymology since 2015.

Obexer, Richard
Richard Obexer is a BBSRC Discovery Fellow at the Manchester Institute of Biotechnology and the Department of Chemistry at The University of Manchester. He completed his PhD in 2016 in Chemistry at ETH Zürich under Prof Donald Hilvert where he focused on directed evolution of computationally designed enzymes using droplet-based microfluidics. He subsequently undertook postdoctoral research in the laboratories of Prof. Hiroaki Suga, Prof. Dek Woolfson, and Dr. Sarah Lovelock, focusing on mRNA display for the discovery of macrocyclic peptide binders, protein design for liquid–liquid phase separation, and biocatalytic approaches to the production of therapeutic oligonucleotides. He established his independent research group in 2023. His work combines de novo protein design with ultra-high-throughput directed evolution to uncover sequence–structure–function relationships that govern enzyme catalysis, enabling the development of efficient and programmable biocatalysts.



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