Special Issue "Biocatalysis for Industrial Applications"

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

Deadline for manuscript submissions: closed (31 January 2019)

Special Issue Editors

Guest Editor
Dr. Ioannis V. Pavlidis

Department of Chemistry - University of Crete, Voutes University Campus, 70013, Heraklion, Greece
Website | E-Mail
Interests: enzyme discovery; enzyme optimization; protein engineering; biocatalysis; biomass and waste valorization
Guest Editor
Dr. Per-Olof Syrén

School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Fibre and polymer Technology, Science for Life Laboratory, KTH Royal Institute of Technology, Teknikringen 56-58, 100 44 Stockholm, Sweden
Website | E-Mail
Interests: in silico enzyme design; bioinformatics; enzyme discovery; protein mass spectrometry; synthetic biology; artificial pathway design; polymer technology; material recycling

Special Issue Information

Dear Colleagues,

Biocatalysis has been established as a competitive alternative to traditional metallo- and organo-catalysis. The high selectivity of enzymes, together with their ability to catalyze reactions under mild conditions, have attracted the interest of industries, in some cases even to develop sustainable environmentally-friendly alternatives to commercialized chemical processes. The advances in various fields, such as biotechnology, molecular biology and bioinformatics provided the means to develop tailor-made biocatalysts, as native enzymes in most cases do not meet the industrial standards (in terms of stability, specificity and catalytic activity). With the tools of our age, we are even able to design enzymes that catalyze reactions that have never been observed in nature before. More than that, the advances in metabolic engineering and genome editing facilitated the use of the metabolism of a host to produce complicated products from simple carbon sources in one pot. Thus, there is a constant rise on the number of bioprocesses in industrial applications, especially in the food, pharma and cosmetics industry, as well on the production of basic, as well as specialized, chemicals.

This Special Issue aims to highlight the potential of biocatalysis in industry via selected articles and to emphasize the trends that lead to broader industrial enzyme applications, as well as the challenges to be faced. Submissions to this Special Issue on “Biocatalysis for Industrial Applications” are welcome in the form of original research papers or short reviews which reflect the state-of-the-art and provide a new insight via a meta-analysis of published data.

Dr. Ioannis V. Pavlidis
Dr. Per-Olof Syrén
Guest Editors

Manuscript Submission Information

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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.

Keywords

  • Enzyme technology
  • biocatalysis
  • bioprocess
  • white biotechnology
  • protein engineering
  • rational design
  • directed evolution
  • industrial requirements
  • industrial applications

Published Papers (3 papers)

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Research

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Open AccessArticle A Novel Method of Affinity Tag Cleavage in the Purification of a Recombinant Thermostable Lipase from Aneurinibacillus thermoaerophilus Strain HZ
Catalysts 2018, 8(10), 479; https://doi.org/10.3390/catal8100479
Received: 20 August 2018 / Revised: 2 October 2018 / Accepted: 9 October 2018 / Published: 20 October 2018
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Abstract
The development of an efficient and economical purification method is required to obtain a pure and mature recombinant protein in a simple process with high efficiency. Hence, a new technique was invented to cleave the tags from the N-terminal region of recombinant fusion [...] Read more.
The development of an efficient and economical purification method is required to obtain a pure and mature recombinant protein in a simple process with high efficiency. Hence, a new technique was invented to cleave the tags from the N-terminal region of recombinant fusion HZ lipase in the absence of protease treatment. The recombinant pET32b/rHZ lipase was overexpressed into E. coli BL21 (DE3). Affinity chromatography was performed as the first step of purification. The stability of the protein was then tested in different temperatures. The fused Trx-His-S-tags to the rHZ lipase was cleaved by treatment of the fusion protein at 20 °C in 100 mM Tris-HCl buffer, pH 8.0. The precipitated tag was removed, and the mature recombinant enzyme was further characterized to specify its properties. A purification yield of 78.9% with 1.3-fold and 21.8 mg total purified mature protein was obtained from 50 mL starting a bacterial culture. N-terminal sequencing of purified recombinant HZ lipase confirmed the elimination of the 17.4 kDa tag from one amino acid before the native start codon (Methionine) of the protein. The mature rHZ lipase was highly active at 65 °C and a pH of 7.0, with a half-life of 2 h 15 min at 55 °C and 45 min at 60 °C. The rHZ lipase showed a preference for the hydrolysis of natural oil with a long carbon chain (C18) and medium-size acyl chain p-nitrophenyl esters (C10). The enzyme remained stable in the presence of nonpolar organic solvents, and its activity was increased by polar organic solvents. This study thus demonstrates a simple and convenient purification method which resulted in the high yield of mature enzyme along with unique and detailed biochemical characterization of rHZ lipase, making the enzyme favorable in various industrial applications. Full article
(This article belongs to the Special Issue Biocatalysis for Industrial Applications)
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Open AccessArticle Immobilization of Chitosanases onto Magnetic Nanoparticles to Enhance Enzyme Performance
Catalysts 2018, 8(9), 401; https://doi.org/10.3390/catal8090401
Received: 7 September 2018 / Revised: 16 September 2018 / Accepted: 17 September 2018 / Published: 18 September 2018
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Abstract
In this study, chitosanase cloning from Streptomyces albolongus was fermented and purified by a Ni-NTA column. Fe3O4-SiO2 magnetite nanoparticles (MNPs) were synthesized by the co-precipitation method coating with silica via a sol-gel reaction and were then amino functioned [...] Read more.
In this study, chitosanase cloning from Streptomyces albolongus was fermented and purified by a Ni-NTA column. Fe3O4-SiO2 magnetite nanoparticles (MNPs) were synthesized by the co-precipitation method coating with silica via a sol-gel reaction and were then amino functioned by treating with 3-aminopropyltriethoxysilane. Chitosanases were immobilized onto the surface of MNPs by covalent bonding ([email protected]). Transmission electron microscopy (TEM), Fourier transform infrared spectrometer (FT–IR), and magnetic measurements were used to illustrate the MNPs and immobilized chitosanase. The optimal conditions of immobilization were studied. The thermal, pH, and stabilities of immobilized chitosanase were tested and the results showed that the stabilities were significantly enhanced compared with free chitosanase. After being recycled 10 times, the residual activity of the immobilized chitosanase was 43.7% of the initial activity. Full article
(This article belongs to the Special Issue Biocatalysis for Industrial Applications)
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Review

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Open AccessReview Biocatalytic Synthesis of Fungal β-Glucans
Catalysts 2018, 8(7), 274; https://doi.org/10.3390/catal8070274
Received: 4 May 2018 / Revised: 25 June 2018 / Accepted: 4 July 2018 / Published: 6 July 2018
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Abstract
Glucans are the dominant polysaccharide constituents of fungal cell walls. Remarkably, these major bioactive polysaccharides account for the beneficial effects that have been observed by many mushrooms of medicinal interest. Accordingly, the prevailing tendency is the use of bioactive mushroom β-glucans mainly [...] Read more.
Glucans are the dominant polysaccharide constituents of fungal cell walls. Remarkably, these major bioactive polysaccharides account for the beneficial effects that have been observed by many mushrooms of medicinal interest. Accordingly, the prevailing tendency is the use of bioactive mushroom β-glucans mainly in pharmaceutical industries or as food additives, since it seems that they can be involved in meeting the overall growing demand for food in the future, but also in medical and material sectors. β-(1,3)-Glucan synthase (GLS) is the responsible enzyme for the synthesis of these important polysaccharides, which is a member of the glycosyl transferase (GT) family. For optimizing the production of such natural polymers of great interest, the comprehension of the fungal synthetic mechanism, as well as the biochemical and molecular characteristics of the key enzyme GLS and its expression seem to be crucial. Overall, in this review article, the fungal β-glucans biosynthesis by GLS is summarized, while the in vitro synthesis of major polysaccharides is also discussed, catalyzed by glycoside hydrolases (GHs) and GTs. Possible future prospects of GLS in medicine and in developing other potential artificial composite materials with industrial applications are also summarized. Full article
(This article belongs to the Special Issue Biocatalysis for Industrial Applications)
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