Special Issue "Bioprocess Engineering and Enzyme Application"

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".

Deadline for manuscript submissions: 31 March 2021.

Special Issue Editors

Dr. Scott A. Walper

Guest Editor
Naval Research Laboratory, Washington, D.C., United States
Interests: bioremediation; synthetic biology; community engineering
Dr. Gregory A. Ellis

Guest Editor
Naval Research Laboratory, Washington, D.C., United States
Interests: synthetic biology; metabolomics; natural products

Special Issue Information

Dear Colleagues,

In nature, biological systems are able to conduct highly efficient catabolic and anabolic reactions within the complicated matrix that is the cellular environment. These biochemical reactions are driven by proteinaceous catalysts called enzymes, which are partnered with cofactors and energetic molecules that in combination drive life as we know it. Evolved over millennia, biological systems offer advantages over many conventional chemistries, including stereoselectivity in product formation, activity under mild biological conditions, environmentally friendly byproducts, and others. With advances in our understanding of molecular engineering of organisms and improving biochemical processes through enzyme selection and reaction optimization, the biological synthesis of everything from commodity to fine chemicals is on the horizon, either alone or in concert with organic synthesis. In this Special Issue, we will examine scientific advances in biomanufacturing focusing on traditional cellular-based systems of production, the rise in cell-free systems that rely on transcription/translation machinery in vitro, and synthetic biochemistry systems that utilize purified enzymes for biosynthesis.

Dr. Scott A. Walper
Dr. Gregory A. Ellis
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Catalysts is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2000 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • enzyme
  • biomanufacturing
  • bioprocessing
  • synthetic biology
  • metabolic engineering

Published Papers (1 paper)

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Research

Open AccessArticle
In Vivo, High-Throughput Selection of Thermostable Cyclohexanone Monooxygenase (CHMO)
Catalysts 2020, 10(8), 935; https://doi.org/10.3390/catal10080935 - 13 Aug 2020
Abstract
Cyclohexanone monooxygenase (CHMO) from Acinetobacter sp. NCIMB 9871 is characterized as having wide substrate versatility for the biooxidation of (cyclic) ketones into esters and lactones with high stereospecificity. Despite industrial potential, CHMO usage is restricted by poor thermostability. Limited high-throughput screening tools and [...] Read more.
Cyclohexanone monooxygenase (CHMO) from Acinetobacter sp. NCIMB 9871 is characterized as having wide substrate versatility for the biooxidation of (cyclic) ketones into esters and lactones with high stereospecificity. Despite industrial potential, CHMO usage is restricted by poor thermostability. Limited high-throughput screening tools and challenges in rationally engineering thermostability have impeded CHMO engineering efforts. We demonstrate the application of an aerobic, high-throughput growth selection platform in Escherichia coli (strain MX203) for the discovery of thermostability enhancing mutations for CHMO. The selection employs growth for the easy readout of CHMO activity in vivo, by requiring nicotinamide adenine dinucleotide phosphate (NADPH)-consuming enzymes to restore cellular redox balance. In the presence of the native substrate cyclohexanone, variant CHMO GV (A245G-A288V) was discovered from a random mutagenesis library screened at 42 °C. This variant retained native activity, exhibited ~4.4-fold improvement in residual activity after 30 °C incubation, and demonstrated ~5-fold higher cyclohexanone conversion at 37 °C compared to the wild type. Molecular modeling indicates that CHMO GV experiences more favorable residue packing and supports additional backbone hydrogen bonding. Further rational design resulted in CHMO A245G-A288V-T415C with improved thermostability at 45 °C. Our platform for oxygenase evolution enabled the rapid engineering of protein stability critical for industrial scalability. Full article
(This article belongs to the Special Issue Bioprocess Engineering and Enzyme Application)
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