Journal Menu► ▼ Journal Menu
Journal Browser► ▼ Journal Browser
Special Issue "Advances in the Design and Characterization of Heterogeneous Biocatalysts"
Deadline for manuscript submissions: 15 February 2020.
Dr. Alexander Dennig Website 1 Website 2 E-Mail
Graz University of Technology, Institute of Biotechnology and Biochemical Engineering, Petersgasse 12/I and Austrian Centre of Industrial Biotechnology (acib), Petersgasse 14, 8010 Graz, Austria
Interests: enzymology; biocascades; reaction and protein engineering; green chemistry
Dr. Javier Rocha-Martin Website 1 Website 2 Website 3 E-Mail
Institute of Catalysis and Petrochemistry, Spanish Council for Scientific Research (CSIC), Marie Curie 2, 28049 Madrid, Spain
Interests: protein immobilization; protein engineering; enzyme stabilization; multienzyme systems; cascade reactions
Heterogeneous biocatalysts are of great relevance in the development of modern (bio)chemical manufacturing processes. Enzyme immobilization has a long-standing tradition, with many successful examples found at both academic and industrial level. The body of knowledge is well-established and there is a broad repertoire of methodologies for immobilization, involving different chemistries and carrier materials. Fueled by the constant discovery of new enzymes/reactivities, new challenges need to be formulated for heterogeneous biocatalysts. The preparation of heterogeneous biocatalysts is not yet ready to solve emerging challenges, such as multimeric complex enzymes, the stabilization for application in nonconventional reaction media, multienzyme reaction systems, nor can it help with integrating catalysts into new reactor configurations. There is a pressing need to develop innovative concepts for the reuse of cofactors and the level of depiction for heterogeneous biocatalysts by structural features or spatiotemporal resolution of local concentration of reactants and products. To this end, a merged strategic research field can be formulated that would possibly be best described by the term “heterogeneous biocatalyst engineering”.
This Special Issue aims at hosting original contributions dealing with advances in the design, application, and characterization of immobilized biocatalysts. The main topics are:
- Immobilized new enzymes and biocascades of high synthetic relevance;
- New techniques of immobilization dealing with enzyme activity or stability;
- New materials for enzyme immobilization;
- Immobilized enzymes in new reactor concepts: e.g. flow microreactors, intensifying reactions and reactors...
- Advances in the characterization of immobilized enzymes.
Dr. Juan M. Bolivar
Dr. Alexander Dennig
Dr. Javier Rocha-Martin
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 1600 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.
- enzyme immobilization
- enzyme stabilization
- advanced/biohybrid materials
- green chemistry
- heterogeneous catalysts
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.
1. Title: Substrate Identification Method for Protein Phosphatases Using Phosphorylation Mimic Phage Display
Authors: Takuya Yoshida, Kazuki Yamazaki, Takashi Yoneda, Atsushi Kaneko, and Yoshiro Chuman
Affiliation: Laboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Niigata University, Niigata, 950-2181, Japan
Abstract: Protein phosphorylation is the most widespread type of post-translational modification and disordered regulation of protein phosphorylation often causes serious diseases. Protein phosphatases are divided into two major groups: tyrosine (Tyr) phosphatases and serine/threonine (Ser/Thr) phosphatases. Substrate trapping mutants are frequently used to characterize Tyr phosphatases and identify their substrates; however, a rapid and simple method to identify substrates for Ser/Thr phosphatases has yet to be developed. The TFIIF-associating component of RNA polymerase II C-terminal domain (CTD) phosphatase/small CTD phosphatase (FCP/SCP) phosphatase family is one of the three Ser/Thr protein phosphatase families. Defects or control failures of these phosphatases is correlated with various diseases such as cancer and neuropathy; however, the pathogenic mechanism is not well understood. Recently we have reported that the development of a novel methodology, termed Phosphorylation Mimic Phage Display (PMPD), to identify the substrates for FCP/SCP type Ser/Thr phosphatase Scp1 using peptide phage display libraries with AlF4− . Here we report that PMPD method using BeF3- instead of AlF4− to identify the novel substrate peptides against Scp1. After screening peptide phages bound to Scp1, we identified the several clones bound to Scp1 in a BeF3--dependent manner. Synthetic phospho-peptide BeM12-1 with the highest frequency showed the direct binding to the Scp1, although the binding was inhibited with the addition of BeF3- , indicating that the peptide binds to the active center of catalytic site in Scp1. Interestingly kinetics analysis revealed that BeM12-1 did not work as a substrate but a competitive inhibitor for Scp1. These data suggested that PMPD method may be applicable for the identification of both of novel substrates and inhibitors for FCP/SCP phosphatases family (Fig. 1).
Fig. 1. Model of Phosphorylation Mimic Phage Display (PMPD) method.
 K. Otsubo, T. Yoneda, A. Kaneko, S. Yagi, K. Furukawa, and Y. Chuman, Protein Pept. Lett., 2018, 25(1), 76-83.
2. Title: MODELLING OF KINETICS AND MASS TRANSFER IN LENTIL-SHAPED IMMOBILIZED BIOCATALYST PARTICLES
Authors: Milan Polakovič, Mário Miháľ, Jozef Markoš
Polyvinyl alcohol (PVA) gels belong to typical carriers for the immobilization of whole cells by entrapment. A PVA gel with a good chemical and mechanical stability, enabling high cell concentrations and good transport properties was developed by Vorlop et al. (1998a,b). A part of this invention was a manufacturing procedure of lentil-shaped gel particles named LentiKats. The same name has a Czech company who own the technology of production of these immobilized biocatalyst particles (Stloukal et al., 2007). Dozens of papers and several patents were published on different applications of LentiKats particles which typical dimensions are: the width of 3-4 mm and thickness of 0.2-0.4 mm.
None of these papers treated rigorously the effect of mass transfer resistance on the kinetics of a biocatalytic process in spite of that LentiKats have been promoted as particles diminishing the problem of mass transfer resistance. We have recently estimated the effective diffusion coefficient of sucrose from inverse size exclusion experiments when the slab geometry was intuitively considered to represent the shape of LentiKats particles (Schenkmeyerová et al., 2014)...
3. Title: Deciphering the kinetics of immobilized oxidoreductases through single-particle studies
Author: Fernando Lopez-Gallego