Special Issue "Enzyme Immobilization"
A special issue of Molecules (ISSN 1420-3049).
Deadline for manuscript submissions: 15 May 2014
Prof. Dr. Roberto Fernandez-Lafuente
Institute of catalysis and petrochemsitry-CSIC, Campus UAM-CSIC Cantoblanco, 28049 Madrid, Spain
Phone: + 34 91 585 4941
Fax: +34 91 585 4760
Interests: enzyme immobilization; stabilization and purification; biocatalyst and biosensors design; bioprocesses optimization
The immobilization of enzymes and proteins is a seemingly ancient research area that still attracts great interest. The initial interest in enzyme immobilization was motivated by a desire to simplify the reuse of these expensive biocatalysts. However, at present, immobilization has developed into a very powerful tool that has been used to overcome many enzyme limitations. Applications include improving enzyme stability, activity, selectivity or specificity, reducing inhibition problems, and even coupling immobilization and purification, etc.
To date, many immobilization protocols have been reported. However, research is still the cornerstone of obtaining full control of the orientation of the enzyme on the support surface, and of the intensity of the support-enzyme interactions. Moreover, immobilization should not be considered an alternative to any other enzyme improvement strategy. For example, genetic and chemical tools may be utilized to produce a better enzyme that maintain improved properties after immobilization, or to improve immobilization; in both situations, alternative techniques produce an improved biocatalyst.
Thus, the efforts to design strategies involving the coupled use of immobilization with microbiological (e.g., the use of thermophilic enzymes), chemical or genetic modifications are of special interest. Enzymes are co-immobilized to catalyze cascade reactions; however, this process may produce additional complications. This special issue invites submissions (i.e., research or review papers) discussing the design of new immobilization protocols, especially when the control of the enzyme orientation is intended by design of the support, or modification of the enzyme. Papers related to the modification of immobilized enzymes, or to the modification of the support surface after enzyme immobilization, are also welcome.
Dr. Roberto Fernandez-Lafuente
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.
- controlled enzyme immobilization and co-immobilization
- heterofunctional supports
- improved enzyme properties via immobilization
- chemical or genetic modification and immobilization
- immobilization of enzymes from thermophilic microorganisms
Article: Surface-Functionalized Hyperbranched Poly(Amido Acid) Magnetic Nanocarriers for Covalent Immobilization of a Bacterial γ-Glutamyltranspeptidase
Molecules 2014, 19(4), 4997-5012; doi:10.3390/molecules19044997
Received: 11 March 2014; in revised form: 15 April 2014 / Accepted: 17 April 2014 / Published: 22 April 2014| Download PDF Full-text (2201 KB) | Supplementary Files
Article: Laccase Immobilized on a PAN/Adsorbents Composite Nanofibrous Membrane for Catechol Treatment by a Biocatalysis/Adsorption Process
Molecules 2014, 19(3), 3376-3388; doi:10.3390/molecules19033376
Received: 20 January 2014; in revised form: 6 March 2014 / Accepted: 6 March 2014 / Published: 19 March 2014| Download PDF Full-text (1930 KB) | Download XML Full-text
Last update: 23 October 2013