Special Issue "Biocatalysts: Design and Application"

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Metal Catalysis".

Deadline for manuscript submissions: 31 January 2019

Special Issue Editors

Guest Editor
Prof. Dr. Cesar Mateo

Group of Chemical Processes Catalyzed by enzymes, Departament of Biocatalysis, Institute of Catalysis (ICP-CSIC), Marie Curie 2, Cantoblanco, Campus UAM, 28049 Madrid, Spain
Website | E-Mail
Interests: enzyme processes; biocatalysis; CO2 transformation; red-ox processes; enzyme immobilization
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,

The use of biocatalysts in chemical reactions are of great interest because they are carried out under very mild and environmentally green conditions. The preparation of robust and efficient biocatalysts is a key issue for their possible implementation into large-scale processes.

This special issue is focused on different papers dealing with the development of new strategies to improve different biocatalysts, their application in processes of industrial interest as well as new kind of applications of these catalysts in different fields.

Prof. Dr. Cesar Mateo
Prof. Dr. Jose M. Palomo
Guest Editors

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 1300 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

  • protein chemistry
  • molecular biology
  • immobilization
  • biocatalysis
  • biotransformations
  • carbohydrate chemistry
  • cascade reaction
  • nanocatalysis

Published Papers (2 papers)

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Research

Open AccessArticle Study of Extraction and Enzymatic Properties of Cell-Envelope Proteinases from a Novel Wild Lactobacillus plantarum LP69
Catalysts 2018, 8(8), 325; https://doi.org/10.3390/catal8080325
Received: 17 July 2018 / Revised: 5 August 2018 / Accepted: 7 August 2018 / Published: 8 August 2018
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Abstract
Lactobacilli cell-envelope proteinases (CEPs) have been widely used in the development of new streams of blockbuster nutraceuticals because of numerous biopharmaceutical potentials; thus, the development of viable methods for CEP extraction and the improvement of extraction efficiency will promote their full-scale application. In
[...] Read more.
Lactobacilli cell-envelope proteinases (CEPs) have been widely used in the development of new streams of blockbuster nutraceuticals because of numerous biopharmaceutical potentials; thus, the development of viable methods for CEP extraction and the improvement of extraction efficiency will promote their full-scale application. In this study, CEP from a novel wild Lactobacillus plantarum LP69 was released from cells by incubating in calcium-free buffer. The extraction conditions of CEP were optimized by response surface methodology with the enzyme activity and specific activity as the detective marker. The optimal extraction conditions were: time of 80 min, temperature of 39 °C and buffer pH of 6.5. Under these conditions, enzyme activity and specific activity were (23.94 ± 0.86) U/mL and (1.37 ± 0.03) U/mg, respectively, which were well matched with the predicted values (22.12 U/mL and 1.36 U/mg). Optimal activity of the crude CEP occurred at pH 8.0 and 40 °C. It is a metallopeptidase, activated by Ca2+, inhibited by Zn2+ and ethylene-diamine-tetra-acetic acid, and a serine proteinase which is inhibited by phenylmethylsulfonyl fluoride. Kinetic studies showed that CEP from LP69 could hydrolyze whey protein, lactoglobulin and casein. Our study improves the extraction efficiency of CEPs from LP69, providing the reference for their industrial development. Full article
(This article belongs to the Special Issue Biocatalysts: Design and Application)
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Open AccessArticle Electrochemical Biosensor for the Determination of Amlodipine Besylate Based on Gelatin–Polyaniline Iron Oxide Biocomposite Film
Catalysts 2018, 8(6), 233; https://doi.org/10.3390/catal8060233
Received: 19 April 2018 / Revised: 10 May 2018 / Accepted: 18 May 2018 / Published: 4 June 2018
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Abstract
In the present study, a new biosensor based on lipase from Candida rugosa (CRL) was developed for amlodipine besylate drug (AMD) with biodegradable material using a mixture of polyaniline iron oxide and gelatin. Polyaniline/Fe2O3 (PANI@Fe2O3) was
[...] Read more.
In the present study, a new biosensor based on lipase from Candida rugosa (CRL) was developed for amlodipine besylate drug (AMD) with biodegradable material using a mixture of polyaniline iron oxide and gelatin. Polyaniline/Fe2O3 (PANI@Fe2O3) was prepared by a chemical polymerization method in a medium of ammonium persulfate as an oxidant and characterized by employing Scanning Electron Microscopy (SEM), Fourier Transform Infrared (FTIR), and Ultra-violet (UV) spectroscopy. The purified enzyme was entrapped in the biocomposite matrix film with the aid of a glutaraldehyde cross-linking reagent to establish the immobilization of the lipase. The principle of the biosensor is based on the electrochemical properties of amlodipine besylate (AMD), which were studied for the first time using the cyclic voltammetric method. The cathodic behavior of AMD was measured on the irreversible reduction signal at −0.185 V versus Ag/AgCl at pH 7.4 and 30 °C in a phosphate alkaline buffer. Full article
(This article belongs to the Special Issue Biocatalysts: Design and Application)
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