E-Book, Englisch, Band Volume 714, 412 Seiten
Reihe: Methods in Enzymology
Tischler Biocatalysis
1. Auflage 2025
ISBN: 978-0-443-31789-7
Verlag: Elsevier Science & Techn.
Format: EPUB
Kopierschutz: 6 - ePub Watermark
E-Book, Englisch, Band Volume 714, 412 Seiten
Reihe: Methods in Enzymology
ISBN: 978-0-443-31789-7
Verlag: Elsevier Science & Techn.
Format: EPUB
Kopierschutz: 6 - ePub Watermark
Biocatalysis, Volume 714 provides a wide range of themes dealing with the identification and application of biocatalysts. This includes various formats such as whole-cell or cell-free biocatalysis as well as immobilized variants. Specific chapters in this new release include Biocatalysis: How to select the proper mode of application, Documentation in biocatalysis and data handling, Mining metagenomes from extremophiles as resource for novel glycoside hydrolases for industrial applications, Functional Metaproteomics, Sequence-function relation for the prediction of enzyme properties: A case study on flavin-dependent oxidases, P450 monooxygenase in whole-cell format, and more.Additional sections cover Regio- and Stereospecific oxidation based on di-iron monooxygenases producing whole cells, Recombinant enzyme expression and targeted mutagenesis in Aromatoleum species, C.necator as a model organism for CO2-based biotechnology, Cupriavidus in whole-cell biocatalysis, Whole-cell biocatalysis with Myxobacteria, Streptomyces for natural product formation: Targeted mutagenesis in PKS, Reductive Amination: Methods for cell-free and whole-cell biocatalysis, Challenges and good practices on transaminase-catalysed synthesis of optically pure amines, W-enzymes in biocatalysis: Chances and difficulties for the user, Atroposelective biocatalysis employing ADHs, Applications of alcohol oxidases, and much more. - Provides guidance on how to identify, produce, describe, and apply biocatalysts, including documentation - Includes broad perspectives on biocatalysis, including its advantages as well as its hurdles - Presents a plethora of applications of a diverse set of enzyme-based catalysis