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Applied Sciences
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Trends in Biocatalysts Technology
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Trends in Biocatalysts Technology

A special issue of Applied Sciences (ISSN 2076-3417). This special issue belongs to the section "Applied Biosciences and Bioengineering".

Deadline for manuscript submissions: closed (30 April 2021) | Viewed by 12230

Special Issue Editors

Assoc. Prof. Carl Grey

E-Mail Website
Guest Editor
Division of Biotechnology, Department of Chemistry, Lund University, Naturvetarvägen 14, 221 00 Lund, Sweden
Interests: enzyme technology; biocatalysis; bioprocess engineering; bioanalytical chemistry
Dr. Javier Linares-Pastén

E-Mail Website
Guest Editor
Department of Chemistry, Lund University, 22100 Lund, Sweden
Interests: molecular biotechnology; biocatalysts engineering; development of biorefinery processes
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Biocatalysis uses enzymes, either in pure form or as whole cells. In nature, they are responsible for performing most chemical reactions required in all living things. It is certainly possible to mimic this feature and also adapt biocatalysis for chemical transformation of industrial interest.

Biocatalysts are of great importance in the industry due their high selectivity and ability to work in mild conditions, including water as solvent, moderate temperatures and pH. High selectivity in combination with mild conditions results in a few byproducts, and together with the catalyst itself being renewable, this often makes biocatalysis an environmentally friendly approach. Despite these benefits, however, breakthrough technologies are still required to overcome a number of limitations regarding volumetric productivity, product titer, stability, and operational costs, among others.

Current research is focused on discovering novel enzymes, but also on nucleic acids and other biomolecules as catalysts. On the other hand, whole cells and even microbial consortia are also used for the conversion of a broad variety of raw materials in high-value products. In this Special Issue, we invite submissions that investigate diverse strategies, such as novel enzyme discovery, immobilization of enzymes or cells, biomolecular engineering, metabolic engineering, and new technologies for the development of biocatalysts addressing the future of the industrial bioprocesses.

Assoc. Prof. Carl Grey
Assoc. Prof. Javier Linares-Pastén
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 submissions that pass pre-check are 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. Applied Sciences is an international peer-reviewed open access semimonthly 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 2400 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

  • novel enzymes with potential industrial applications
  • enzyme engineering
  • biotransformations with whole cells
  • catalytic biomolecules other than enzymes
  • bioinformatic and computational approaches in biocatalysis

Published Papers (4 papers)

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Research

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16 pages, 3394 KiB  
Article
Assessment of IsPETase-Assisted Depolymerization of Terephthalate Aromatic Polyesters and the Effect of the Thioredoxin Fusion Domain
by Paula Wagner-Egea, Virginia Tosi, Ping Wang, Carl Grey, Baozhong Zhang and Javier A. Linares-Pastén
Appl. Sci. 2021, 11(18), 8315; https://0-doi-org.brum.beds.ac.uk/10.3390/app11188315 - 08 Sep 2021
Cited by 5 | Viewed by 4054
Abstract
Terephthalate polyesters such as poly(ethylene terephthalate) (PET) have been massively produced over the last few decades due to their attractive properties in multiple applications. However, due to their limited biodegradability, they have accumulated in landfills and oceans, posing an environmental threat. Enzymatic recycling [...] Read more.
Terephthalate polyesters such as poly(ethylene terephthalate) (PET) have been massively produced over the last few decades due to their attractive properties in multiple applications. However, due to their limited biodegradability, they have accumulated in landfills and oceans, posing an environmental threat. Enzymatic recycling technologies are predicted to generate long-term socioeconomic benefits. In the present work, we compared the IsPETase (from Ideonella sakaiensis 201-F6) activity on a series of polyesters, including poly(butylene) terephthalate (PBT), poly(hexamethylene) terephthalate (PHT) and Akestra™, with PET. The IsPETase showed remarkable activity toward PET (39% degradation of the original polyester) that was higher than that toward Akestra™ (0.13%), PBT (0.25%) and PHT (0.13%) after 72 h. Thus, based on experimental data and computational analysis, we report insights into IsPETase activity on a series of terephthalate-based polyesters. Aside from that, the fusion domain (Trx) effect in the production and activity of a recombinant Trx-IsPETase is reported. Full article
(This article belongs to the Special Issue Trends in Biocatalysts Technology)
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18 pages, 62935 KiB  
Article
Modeled 3D-Structures of Proteobacterial Transglycosylases from Glycoside Hydrolase Family 17 Give Insight in Ligand Interactions Explaining Differences in Transglycosylation Products
by Javier A. Linares-Pastén, Lilja Björk Jonsdottir, Gudmundur O. Hreggvidsson, Olafur H. Fridjonsson, Hildegard Watzlawick and Eva Nordberg Karlsson
Appl. Sci. 2021, 11(9), 4048; https://0-doi-org.brum.beds.ac.uk/10.3390/app11094048 - 29 Apr 2021
Cited by 3 | Viewed by 1565
Abstract
The structures of glycoside hydrolase family 17 (GH17) catalytic modules from modular proteins in the ndvB loci in Pseudomonas aeruginosa (Glt1), P. putida (Glt3) and Bradyrhizobium diazoefficiens (previously B. japonicum) (Glt20) were modeled to shed light on reported differences between these homologous [...] Read more.
The structures of glycoside hydrolase family 17 (GH17) catalytic modules from modular proteins in the ndvB loci in Pseudomonas aeruginosa (Glt1), P. putida (Glt3) and Bradyrhizobium diazoefficiens (previously B. japonicum) (Glt20) were modeled to shed light on reported differences between these homologous transglycosylases concerning substrate size, preferred cleavage site (from reducing end (Glt20: DP2 product) or non-reducing end (Glt1, Glt3: DP4 products)), branching (Glt20) and linkage formed (1,3-linkage in Glt1, Glt3 and 1,6-linkage in Glt20). Hybrid models were built and stability of the resulting TIM-barrel structures was supported by molecular dynamics simulations. Catalytic amino acids were identified by superimposition of GH17 structures, and function was verified by mutagenesis using Glt20 as template (i.e., E120 and E209). Ligand docking revealed six putative subsites (−4, −3, −2, −1, +1 and +2), and the conserved interacting residues suggest substrate binding in the same orientation in all three transglycosylases, despite release of the donor oligosaccharide product from either the reducing (Glt20) or non-reducing end (Glt1, Gl3). Subsites +1 and +2 are most conserved and the difference in release is likely due to changes in loop structures, leading to loss of hydrogen bonds in Glt20. Substrate docking in Glt20 indicate that presence of covalently bound donor in glycone subsites −4 to −1 creates space to accommodate acceptor oligosaccharide in alternative subsites in the catalytic cleft, promoting a branching point and formation of a 1,6-linkage. The minimum donor size of DP5, can be explained assuming preferred binding of DP4 substrates in subsite −4 to −1, preventing catalysis. Full article
(This article belongs to the Special Issue Trends in Biocatalysts Technology)
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Review

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36 pages, 1183 KiB  
Review
Metagenomic Discovery and Characterization of Multi-Functional and Monomodular Processive Endoglucanases as Biocatalysts
by Ming Z. Fan, Weijun Wang, Laurence Cheng, Jiali Chen, Wenyi Fan and Min Wang
Appl. Sci. 2021, 11(11), 5150; https://0-doi-org.brum.beds.ac.uk/10.3390/app11115150 - 01 Jun 2021
Cited by 7 | Viewed by 2562
Abstract
Biomass includes cellulose, hemicelluloses, pectin and lignin; constitutes the components of dietary fibre of plant and alge origins in animals and humans; and can potentially provide inexhaustible basic monomer compounds for developing sustainable biofuels and biomaterials for the world. Development of efficacious cellulases [...] Read more.
Biomass includes cellulose, hemicelluloses, pectin and lignin; constitutes the components of dietary fibre of plant and alge origins in animals and humans; and can potentially provide inexhaustible basic monomer compounds for developing sustainable biofuels and biomaterials for the world. Development of efficacious cellulases is the key to unlock the biomass polymer and unleash its potential applications in society. Upon reviewing the current literature of cellulase research, two characterized and/or engineered glycosyl hydrolase family-5 (GH5) cellulases have displayed unique properties of processive endoglucanases, including GH5-tCel5A1 that was engineered and was originally identified via targeted genome sequencing of the extremely thermophilic Thermotoga maritima and GH5-p4818Cel5_2A that was screened out of the porcine hindgut microbial metagenomic expression library. Both GH5-tCel5A1 and GH5-p4818Cel5_2A have been characterized as having small molecular weights with an estimated spherical diameter at or < 4.6 nm; being monomodular without a required carbohydrate-binding domain; and acting as processive β-1,4-endoglucanases. These two unique GH5-tCel5A1 and GH5-p4818Cel5_2A processive endocellulases are active in hydrolyzing natural crystalline and pre-treated cellulosic substrates and have multi-functionality towards several hemicelluloses including β-glucans, xylan, xylogulcans, mannans, galactomannans and glucomannans. Therefore, these two multifunctional and monomodular GH5-tCel5A1 and GH5-p4818Cel5_2A endocellulases already have promising structural and functional properties for further optimization and industrial applications. Full article
(This article belongs to the Special Issue Trends in Biocatalysts Technology)
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14 pages, 1644 KiB  
Review
Enzymatic Synthesis and Characterization of Different Families of Chitooligosaccharides and Their Bioactive Properties
by Noa Miguez, Peter Kidibule, Paloma Santos-Moriano, Antonio O. Ballesteros, Maria Fernandez-Lobato and Francisco J. Plou
Appl. Sci. 2021, 11(7), 3212; https://0-doi-org.brum.beds.ac.uk/10.3390/app11073212 - 03 Apr 2021
Cited by 26 | Viewed by 3291
Abstract
Chitooligosaccharides (COS) are homo- or hetero-oligomers of D-glucosamine (GlcN) and N-acetyl-D-glucosamine (GlcNAc) that can be obtained by chitosan or chitin hydrolysis. Their enzymatic production is preferred over other methodologies (physical, chemical, etc.) due to the mild conditions required, the fewer amounts of waste [...] Read more.
Chitooligosaccharides (COS) are homo- or hetero-oligomers of D-glucosamine (GlcN) and N-acetyl-D-glucosamine (GlcNAc) that can be obtained by chitosan or chitin hydrolysis. Their enzymatic production is preferred over other methodologies (physical, chemical, etc.) due to the mild conditions required, the fewer amounts of waste and its efficiency to control product composition. By properly selecting the enzyme (chitinase, chitosanase or nonspecific enzymes) and the substrate properties (degree of deacetylation, molecular weight, etc.), it is possible to direct the synthesis towards any of the three COS types: fully acetylated (faCOS), partially acetylated (paCOS) and fully deacetylated (fdCOS). In this article, we review the main strategies to steer the COS production towards a specific group. The chemical characterization of COS by advanced techniques, e.g., high-performance anion-exchange chromatography with pulsed amperometric detection (HPAEC-PAD) and MALDI-TOF mass spectrometry, is critical for structure–function studies. The scaling of processes to synthesize specific COS mixtures is difficult due to the low solubility of chitin/chitosan, the heterogeneity of the reaction mixtures, and high amounts of salts. Enzyme immobilization can help to minimize such hurdles. The main bioactive properties of COS are herein reviewed. Finally, the anti-inflammatory activity of three COS mixtures was assayed in murine macrophages after stimulation with lipopolysaccharides. Full article
(This article belongs to the Special Issue Trends in Biocatalysts Technology)
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