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) | Viewed by 52144

Special Issue Editors

Department of Chemistry - University of Crete, Voutes University Campus, 70013 Heraklion, Greece
Interests: enzyme discovery; enzyme optimization; protein engineering; biocatalysis; biomass and waste valorization
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
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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Keywords

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

Published Papers (9 papers)

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Research

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12 pages, 3415 KiB  
Article
Immobilization of Phospholipase D on Silica-Coated Magnetic Nanoparticles for the Synthesis of Functional Phosphatidylserine
by Qingqing Han, Haiyang Zhang, Jianan Sun, Zhen Liu, Wen-can Huang, Changhu Xue and Xiangzhao Mao
Catalysts 2019, 9(4), 361; https://doi.org/10.3390/catal9040361 - 15 Apr 2019
Cited by 11 | Viewed by 2778
Abstract
In this study, silica-coated magnetic nanoparticles (Fe3O4/SiO2) were synthesized and applied in the immobilization of phospholipase D (PLDa2) via physical adsorption and covalent attachment. The immobilized PLDa2 was applied in the synthesis of functional [...] Read more.
In this study, silica-coated magnetic nanoparticles (Fe3O4/SiO2) were synthesized and applied in the immobilization of phospholipase D (PLDa2) via physical adsorption and covalent attachment. The immobilized PLDa2 was applied in the synthesis of functional phosphatidylserine (PS) through a transphophatidylation reaction. The synthesis process and characterizations of the carriers were examined by scanning electron microscope (SEM), transmission electron microscope (TEM), and Fourier-transform infrared spectroscopy (FT-IR). The optimum immobilization conditions were evaluated, and the thermal and pH stability of immobilized and free PLDa2 were measured and compared. The tolerance to high temperature of immobilized PLDa2 increased remarkably by 10°C. Furthermore, the catalytic activity of the immobilized PLDa2 remained at 40% after eight recycles, which revealed that silica-coated magnetic nanoparticles have potential application for immobilization and catalytic reactions in a biphasic system. Full article
(This article belongs to the Special Issue Biocatalysis for Industrial Applications)
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17 pages, 1825 KiB  
Communication
An Enzyme Cascade Synthesis of Vanillin
by Tobias Klaus, Alexander Seifert, Tim Häbe, Bettina M. Nestl and Bernhard Hauer
Catalysts 2019, 9(3), 252; https://doi.org/10.3390/catal9030252 - 12 Mar 2019
Cited by 17 | Viewed by 5978
Abstract
A novel approach for the synthesis of vanillin employing a three-step two-enzymatic cascade sequence is reported. Cytochrome P450 monooxygenases are known to catalyse the selective hydroxylation of aromatic compounds, which is one of the most challenging chemical reactions. A set of rationally designed [...] Read more.
A novel approach for the synthesis of vanillin employing a three-step two-enzymatic cascade sequence is reported. Cytochrome P450 monooxygenases are known to catalyse the selective hydroxylation of aromatic compounds, which is one of the most challenging chemical reactions. A set of rationally designed variants of CYP102A1 (P450 BM3) from Bacillus megaterium at the amino acid positions 47, 51, 87, 328 and 437 was screened for conversion of the substrate 3-methylanisole to vanillyl alcohol via the intermediate product 4-methylguaiacol. Furthermore, a vanillyl alcohol oxidase (VAO) variant (F454Y) was selected as an alternative enzyme for the transformation of one of the intermediate compounds via vanillyl alcohol to vanillin. As a proof of concept, the bi-enzymatic three-step cascade conversion of 3-methylanisole to vanillin was successfully evaluated both in vitro and in vivo. Full article
(This article belongs to the Special Issue Biocatalysis for Industrial Applications)
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15 pages, 4629 KiB  
Article
The Synthesis of Mannose-6-Phosphate Using Polyphosphate-Dependent Mannose Kinase
by Wenlong Zhu, Miaomiao Gao, Biqiang Chen, Tianwei Tan, Hui Cao and Luo Liu
Catalysts 2019, 9(3), 250; https://doi.org/10.3390/catal9030250 - 09 Mar 2019
Cited by 3 | Viewed by 3462
Abstract
Mannose-6-phosphate (M6P) is involved in many metabolic pathways in life, and it has important applications in the treatment of diseases. This study explored a cost-effective enzyme catalytic synthesis method of M6P, using polyphosphate-dependent mannose kinase from Arthrobacter species. This synthesis uses polyphosphate to [...] Read more.
Mannose-6-phosphate (M6P) is involved in many metabolic pathways in life, and it has important applications in the treatment of diseases. This study explored a cost-effective enzyme catalytic synthesis method of M6P, using polyphosphate-dependent mannose kinase from Arthrobacter species. This synthesis uses polyphosphate to replace expensive ATP, and it is greener and safer than chemical synthesis. This study investigated the effects of key factors such as metal ions, temperature, and substrate addition on this enzymatic reaction, and improved the conversion efficiency. We moreover take advantage of the response surface method to explore the best catalytic conditions synthetically. The conversion was 99.17% successful under the optimal reaction conditions. After a series of optimizations, we carried out a 200 mL scale-up experiment, which proved that the method has good prospects for industrial applications. Full article
(This article belongs to the Special Issue Biocatalysis for Industrial Applications)
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11 pages, 2025 KiB  
Communication
Synthetic Biomimetic Coenzymes and Alcohol Dehydrogenases for Asymmetric Catalysis
by Laia Josa-Culleré, Antti S. K. Lahdenperä, Aubert Ribaucourt, Georg T. Höfler, Serena Gargiulo, Yuan-Yang Liu, Jian-He Xu, Jennifer Cassidy, Francesca Paradisi, Diederik J. Opperman, Frank Hollmann and Caroline E. Paul
Catalysts 2019, 9(3), 207; https://doi.org/10.3390/catal9030207 - 26 Feb 2019
Cited by 16 | Viewed by 6011
Abstract
Redox reactions catalyzed by highly selective nicotinamide-dependent oxidoreductases are rising to prominence in industry. The cost of nicotinamide adenine dinucleotide coenzymes has led to the use of well-established elaborate regeneration systems and more recently alternative synthetic biomimetic cofactors. These biomimetics are highly attractive [...] Read more.
Redox reactions catalyzed by highly selective nicotinamide-dependent oxidoreductases are rising to prominence in industry. The cost of nicotinamide adenine dinucleotide coenzymes has led to the use of well-established elaborate regeneration systems and more recently alternative synthetic biomimetic cofactors. These biomimetics are highly attractive to use with ketoreductases for asymmetric catalysis. In this work, we show that the commonly studied cofactor analogue 1-benzyl-1,4-dihydronicotinamide (BNAH) can be used with alcohol dehydrogenases (ADHs) under certain conditions. First, we carried out the rhodium-catalyzed recycling of BNAH with horse liver ADH (HLADH), observing enantioenriched product only with unpurified enzyme. Then, a series of cell-free extracts and purified ketoreductases were screened with BNAH. The use of unpurified enzyme led to product formation, whereas upon dialysis or further purification no product was observed. Several other biomimetics were screened with various ADHs and showed no or very low activity, but also no inhibition. BNAH as a hydride source was shown to directly reduce nicotinamide adenine dinucleotide (NAD) to NADH. A formate dehydrogenase could also mediate the reduction of NAD from BNAH. BNAH was established to show no or very low activity with ADHs and could be used as a hydride donor to recycle NADH. Full article
(This article belongs to the Special Issue Biocatalysis for Industrial Applications)
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23 pages, 3639 KiB  
Article
A Novel Method of Affinity Tag Cleavage in the Purification of a Recombinant Thermostable Lipase from Aneurinibacillus thermoaerophilus Strain HZ
by Malihe Masomian, Raja Noor Zaliha Raja Abd Rahman and Abu Bakar Salleh
Catalysts 2018, 8(10), 479; https://doi.org/10.3390/catal8100479 - 20 Oct 2018
Cited by 8 | Viewed by 4812
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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10 pages, 7643 KiB  
Article
Immobilization of Chitosanases onto Magnetic Nanoparticles to Enhance Enzyme Performance
by Wei Wang, Na Guo, Wencan Huang, Zhaohui Zhang and Xiangzhao Mao
Catalysts 2018, 8(9), 401; https://doi.org/10.3390/catal8090401 - 18 Sep 2018
Cited by 16 | Viewed by 4021
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 (MNPs@chitosanase). 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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20 pages, 2715 KiB  
Review
Industrial Application of 2-Oxoglutarate-Dependent Oxygenases
by Christin Peters and Rebecca M. Buller
Catalysts 2019, 9(3), 221; https://doi.org/10.3390/catal9030221 - 28 Feb 2019
Cited by 39 | Viewed by 8881
Abstract
C–H functionalization is a chemically challenging but highly desirable transformation. 2-oxoglutarate-dependent oxygenases (2OGXs) are remarkably versatile biocatalysts for the activation of C–H bonds. In nature, they have been shown to accept both small and large molecules carrying out a plethora of reactions, including [...] Read more.
C–H functionalization is a chemically challenging but highly desirable transformation. 2-oxoglutarate-dependent oxygenases (2OGXs) are remarkably versatile biocatalysts for the activation of C–H bonds. In nature, they have been shown to accept both small and large molecules carrying out a plethora of reactions, including hydroxylations, demethylations, ring formations, rearrangements, desaturations, and halogenations, making them promising candidates for industrial manufacture. In this review, we describe the current status of 2OGX use in biocatalytic applications concentrating on 2OGX-catalyzed oxyfunctionalization of amino acids and synthesis of antibiotics. Looking forward, continued bioinformatic sourcing will help identify additional, practical useful members of this intriguing enzyme family, while enzyme engineering will pave the way to enhance 2OGX reactivity for non-native substrates. Full article
(This article belongs to the Special Issue Biocatalysis for Industrial Applications)
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18 pages, 2615 KiB  
Review
Application of Cell-Free Protein Synthesis for Faster Biocatalyst Development
by Jascha Rolf, Katrin Rosenthal and Stephan Lütz
Catalysts 2019, 9(2), 190; https://doi.org/10.3390/catal9020190 - 19 Feb 2019
Cited by 36 | Viewed by 9743
Abstract
Cell-free protein synthesis (CFPS) has become an established tool for rapid protein synthesis in order to accelerate the discovery of new enzymes and the development of proteins with improved characteristics. Over the past years, progress in CFPS system preparation has been made towards [...] Read more.
Cell-free protein synthesis (CFPS) has become an established tool for rapid protein synthesis in order to accelerate the discovery of new enzymes and the development of proteins with improved characteristics. Over the past years, progress in CFPS system preparation has been made towards simplification, and many applications have been developed with regard to tailor-made solutions for specific purposes. In this review, various preparation methods of CFPS systems are compared and the significance of individual supplements is assessed. The recent applications of CFPS are summarized and the potential for biocatalyst development discussed. One of the central features is the high-throughput synthesis of protein variants, which enables sophisticated approaches for rapid prototyping of enzymes. These applications demonstrate the contribution of CFPS to enhance enzyme functionalities and the complementation to in vivo protein synthesis. However, there are different issues to be addressed, such as the low predictability of CFPS performance and transferability to in vivo protein synthesis. Nevertheless, the usage of CFPS for high-throughput enzyme screening has been proven to be an efficient method to discover novel biocatalysts and improved enzyme variants. Full article
(This article belongs to the Special Issue Biocatalysis for Industrial Applications)
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23 pages, 2314 KiB  
Review
Biocatalytic Synthesis of Fungal β-Glucans
by Lefki-Maria Papaspyridi, Anastasia Zerva and Evangelos Topakas
Catalysts 2018, 8(7), 274; https://doi.org/10.3390/catal8070274 - 06 Jul 2018
Cited by 19 | Viewed by 5393
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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