Special Issue "Biocatalysis"
QuicklinksA special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry, Molecular Biology and Biophysics".
Deadline for manuscript submissions: closed (31 December 2009)
Special Issue Editors
Guest Editor
Prof. Dr. Martin Hartmann
Erlangen Catalysis Resource Center, Universität Erlangen-Nürnberg, Egerlandstr. 3, 91058 Erlangen, Germany
E-Mail:
Editorial Advisor
Prof. Dr. Uwe T. Bornscheuer
Institute of Biochemistry, Deptartment of Biotechnology & Enzyme Catalysis, Greifswald University, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany
Website: http://www.chemie.uni-greifswald.de/~biotech/
E-Mail:
Interests: biocatalysis; protein engineering; high-throughput screening; enantioselective synthesis
Published Papers
Special Issue Information
Biocatalysis encompasses the use of enzymes or whole cell systems for the conversion of readily available, inexpensive starting materials to high value products. Enzymes frequently display extraordinary chemo-, enantio- or regioselectivity, making them attractive catalysts for a wide range of chemical transformations. Enzymes typically operate under mild conditions of pH and temperature and often are compatible to each other. As a result of these advantages, enzymes and whole cells are increasingly applied in areas ranging from the production of intermediates for pharmaceuticals, fine chemicals, agrichemicals, biofuels and performance chemicals. In the light of the increasing importance of biocatalysis, the International Journal of Molecular Science will publish a special issuecovering both fundamental aspects of biocatalysis and advances in industrial applications. Reviews and original papers are welcome and will be considered for publication. Possible Topics include (but are not limited to) directed molecular evolution of enzymes, enzyme discovery and high-throughput screening, enzyme optimization, stabilization and immobilization, new types of reaction transformations, industrial application of enzymes including utilization of biomass, process development and reaction engineering.
Prof. Dr. Martin Hartmann
Guest Editor
Submission
All papers should be submitted to ijms@mdpi.org. To be published continuously until the deadline and papers will be listed together at the special issue website.
Submitted papers should not have been published previously, nor be under consideration for publication elsewhere. All papers are refereed through a peer-review process. A guide for authors is available on the Instructions for Authors page. The International Journal of Molecular Sciences is an international peer-reviewed monthly journal published by Molecular Diversity Preservation International.
Open Access publication fees are 800 CHF per paper. English correction fees and/or formatting fees (250 CHF) will be added in certain cases (1050 CHF per paper for those papers that require extensive additional formatting and/or English corrections).
Keywords
- protein engineering
- enzyme immobiliation
- enantioselective catalysis
- non-conventional media
- bioprocess engineering
Planned Papers
Feature Papers
Type of Paper: Article
Title: Engineering Cofaktor Preference of Ketone Reducing Biocatalysts: A Mutagenesis Study on a γ-Diketone Reductase from the Yeast Saccharomyces cerevisiae Serving as an Example
Authors: M. Katzberg 1, N. Skorupa-Parachin 2, M. F. Gorwa-Grauslund 2, B. Hahn-Hägerdahl 2 and M. Bertau 1,*
Affiliations: 1 Department of Technical Chemistry, University of Mining and Technology Freiberg, Germany
2 Department of Applied Microbiology, Lund University, Lund, Sweden
* Author to whom correspondence should be addressed; E-Mail: martin.bertau@chemie.tu-freiberg.de
Abstract: The synthesis of pharmaceuticals, catalyst, flavours and agrochemicals more and more relies on enantiopure chiral building blocks. These can be produced environmentally friendly and efficiently via bioreduction of prochiral ketones catalysed by dehydrogenases. A productive source of these biocatalysts accepting a broad range of substrates is the yeast Saccharomyces cerevisiae, whose genome also encodes a reductase catalysing sequential reduction of the γ-diketone 2,5-hexanedione furnishing the diol (2S,5S)-hexanediol and the γ-hydroxyketone (5S)-hydroxy-2-hexanone with high enantio- and diastereoselectivity (ee and de >99.5 %). However this dehydrogenase like most of the biocatalysis relevant dehydrogenases in this yeast prefer NADPH as the hydrogen donating cofaktor. However NADH is more stable and cheaper than NADPH and thus it would be more effective to use NADH in cell-free reduction systems. To achieve this, the cofactor binding site of the dehydrogenase was altered by site-directed mutagenesis. The results show that the rational approach based on a homology model of the enzyme allowed us to generate a mutant enzyme, which exhibits a relaxed cofactor preference and thus is able to use both NADPH and NADH. Results obtained from other mutants are discussed and point towards the limits of rationally designed mutants.
Regular Papers
Type of Paper: Article
Title: Fructose Production by Inulinase Covalently Immobilized on Sepabeads in Batch and Fluidized Bed Reactor
Authors: Emanuele Ricca and Stefano Curcio
Affiliations: Department of Engineering Modeling, University of Calabria, I-87036 Arcavacata di Rende (CS), Italy; E-mail: stefano.curcio@unical.it
Abstract: The present work is an experimental study of the performance of a recently designed immobilized enzyme: inulinase from Aspergillus sp. covalently immobilized on Sepabeads. The aim of the work is to test the new biocatalyst in conditions of industrial interest and to assess the feasibility of the process in a fluidized bed reactor (FBR). The catalyst was first tested in a batch reactor in various sets of conditions as compared to a certain set of conditions assumed as a standard. Once the response of the catalyst to different operating conditions was tested and the operational stability assessed, one of the sets of conditions tested in batch was chosen for tests in FBR. Prior to reaction tests, preliminary fluidization tests were realized in order to define an operating range of admissible flow rates. As a result, the FBR was run at different feed flow rates in a closed cycle configuration and its performance was compared to that of the batch system. The FBR proved to be performing and suitable for scale up to large fructose production.
Keywords: enzyme reaction; inulin hydrolysis; fluidized bed reactor; fructose
Last update: 2 March 2010
loading...