Special Issue "Gas Phase Reactions"
A special issue of Molecules (ISSN 1420-3049).
Deadline for manuscript submissions: closed (30 June 2013)
Prof. Dr. Dietmar A. Plattner
Institute for Organic Chemistry and Biochemistry, Albert-Ludwigs-University of Freiburg, Albertstrasse 21, D-79104 Freiburg, Germany
Interests: reactions in the gas phase; Mass spectrometry; reactions under non-standard conditions; enzyme catalysis
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. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as 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 refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed Open Access monthly journal published by MDPI.
Molecules 2013, 18(7), 8358-8375; doi:10.3390/molecules18078358
Received: 29 May 2013; in revised form: 26 June 2013 / Accepted: 11 July 2013 / Published: 16 July 2013| Download PDF Full-text (315 KB)
Molecules 2013, 18(8), 9901-9918; doi:10.3390/molecules18089901
Received: 15 July 2013; in revised form: 8 August 2013 / Accepted: 13 August 2013 / Published: 16 August 2013| Download PDF Full-text (1926 KB)
Article: Pressure Dependent Product Formation in the Photochemically Initiated Allyl + Allyl Reaction
Molecules 2013, 18(11), 13608-13622; doi:10.3390/molecules181113608
Received: 27 August 2013; in revised form: 17 October 2013 / Accepted: 22 October 2013 / Published: 4 November 2013| Download PDF Full-text (410 KB)
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Type of Paper: Review
Title: “Solid/gas Biocatalysis, an Efficient Tool for Fundamental Studies on Enzyme Activity and Selectivity”
Authors: M. Graber, A. Mensi, N. Fniter, B. Belkhiria and Z. Marton
Affiliations: UMR 7266 CNRS-ULR, LIENSS, LIttoral ENvironnement SociétéS, Université de La Rochelle, Pôle Sciences et Technologie, Bâtiment Marie Curie, Avenue Michel Crépeau, 17042 La Rochelle, France
Abstract: From the middle of the 1980s, it was demonstrated that solid–gas biocatalysis was possible with enzymes usually acting on liquid substrates, with several examples of enzyme in the dry state acting on gaseous substrates. Different isolated enzymes were tested successfully such as the horse liver dehydrogenase, the Sulfolobus solfataricus dehydrogenase, the Pischia pastoris alcohol oxidase, the baker’s yeast alcohol dehydrogenase and lipolytic enzymes. This opened a new research area that led to the definition of new continuous cleaner processes for single or multi steps biotransformations, involving either enzymatic solid–gas bioreactors or microbial set-ups.
Since solid–gas bioreactors allow control and independent variation of the thermodynamic activity of substrates and other added components, they offer the possibility to modulate and to study the effect of each component present in the microenvironment of the biocatalyst. Therefore these solid–gas systems constitute an efficient tool to understand and rationalize the effects of the microenvironment of an enzyme on its activity, selectivity and stability.
In this review, some examples of the benefits of this thermodynamic approach and control of enzymatic reactions are discussed, and an overview of some applications of solid–gas technology to fundamental studies related to the influence of the microenvironment on enzymes are given.
Last update: 1 February 2013