Special Issue "Biocatalysis and Fermentation—Enzyme Production and Whole Cell Biocatalysis"

A special issue of Fermentation (ISSN 2311-5637).

Deadline for manuscript submissions: closed (30 November 2019).

Special Issue Editor

Prof. Dr. David J. Timson
E-Mail Website1 Website2 Website3
Guest Editor
School of Pharmacy and Biomolecular Sciences, University of Brighton, Brighton, UK
Interests: enzyme engineering; yeast as models for human diseases; yeast growth under adverse conditions

Special Issue Information

Dear Colleagues,

Biocatalysis offers significant opportunities. Enzymes catalyse a vast range of chemical reactions, often with exquisite regio- and stereo-selectivity. They often do so at faster rates than traditional chemical catalysts and at lower temperatures and pressures. Enzymes typically operate in aqueous solution and are naturally biodegradable. Their potential for exploitation in “green chemistry” is substantial. The production of enzymes for biocatalysis typically requires the expression of the protein in a recombinant host, often bacteria or yeasts. Optimisation of fermentation conditions can result in significant advantages through the improvement of yield, quality and purity of the enzyme. Site-directed mutagenesis methods can be applied to engineer enzymes for altered specificity or improved stability. Alternatively, whole cells can be used as reaction vessels to synthesise particular chemicals. Often this requires engineering of the metabolic pathways present in the cells to redirect biosynthesis towards the desired product. Again, optimisation of the growth conditions is likely to be necessary to maximise yield. This Special Issue focuses on the use of microbial cells for the production of biocatalysts and in whole cell biocatalysis. Papers describing the optimisation of the production of enzymes and the operation of whole cell biocatalysis are encouraged as are papers describing theoretical approaches which can be applied to yield improvement.

Prof. David J. Timson
Guest Editor

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. Fermentation is an international peer-reviewed open access quarterly 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 1000 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

  • biocatalysis
  • recombinant enzyme
  • whole cell biocatalysis
  • protein overexpression
  • enzyme engineering
  • metabolic pathway engineering
  • green chemistry
  • bioreactors
  • enzyme biotechnology
  • yield improvement

Published Papers (2 papers)

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Research

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Open AccessArticle
Basidiomycotic Yeast Cryptococcus diffluens Converts l-Galactonic Acid to the Compound on the Similar Metabolic Pathway in Ascomycetes
Fermentation 2019, 5(3), 73; https://doi.org/10.3390/fermentation5030073 - 05 Aug 2019
Abstract
(1) Background: It has been shown that d-galacturonic acid is converted to l-galactonic acid by the basidiomycotic yeast, Cryptococcus diffluens. However, two pathways are hypothesized for the l-galactonic acid conversion process in C. diffluens. One is similar to [...] Read more.
(1) Background: It has been shown that d-galacturonic acid is converted to l-galactonic acid by the basidiomycotic yeast, Cryptococcus diffluens. However, two pathways are hypothesized for the l-galactonic acid conversion process in C. diffluens. One is similar to the conversion process of the filamentous fungi in d-galacturonic acid metabolism and another is the conversion process to l-ascorbic acid, reported in the related yeast, C. laurentii. It is necessary to determine which, if either, process occurs in C. diffluens in order to produce novel value-added products from d-galacturonic acid using yeast strains. (2) Methods: The diethylaminoethy (DEAE)-fractionated enzyme was prepared from the cell-free extract of C. diffluens by the DEAE column chromatography. The l-galactonic acid conversion activity was assayed using DEAE-fractionated enzyme and the converted product was detected and fractionated by high-performance anion-exchange chromatography. Then, the molecular structure was identified by nuclear magnetic resonance analysis. (3) Results: The product showed similar chemical properties to 2-keto-3-deoxy-l-galactonic acid (l-threo-3-deoxy-hexulosonic acid). (4) Conclusions: It is suggested that l-galactonic acid is converted to 2-keto-3-deoxy-l-galactonic acid by dehydratase in C. diffluens. The l-galactonic acid conversion process of C. diffluens is a prioritized pathway, similar to the pathway of ascomycetes. Full article
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Review

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Open AccessReview
Four Challenges for Better Biocatalysts
Fermentation 2019, 5(2), 39; https://doi.org/10.3390/fermentation5020039 - 09 May 2019
Abstract
Biocatalysis (the use of biological molecules or materials to catalyse chemical reactions) has considerable potential. The use of biological molecules as catalysts enables new and more specific syntheses. It also meets many of the core principles of “green chemistry”. While there have been [...] Read more.
Biocatalysis (the use of biological molecules or materials to catalyse chemical reactions) has considerable potential. The use of biological molecules as catalysts enables new and more specific syntheses. It also meets many of the core principles of “green chemistry”. While there have been some considerable successes in biocatalysis, the full potential has yet to be realised. This results, partly, from some key challenges in understanding the fundamental biochemistry of enzymes. This review summarises four of these challenges: the need to understand protein folding, the need for a qualitative understanding of the hydrophobic effect, the need to understand and quantify the effects of organic solvents on biomolecules and the need for a deep understanding of enzymatic catalysis. If these challenges were addressed, then the number of successful biocatalysis projects is likely to increase. It would enable accurate prediction of protein structures, and the effects of changes in sequence or solution conditions on these structures. We would be better able to predict how substrates bind and are transformed into products, again leading to better enzyme engineering. Most significantly, it may enable the de novo design of enzymes to catalyse specific reactions. Full article
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