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Journals
Catalysts
Special Issues
Design and Application of Advanced Biocatalysts
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Design and Application of Advanced Biocatalysts

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

Deadline for manuscript submissions: closed (31 December 2022) | Viewed by 7964

Special Issue Editors

Prof. Dr. Maria H. L. Ribeiro

E-Mail Website
Guest Editor
Faculty of Pharmacy, University of Lisbon, 1649-003 Lisbon, Portugal
Interests: biocatalysis; enzyme immobilization; stabilization and purification; bioactive compounds; microreactors; bioprocesses optimization; pharmaceutical biotechnology
Dr. Bin Wu

E-Mail Website
Guest Editor
College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, No. 30 Puzhu South Road, Jiangbei New Area, Nanjing 211800, China
Interests: enzyme engineering (such as cellulase, xylanase, lipase, decarboxylase, etc)

Special Issue Information

Dear Colleagues,

It is my pleasure to invite you to contribute to the Special Issue “Design and Application of Advanced Biocatalysts”, which aims to present recent advances in the design and development of biocatalysts based on different strategies, including whole-cell, enzyme, and protein engineering (e.g., rational design, directed evolution, metagenomics); multi-enzyme systems; immobilization; among others. This Special Issue will focus on recent and emerging advances in the area of enzyme technologies and the integration of protein and process engineering critical to implementation in manufacturing processes toward applications in various the fields of health, food, and chemistry.

Nowadays, biocatalysts are very appealing to industry, namely, the pharmaceutical, food, cosmetic, and textile industries. In the context of green and sustainable chemistry, biocatalysis represents an interesting alternative, able to synthesize products not accessible through conventional chemistry approaches, due to the comparatively mild reaction conditions; high activities; chemo-, regio-, and stereoselectivities of biocatalysts; generally shorter reaction time; lower energy consumption; and lower waste generation. Of particular interest are biocatalysts aimed at the optimization of discovery and production, immobilization and recycling, process and sustainability design and metrics that are fundamental to accessing new activities and increasing catalytic efficiency and stability.

Prof. Dr. Maria H. L. Ribeiro
Dr. Bin Wu
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. 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 2700 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

  • design
  • biocatalysts
  • biocatalysis
  • immobilization
  • protein engineering
  • process engineering
  • applications
  • pharmaceutical, food, and cosmetics industies

Published Papers (3 papers)

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Research

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10 pages, 3726 KiB  
Article
Enzymatic Preparation of l-Malate in a Reaction System with Product Separation and Enzyme Recycling
by Guosi Li, Fucheng Zhu, Fangli Gu, Xinjian Yin, Qilin Xu, Menghua Ma, Li Zhu, Baowei Lu and Naidong Chen
Catalysts 2022, 12(6), 587; https://0-doi-org.brum.beds.ac.uk/10.3390/catal12060587 - 27 May 2022
Cited by 3 | Viewed by 1499
Abstract
Reaction coupling separation systems using calcium fumarate as a substrate can break the reaction equilibrium and promote the production of l-malate. However, the low reusability and stability of fumarase limit its further application. In this study, partially purified fumarase of Thermus thermophilus [...] Read more.
Reaction coupling separation systems using calcium fumarate as a substrate can break the reaction equilibrium and promote the production of l-malate. However, the low reusability and stability of fumarase limit its further application. In this study, partially purified fumarase of Thermus thermophilus (87.0 U mg−1) was immobilized within konjac-κ-carrageenan beads. An amalgamation of konjac and carrageenan gum (2%) was used to form the beads, and polyethylene polyamine (0.2%) and glutaraldehyde (0.1%) were used as the cross-linking agents. The pH and temperature profiles of free and immobilized fumarases were remarkably similar. The diffusion limit of immobilized fumarase caused a decline in the maximal velocity (Vmax), whereas the kinetic constant (Km) value increased. Optimization of the parameters for biotransformation by immobilized fumarase showed that 88.3% conversion of 200 mM calcium fumarate could be achieved at 55 °C within 8 h. The beads were stored for 30 days at 4 °C with minimal loss in activity and were reusable for up to 20 cycles with 78.1% relative activity. By recycling the reaction supernatant, a total amount of 3.98 M calcium fumarate was obtained with a conversion of 99.5%, which is the highest value ever reported. Full article
(This article belongs to the Special Issue Design and Application of Advanced Biocatalysts)
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26 pages, 5856 KiB  
Article
Design of a New Gemini Lipoaminoacid with Immobilized Lipases Based on an Eco-Friendly Biosynthetic Process
by Patrícia M. Carvalho, Rita C. Guedes, Maria R. Bronze, Célia M. C. Faustino and Maria H. L. Ribeiro
Catalysts 2021, 11(2), 164; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11020164 - 25 Jan 2021
Cited by 1 | Viewed by 1742
Abstract
Lipoaminoacids (LAA) are an important group of biosurfactants, formed by a polar hydrophilic part (amino acid) and a hydrophobic tail (lipid). The gemini LAA structures allow the formation of a supramolecular complex with bioactive molecules, like DNA, which provides them with good transfection [...] Read more.
Lipoaminoacids (LAA) are an important group of biosurfactants, formed by a polar hydrophilic part (amino acid) and a hydrophobic tail (lipid). The gemini LAA structures allow the formation of a supramolecular complex with bioactive molecules, like DNA, which provides them with good transfection efficiency. Since lipases are naturally involved in lipid and protein metabolism, they are an alternative to the chemical production of LAA, offering an eco-friendly biosynthetic process option. This work aimed to design the production of novel cystine derived gemini through a bioconversion system using immobilized lipases. Three lipases were used: porcine pancreatic lipase (PPL); lipase from Thermomyces lanuginosus (TLL); and lipase from Rizhomucor miehei (RML). PPL was immobilized in sol-gel lenses. L-cystine dihydrochloride and dodecylamine were used as substrates for the bioreaction. The production of LAA was evaluated by thin layer chromatography (TLC), and colorimetric reaction with eosin. The identification and quantification was carried out by High Performance Liquid Chromatographer-Mass Spectrometry (HPLC-MS/MS). The optimization of media design included co-solvent (methanol, dimethylsulfoxide), biphasic (n-hexane and 2-propanol) or solvent-free media, in order to improve the biocatalytic reaction rates and yields. Moreover, a new medium was tested where dodecylamine was melted and added to the cystine and to the biocatalyst, building a system of mainly undissolved substrates, leading to 5 mg/mL of LAA. Most of the volume turned into foam, which indicated the production of the biosurfactant. For the first time, the gemini derived cystine lipoaminoacid was produced, identified, and quantified in both co-solvent and solvent-free media, with the lipases PPL, RML, and TLL. Full article
(This article belongs to the Special Issue Design and Application of Advanced Biocatalysts)
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Review

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24 pages, 5734 KiB  
Review
Integrative Structural and Computational Biology of Phytases for the Animal Feed Industry
by Nima Ghahremani Nezhad, Raja Noor Zaliha Raja Abd Rahman, Yahaya M. Normi, Siti Nurbaya Oslan, Fairolniza Mohd Shariff and Thean Chor Leow
Catalysts 2020, 10(8), 844; https://0-doi-org.brum.beds.ac.uk/10.3390/catal10080844 - 28 Jul 2020
Cited by 8 | Viewed by 4081
Abstract
Resistance to high temperature, acidic pH and proteolytic degradation during the pelleting process and in the digestive tract are important features of phytases as animal feed. The integration of insights from structural and in silico analyses into factors affecting thermostability, acid stability, proteolytic [...] Read more.
Resistance to high temperature, acidic pH and proteolytic degradation during the pelleting process and in the digestive tract are important features of phytases as animal feed. The integration of insights from structural and in silico analyses into factors affecting thermostability, acid stability, proteolytic stability, catalytic efficiency and specific activity, as well as N-glycosylation, could improve the limitations of marginal stable biocatalysts with trade-offs between stability and activity. Synergistic mutations give additional benefits to single substitutions. Rigidifying the flexible loops or inter-molecular interactions by reinforcing non-bonded interactions or disulfide bonds, based on structural and roof mean square fluctuation (RMSF) analyses, are contributing factors to thermostability. Acid stability is normally achieved by targeting the vicinity residue at the active site or at the neighboring active site loop or the pocket edge adjacent to the active site. Extending the positively charged surface, altering protease cleavage sites and reducing the affinity of protease towards phytase are among the reported contributing factors to improving proteolytic stability. Remodeling the active site and removing steric hindrance could enhance phytase activity. N-glycosylation conferred improved thermostability, proteases degradation and pH activity. Hence, the integration of structural and computational biology paves the way to phytase tailoring to overcome the limitations of marginally stable phytases to be used in animal feeds. Full article
(This article belongs to the Special Issue Design and Application of Advanced Biocatalysts)
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