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Special Issue "Biomolecular Catalysts"

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: 30 November 2018

Special Issue Editor

Guest Editor
Prof. Dr. Jose M. Palomo

Group of Chemical Biology and Biocatalysis, Departament of Biocatalysis, Institute of Catalysis (ICP-CSIC), Marie Curie 2, Cantoblanco, Campus UAM, 28049 Madrid, Spain
Website | E-Mail
Interests: protein chemistry; nanocatalysis; biotransformations; carbohydrate chemistry; chemical biology

Special Issue Information

Dear Colleagues,

Chemists have long been inspired by the exquisite selectivity and efficiency of biomolecular catalysts. The development of new catalysts with improved properties, new activities and selectivities making processes economically and environmentally sustainable are mandatory in our future. The application of biomolecules, such as polymers, peptides or proteins to create interesting networks for metal complexes to create nanostructurated artificial catalysts are extremely important in the development of chemical process such as synthetic molecules, sustainable fuels, medical biosensors, etc. Additionally, the engineering, design and creation of nanoreactors using biomolecules are of special interest to improving properties of extremely sensitive enzymes.

This Special Issue will be focused on innovative and novel research in the creation and application of biomolecular catalysts.

Prof. Jose M. Palomo
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. Molecules 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 1800 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

  • enzymes
  • cells
  • microorganisms
  • virus
  • metalloenzymes
  • artificial enzymes
  • peptides
  • polymers
  • biohybrids
  • bionanomaterials
  • directed evolution
  • computational chemistry
  • bioorganic chemistry
  • chemical biology
  • heterogeneous catalysis
  • homogeneous catalysis
  • biocatalysis
  • nanocatalysis

Published Papers (2 papers)

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Research

Open AccessArticle Ultra-Small Pd(0) Nanoparticles into a Designed Semisynthetic Lipase: An Efficient and Recyclable Heterogeneous Biohybrid Catalyst for the Heck Reaction under Mild Conditions
Molecules 2018, 23(9), 2358; https://doi.org/10.3390/molecules23092358
Received: 27 July 2018 / Revised: 13 September 2018 / Accepted: 13 September 2018 / Published: 14 September 2018
PDF Full-text (3731 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
A novel heterogeneous enzyme-palladium (Pd) (0) nanoparticles (PdNPs) bionanohybrid has been synthesized by an efficient, green, and straightforward methodology. A designed Geobacillus thermocatenulatus lipase (GTL) variant genetically and then chemically modified by the introduction of a tailor-made cysteine-containing complementary peptide- was used as
[...] Read more.
A novel heterogeneous enzyme-palladium (Pd) (0) nanoparticles (PdNPs) bionanohybrid has been synthesized by an efficient, green, and straightforward methodology. A designed Geobacillus thermocatenulatus lipase (GTL) variant genetically and then chemically modified by the introduction of a tailor-made cysteine-containing complementary peptide- was used as the stabilizing and reducing agent for the in situ formation of ultra-small PdNPs nanoparticles embedded on the protein structure. This bionanohybrid was an excellent catalyst in the synthesis of trans-ethyl cinnamate by Heck reaction at 65 °C. It showed the best catalytic performance in dimethylformamide (DMF) containing 10–25% of water as a solvent but was also able to catalyze the reaction in pure DMF or with a higher amount of water as co-solvent. The recyclability and stability were excellent, maintaining more than 90% of catalytic activity after five cycles of use. Full article
(This article belongs to the Special Issue Biomolecular Catalysts)
Figures

Figure 1

Open AccessArticle New Triterpenoid from Novel Triterpenoid 15-O-Glycosylation on Ganoderic Acid A by Intestinal Bacteria of Zebrafish
Molecules 2018, 23(9), 2345; https://doi.org/10.3390/molecules23092345
Received: 30 August 2018 / Revised: 12 September 2018 / Accepted: 12 September 2018 / Published: 13 September 2018
PDF Full-text (1976 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Functional bacteria that could biotransform triterpenoids may exist in the diverse microflora of fish intestines. Ganoderic acid A (GAA) is a major triterpenoid from the medicinal fungus Ganoderma lucidum. In studying the microbial biotransformation of GAA, dozens of intestinal bacteria were isolated
[...] Read more.
Functional bacteria that could biotransform triterpenoids may exist in the diverse microflora of fish intestines. Ganoderic acid A (GAA) is a major triterpenoid from the medicinal fungus Ganoderma lucidum. In studying the microbial biotransformation of GAA, dozens of intestinal bacteria were isolated from the excreta of zebrafish. The bacteria’s ability to catalyze GAA were determined using ultra-performance liquid chromatography analysis. One positive strain, GA A07, was selected for functional studies. GA A07 was confirmed as Bacillus sp., based on the DNA sequences of the 16S rRNA gene. The biotransformed metabolite was purified with the preparative high-performance liquid chromatography method and identified as GAA-15-O-β-glucoside, based on the mass and nuclear magnetic resonance spectral data. The present study is the first to report the glycosylation of Ganoderma triterpenoids. Moreover, 15-O-glycosylation is a new microbial biotransformation of triterpenoids, and the biotransformed metabolite, GAA-15-O-β-glucoside, is a new compound. Full article
(This article belongs to the Special Issue Biomolecular Catalysts)
Figures

Figure 1

Planned Papers

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.

Title: A New Strategy for Enzyme Stabilization Based on The Coating of Different Immobilized-Stabilized Enzyme Derivatives with Additives Linked on Hydrophilic Polymers
Author: Valeria miranda, Claudia Bernal, Caio C. Aragon, Jose M. Guisan, Cesar Mateo 

Title: Efficient Production of (R)-Monomethyl-phenylglutarate Catalyzed by Novozym 435: Use of a Stirred Tank Reactor Operated in Form Sequential

Author: Yerko Fredes, Lesly Chamorro, Zaida Cabrera 

Title: A New Application of Biochar: Supports for Lipase Immobilization

Author: Lays C. de Almeida, Felipe A. de Jesus, Flávia M. S. Santos, Anderson dos S. Barbosa, Alini T. Fricks, Lisiane dos S. Freitas, Álvaro S. Lima and Cleide M. F. Soares

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