D
David J. Leak
Researcher at University of Bath
Publications - 127
Citations - 9692
David J. Leak is an academic researcher from University of Bath. The author has contributed to research in topics: Fermentation & Chemistry. The author has an hindex of 31, co-authored 118 publications receiving 8681 citations. Previous affiliations of David J. Leak include University of Warwick & National Technical University.
Papers
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Journal ArticleDOI
Are eucalyptus harvest residues a truly burden-free biomass source for bioenergy? A deeper look into biorefinery process design and Life Cycle Assessment
Guilherme Pessoa Nogueira,Guilherme Pessoa Nogueira,Marcelle McManus,David J. Leak,Telma Teixeira Franco,Marina O.S. Dias,Carla Kazue Nakao Cavaliero +6 more
TL;DR: In this article, an integrated biorefinery process simulation and a Life Cycle Assessment of the coproduction of ethanol and electricity was performed to identify technical and environmental bottlenecks.
Book ChapterDOI
Mechanistic Studies on the Mode of Action of Methane Monooxygenase
Howard Dalton,David J. Leak +1 more
TL;DR: Kinetic measurements suggest that the rate limiting step in the oxidation is oxidation of the bound substrate rather than the supply of electrons to the enzyme-bound substrate, and substrate specificity data from a variety of sources has been reassessed, enabling comparison of the two enzyme systems and proposals concerning the topography of the active site of the soluble enzyme.
Journal ArticleDOI
OnpA, an Unusual Flavin-Dependent Monooxygenase Containing a Cytochrome b5 Domain
TL;DR: Results indicate that OnpA is an unusual FAD-dependent monooxygenase containing a fused cytochrome b(5) domain that is essential for its activity and demonstrate a link between cy tochrome b (5) and flavin-dependent Monooxygenases.
Journal ArticleDOI
Heterologous Microcompartment Assembly in Bacillaceae: Establishing the Components Necessary for Scaffold Formation.
TL;DR: The feasibility of constructing cell factories for small molecules in industrially important Bacillus and Parageobacillus spp.
Journal ArticleDOI
Characterization of the first naturally thermostable terpene synthases and development of strategies to improve thermostability in this family of enzymes.
TL;DR: The first examples of natural TSs exhibiting thermostability are characterized, which catalyse the formation of the sesquiterpene τ‐muurolol at temperatures up to 78 °C and were used as a model to inform the rational engineering of another TS, with the same specificity but low sequence identity to the model.