Biocatalysis

ISSN: 2353-1746

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Biocatalysis is closed for submissions since 2020.

Biocatalysis is a high quality journal designed to have impact on the scientific, academic and industrial sectors. Researchers, working in the field of biochemical catalysis for environmental, health and energy applications can share here results of their work. New approaches such as genomics, proteomics and molecular engineering are welcome as well. The journal includes frontier research tools such as computational chemistry and bionanotechnology. Biocatalysis aims to be the main option to publish relevant scientific and technological findings in all subjects on biochemical transformations.

This journal is international with a fast, rigorous and comprehensive peer-review. It is a strong commitment of the Editor and the prominent Advisory Board to attract the authors by the growing reputation of this new journal.

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Volume 4 Issue 1

January 2018

Open Access February 2, 2018

Novel DyP from the basidiomycete Pleurotus sapidus: substrate screening and kinetics

Alexandru Avram, Arijit Sengupta, Peter H. Pfromm, Holger Zorn, Patrick Lorenz, Tatjana Schwarz, Khanh Quoc Nguyen, Peter Czermak

Page range: 1-13

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Abstract

A novel Dye-decolorizing peroxidase from the basidiomycete Pleurotus sapidus was screened for dyedecolorizing peroxidase activity with 2,2‘-azino-bis(3- ethylbenzothiazoline-6-sulfonic acid), Remazol Brilliant Blue R and Guaiacol. Additionally, the catalytic efficiency on degrading β-carotene into volatile products, and the catalyst storage stability with three different additives were also studied. The apparent inhibition constant (KS) was 51.7 μM. Optimal reaction rates (Vmax) and affinity constants (Km) towards the reducing substrates were obtained using Michaelis-Menten kinetic theory. The trend in the calculated Km’s was found to be 7.0 mM > 0.524 mM > 0.051 mM for Guaiacol, 2,2‘-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and Remazol Brilliant Blue R. The storage stability of the catalyst was evaluated with 7.0% w/v PEG400, 7.0% w/v PEG1450 and 0.1% w/v Tween®80 at 5°C over a period of 45 days. The study revealed the longest activity conservation with PEG1450, where rDyP had lost 30% of initial activity. The enzyme solution presented similar pH and temperature dependence to known fungal dye-decolorizing peroxidases with most prolific enzymatic activities registered at pH 4.0 and temperatures below 30°C. An interesting property of the catalyst was oxidation observed in the absence of hydrogen peroxide.

Open Access May 17, 2018

Optimization of enzymatic synthesis of ethyl hexanoate in a solvent free system using response surface methodology (RSM)

Sarita D. Gawas, Nidya Lokanath, Virendra K. Rathod

Page range: 14-26

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Abstract

The present paper demonstrates application of biocatalysis to the synthesis of ethyl hexanoate, i.e. pineapple flavour ester, in a solvent free system. In order to evaluate the effect of various process parameters on reaction conversion, response surface methodology (RSM) complemented by central composite design (CCD) was employed. A maximum conversion of 88.57% was obtained while changing one factor at a time, at optimum conditions of temperature (50 °C), enzyme dose (2%), molar ratio acid to alcohol (1:3), speed of agitation 250 rpm and reaction time of 120 min. Based on this RSM study, the optimum predicted conditions were: 1:3.39 alcohol to acid ratio, 2.35% enzyme loading and 48.83 oC, for a predicted conversion of 90.99%. The activation energy for the enzymatic esterification was determined and calculated to be 25.76 kJ/mol. The positive values of Gibbs-free energy (ΔG), enthalpy (ΔH) and negative value of entropy (ΔS) revealed that the esterification reaction was non-spontaneous and an endothermic reaction. The reaction seems to follow bi-substrate Ping Pong Bi Bi mechanism with inhibition by both substrates.

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Editorial

Journal Editor
Rafael Vazquez-Duhalt, Universidad Nacional Autónoma de México, Mexico

Associate Editor
Guillermo R. Castro, National University of La Plata, Argentina
Eduardo García-Junceda, Instituto de Química Orgánica General, CSIC, Spain
David Gonzalez, Universidad de la República, Uruguay
Jean-Luc Jestin, France
Enzo Laurenti, Università di Torino, Italy
Andrea Salis, University of Cagliari, Italy

Editorial Advisory Board
Spiros Agathos, Universite Catholique de Louvain, Belgium
Miguel Alcalde, Institute of Catalysis and Petrochemistry (CSIC), Spain
Riccardo Basosi, Universita di Siena, Italy
Patrick C. Cirino, University of Houston, USA
Tadashi Ema, Graduate School of Natural Science and Technology, Japan
Roberto Fernandez-Lafuente, ICP-CSIC, Spain
Richard A. Gross, Rensselaer Polytechnic Institute (RPI), USA
Frank Hollmann, Delft University of Technology, Netherlands
Evgeny Katz, Clarkson University, USA
Byung-Gee Kim, Seoul National Unviersity, South Korea
Stefan Lutz, Emory University, USA
Agustin Lopez Munguía, Instituto de Biotecnología, UNAM, Mexico
Tomoko Matsuda, Tokyo Institute of Technology, Japan
Sergio Riva, Istituto di Chimica del Riconoscimento Molecolare (ICRM), CNR, Italy
Francesco Secundo, National Research Council of Italy, Italy
Burckhard Seelig, University of Minnesota, USA
Rein V. Ulijn, City University of New York, USA
Roland Wohlgemuth, Sigma-Aldrich, Member of Merck Group, USA
John M. Woodley, Technical University of Denmark, Denmark
Huimin Zhao, University of Illinois at Urbana-Champaign, USA

Assistant Editor
Marcela Ayala, National Autonomous University of Mexico (UNAM), Mexico
Jianquan Luo, Technical University of Denmark

Language Editor
Kevin R. Kaufmann, University of California, San Diego, USA
Lisa Pilkington, University of Auckland, New Zealand

Publisher
DE GRUYTER Poland
Bogumiła Zuga 32A Str.
01-811 Warsaw, Poland
T: +48 22 701 50 15

(Deutsch)

Type: Journal
Language: English
Publisher: De Gruyter Open Access
First published: October 3, 2014
Last published: January 1, 2018
Publication Frequency: 1 Issue per Year