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Advances in Enzyme Engineering, Biocatalysis and Biosynthesis

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

Deadline for manuscript submissions: closed (20 July 2023) | Viewed by 8399

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Special Issue Editors

Prof. Dr. Ruizhi Han

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Guest Editor

The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, China
Interests: protein engineering; enzyme engineering; multienzyme cascade reaction; synthesis of food and pharmaceutical by biocatalysis
Special Issues, Collections and Topics in MDPI journals

Dr. Gopal Patel

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Guest Editor

Sagar Institute of Pharmacy and Technology (SIPTec), Gandhi Nagar, Bhopal, India
Interests: microbial fermentation; enzyme immobilization; biocatalysis; enzyme technology; nanotechnology and biotransformation

Special Issue Information

Dear Colleagues,

Enzyme engineering is a vital, modern biotechnology to fine-tune enzymes. As a new high technology, it greatly promotes the development of life and industry. Enzyme engineering strategies not only include natural enzyme mining, heterologous expression, directed evolution, gene shuffling or family shuffling, enzyme immobilization and synzymes but also rational design based on structure–function insights, computational methods and machine learning, as well as novel scaffolding and compartmentalization techniques to improve the performance of multienzyme systems. Efficient enzyme engineering strategies improve enzymatic properties such as the activity, specificity, stability and stereoselectivity as well as balance sequential reactions and route intermediates by co-localizing multiple enzymes. This will facilitate the application of biocatalysis and biosynthesis in food, pharmaceutical and chemicals fields and accelerate the development of a green biological manufacturing industry.

Therefore, for this Special Issue, we are interested in presenting the most recent progress in advances in enzyme engineering, biocatalysis and biosynthesis. Fundamental studies to establish innovative and efficient enzyme engineering strategies as well as studies related to the development of biocatalysis and biosynthesis processes applied to industries are welcome.

It is with great pleasure and honor that we invite you to submit a review article or original research paper for possible publication in this Special Issue.

Prof. Dr. Ruizhi Han
Dr. Gopal Patel
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

enzyme engineering
protein engineering
biocatalysis
biosynthesis

Related Special Issue

Advances in Enzyme Engineering, Biocatalysis and Biosynthesis, 2nd Edition in Catalysts

Published Papers (5 papers)

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Research

12 pages, 2559 KiB

Open AccessFeature PaperArticle

Novel In Vitro Multienzyme Cascade for Efficient Synthesis of d-Tagatose from Sucrose

by Shuangyu Liu, Wenyu Tu, Ye Ni, Yuanyi Guo and Ruizhi Han

Catalysts 2023, 13(12), 1515; https://0-doi-org.brum.beds.ac.uk/10.3390/catal13121515 - 15 Dec 2023

Cited by 1 | Viewed by 1027

Abstract

d-Tagatose is a rare sugar with low calories, and is extensively used in food, beverage, and drug additives. In this study, an in vitro multienzyme cascade route for d-tagatose synthesis from sucrose (MCTS) was designed, which contains five enzymes (sucrose phosphorylase, fructokinase, d-fructose 6-phosphate 4-epimerase, d-tagatose 6-phosphate phosphatase, and polyphosphate kinase). The whole MCTS route comprised a sucrose phosphorylation reaction, and a phosphorylation–dephosphorylation reaction coupled with an ATP regeneration system. After optimization, the conversion of d-tagatose from 10 mM sucrose reached 82.3%. At an elevated sucrose concentration of 50 mM, 72.4% of d-tagatose conversion and 0.27 g·L^–1·h⁻¹ of space–time yield were obtained. Furthermore, ADP consumption decreased to 1% of the sucrose concentration after introducing the ATP regeneration system. The MCTS strategy is an efficient and cost-effective approach for d-tagatose production. Full article

(This article belongs to the Special Issue Advances in Enzyme Engineering, Biocatalysis and Biosynthesis)

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11 pages, 3130 KiB

Open AccessArticle

Engineering the Biosynthesis of prFMN Promotes the Conversion between Styrene/CO₂ and Cinnamic Acid Catalyzed by the Ferulic Acid Decarboxylase Fdc1

by Xiaoni Zhu, Hongfei Li, Jiangang Ren, Yanbin Feng and Song Xue

Catalysts 2023, 13(6), 917; https://0-doi-org.brum.beds.ac.uk/10.3390/catal13060917 - 23 May 2023

Cited by 1 | Viewed by 1699

Abstract

Enzymatic decarboxylation and carboxylation are emerging as prospective processes to produce high-value compounds under mild conditions. Ferulic acid decarboxylase Fdc1 catalyzes broad substrate tolerance against α, β-unsaturated carboxylic acids, and provides green routes for carbon dioxide fixation with the reversible carboxylation, while the activity of the enzyme is limited by the indispensable cofactor prenylated flavin (prFMN), which is unstable and is rarely detected in nature. In this study, a prFMN efficient synthesis route was built using six exogenous enzymes introduced into E. coli cells, leading to the construction of a powerful cell catalyst named SC-6. Based on the metabolic analysis, the results indicated that the reduction of FMN to FMNH₂ was the bottleneck in prFMN synthesis pathway, and introducing FMN reductase increased the production of prFMN 3.8-fold compared with the common flavin prenyltransferase UbiX overexpression strain. Using SC-6 cell catalyst, the decarboxylation activity of Fdc1 increased more than 20 times with cinnamic acid and 4-acetoxycinnamic acid as substrates. Furthermore, the reversible carboxylation reaction was carried out, and the cell catalyst presented 20 times carbon dioxide fixation activity using styrene to produce cinnamic acid. Finally, the maximum yield of cinnamic acid catalyzed by SC-6 achieved 833.68 ± 34.51 mM·mg⁻¹ in two hours. The constructed prFMN pathway in vivo provides fundamentals for efficient decarboxylation and carbon fixation reactions catalyzed by prFMN-dependent enzymes. Full article

(This article belongs to the Special Issue Advances in Enzyme Engineering, Biocatalysis and Biosynthesis)

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14 pages, 2856 KiB

Open AccessEditor’s ChoiceArticle

Role of N-Terminal Extensional Long α-Helix in the Arylesterase from Lacticaseibacillus rhamnosus GG on Catalysis and Stability

by Bin-Chun Li, Tongtong Guo, Xue Li, Xueting Hou and Guo-Bin Ding

Catalysts 2023, 13(2), 441; https://0-doi-org.brum.beds.ac.uk/10.3390/catal13020441 - 18 Feb 2023

Viewed by 1045

Abstract

In the α/β hydrolases superfamily, the extra module modulated enzymatic activity, substrate specificity, and stability. The functional role of N-terminal extensional long α-helix (Ala2-Glu29, designated as NEL-helix) acting as the extra module in the arylesterase LggEst from Lacticaseibacillus rhamnosus GG had been systemically investigated by deletion mutagenesis, biochemical characterization, and biophysical methods. The deletion of the NEL-helix did not change the overall structure of this arylesterase. The deletion of the NEL-helix led to the shifting of optimal pH into the acidity and the loss of thermophilic activity. The deletion of the NEL-helix produced a 10.6-fold drop in catalytic activity towards the best substrate pNPC10. NEL-Helix was crucial for the thermostability, chemical resistance, and organic solvents tolerance. The deletion of the NEL-helix did not change the overall rigidity of enzyme structure and only reduced the local rigidity of the active site. Sodium deoxycholate might partially replenish the loss of activity caused by the deletion of the NEL-helix. Our research further enriched the functional role of the extra module on catalysis and stability in the α/β hydrolase fold superfamily. Full article

(This article belongs to the Special Issue Advances in Enzyme Engineering, Biocatalysis and Biosynthesis)

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9 pages, 5271 KiB

Open AccessFeature PaperArticle

Enzymatic Formation of Recombinant Antibody-Conjugated Gold Nanoparticles in the Presence of Citrate Groups and Bacteria

by Maryam Rad, Gholamhossein Ebrahimipour, Mojgan Bandehpour, Omid Akhavan and Fatemeh Yarian

Catalysts 2022, 12(9), 1048; https://0-doi-org.brum.beds.ac.uk/10.3390/catal12091048 - 14 Sep 2022

Cited by 2 | Viewed by 1512

Abstract

With the spread of deadly diseases worldwide, the design of rapid tests to identify causative microorganisms is necessary. Due to the unique properties of gold nanoparticles, these nanoparticles are used in designing rapid diagnostic tests, such as strip tests. The current study aimed to investigate the ability of gold nanoparticles to bind to single-chain variable fragment antibodies. In this study, the biological and chemical methods included Escherichia coli TOP-10 and the Turkevich method to synthesize the gold nanoparticles, respectively. Then, the effect of synthetic nanoparticles on their capability of binding to recombinant antibodies was assessed by agarose gel and UV-vis spectroscopy. Our result showed that gold nanoparticles had a spherical morphology, and their average size was ~45 nm. Additionally, the citrate groups in gold nanoparticles were able to bind to serine residues in the antibody linker sequence; so, the chemical synthesis of gold nanoparticles is an effective strategy for binding these nanoparticles to antibodies that can be used in designing rapid diagnostic tests to promptly identify infectious microorganisms. Full article

(This article belongs to the Special Issue Advances in Enzyme Engineering, Biocatalysis and Biosynthesis)

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16 pages, 2788 KiB

Open AccessArticle

Effect of Fermentation Response on Biosynthesis of Endopolygalacturonase from a Potent Strain of Bacillus by Utilizing Polymeric Substrates of Agricultural Origin

by Nagina Rafique, Raina Ijaz, Muhammad Zubair Khan, Saima Rafiq, Imran Hayat, Imtiaz Hussain, Khawaja Shafique Ahmad, Romana Tabassum and Zhijian Xie

Catalysts 2022, 12(8), 875; https://0-doi-org.brum.beds.ac.uk/10.3390/catal12080875 - 09 Aug 2022

Cited by 1 | Viewed by 2194

Abstract

Endopolygalacturonase (EndoPGase), EC: 3.2.1.15. is one of the crucial pectinases belonging to the class of carbohydrase. The catalytic action of EndoPGase captivates the attention of the production of this extremely valuable catalyst in the industrial sector. The main focus was to ascertain a potential bacterial candidate for endoPGase production. The isolated bacterial strain was further identified by 16S rRNA gene sequencing. The parameters for enzyme biosynthesis were optimized by a single and multiple factor approach at a time. The results of our investigation led to the identification of a potent strain of Bacillus subtilis NR2 [strain 168]. The sequence of 16S rRNA amplified from the isolated bacterium has been submitted to GenBank under accession number ON738697. The strain was found active for pectic enzyme activity under shaking- flask fermentation at pH 5.0 and 50 °C temperature of incubation. Among all monomeric and polymeric substrates (inducer-substrates), citrus pectin, followed by potato starch and pectin (Sigma) were considered the best enzyme inducers at 1% concentration. In comparison, an increased wheat bran concentration at 5% was proved to be ideal for EndoPGase biosynthesis Moreover, an increasing trend in enzyme activity was observed with the increasing concentration of inducer. The combined effect of three variables (pH, inducer-substrates, and inducer-substrate concentration) was explored by response surface methodology (RSM) involving a Box–Behnken design (BBD). Based on the results, we concluded that the soil-isolated B. subtilis can be effectively utilized for commercial-scale pectinase enzyme biosynthesis. Full article

(This article belongs to the Special Issue Advances in Enzyme Engineering, Biocatalysis and Biosynthesis)

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