Current State-of-the-Art of Biocatalysts

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

Deadline for manuscript submissions: closed (30 November 2022) | Viewed by 4883

Special Issue Editors

University of Agricultural Sciences and Veterinary Medicine Cluj-Napoca64 Calea Floresti street, Cluj-Napoca, Romania
Interests: bioactive compounds; functional foods; edible mushrooms; food safety; green extraction technologies, food preservation; biotechnology; meat science
Special Issues, Collections and Topics in MDPI journals
Faculty of Food Science, University of Agricultural Sciences and Veterinary Medicine Cluj-Napoca, Mănăştur 3-5, 400372 Cluj-Napoca, Romania
Interests: food science; waste exploitation, extraction, and analysis of bioactive compounds; development of new functional products
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

On the quest to a more sustainable society, it is important to replace energy-intensive and environmentally harmful reactions from the thermochemical industry with alternative processes.

Biocatalysis is essential to life and could play an important role in the further improvement of our lives by addressing some of the new challenges that human society is facing. Compared to conventional methods, biocatalysis has advantages such as high stereo-, regio-, and chemoselectivity, efficient catalysis, complex and straightforward transformations, a low rate of byproduct formation, inexpensive refining and purification (uncomplicated), and mild reaction conditions. All of these peculiarities emphasize the potential of biocatalysis as an important tool to accomplish environmentally friendly and sustainable synthesis, reducing the time, cost, waste, and energy consumption of the overall process.

To promote the deployment of biocatalysts in industrial-level applications, we invite submissions of innovative research addressing the "Current State-of-the-Art of Biocatalysts".

 Subject areas covered in this Special Issue include, but are not limited to:

-       Biocatalyst utilization and applications in the food industry;

-       New trends in pharmaceutical biocatalysis;

-       Advances in industrial biocatalyst applications;

-       Waste-based biocatalysts;

-       Biocatalytic microbial conversion;

-       Biocatalytic synthesis of bioactive compounds.

Dr. Melinda Fogarasi
Dr. Anca Farcas
Dr. Oana L. Pop
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

  • Food preservation
  • Byproducts biocatalysts
  • Enzyme catalysis
  • Biocatalytic microbial conversion
  • Biocatalytic synthesis of bioactive compounds
  • Industrial biocatalyst applications

Published Papers (3 papers)

Order results
Result details
Select all
Export citation of selected articles as:

Research

11 pages, 1425 KiB  
Article
One-Pot Synthesis of β-Alanine from Maleic Acid via Three-Enzyme Cascade Biotransformation
Catalysts 2023, 13(2), 267; https://doi.org/10.3390/catal13020267 - 24 Jan 2023
Cited by 2 | Viewed by 1225
Abstract
A novel and efficient one-pot three-enzyme cascade method for the synthesis of β-alanine from maleic acid was developed. Two recombinant E. coli strains were constructed. The E. coli (MaiA-AspA) co-expressing maleic cis-trans isomerase (MaiA) and L-aspartase (AspA) catalyzed the biotransformation of maleic [...] Read more.
A novel and efficient one-pot three-enzyme cascade method for the synthesis of β-alanine from maleic acid was developed. Two recombinant E. coli strains were constructed. The E. coli (MaiA-AspA) co-expressing maleic cis-trans isomerase (MaiA) and L-aspartase (AspA) catalyzed the biotransformation of maleic acid to L-aspartate via fumaric acid, and E. coli (ADC) expressing L-aspartate-α-decarboxylase (ADC) catalyzed the bioconversion of L-aspartate to β-alanine. After systematic optimization of reaction conditions for each strain, the whole cells of two strains were combined for one-pot synthesis of β-alanine. It was found that the ratio of the two kinds of cells as well as the cell amount play critical roles in the reaction rate and yield of β-alanine. Adding two kinds of cells in one-pot at the beginning of the reaction was better than adding step by step. Under optimal conditions, the concentration of β-alanine reached 751 mM after a 9 h reaction, corresponding to a 93.9% yield and 178 g/L/d space-time yield. The developed new route showed application potential for green and efficient biosynthesis of β-alanine from a cheap substrate by tandem biocatalysts. Full article
(This article belongs to the Special Issue Current State-of-the-Art of Biocatalysts)
Show Figures

Figure 1

16 pages, 2077 KiB  
Article
Kinetic Study and Modeling of Wild-Type and Recombinant Broccoli Myrosinase Produced in E. coli and S. cerevisiae as a Function of Substrate Concentration, Temperature, and pH
Catalysts 2022, 12(7), 683; https://doi.org/10.3390/catal12070683 - 22 Jun 2022
Cited by 2 | Viewed by 1377
Abstract
The myrosinase enzyme hydrolyzes glucosinolates, among which is glucoraphanin, the precursor of the anticancer isothiocyanate sulforaphane (SFN). The main source of glucoraphanin is Brassicaceae; however, its natural concentration is relatively low, limiting the availability of SFN. An option to obtain SFN is [...] Read more.
The myrosinase enzyme hydrolyzes glucosinolates, among which is glucoraphanin, the precursor of the anticancer isothiocyanate sulforaphane (SFN). The main source of glucoraphanin is Brassicaceae; however, its natural concentration is relatively low, limiting the availability of SFN. An option to obtain SFN is its exogenous production, through enzymatic processes and under controlled conditions, allowing complete conversion of glucoraphanin to SFN. We characterized the kinetics of wild-type (BMYR) and recombinant broccoli myrosinases produced in E. coli (EMYR) and S. cerevisiae (SMYR) in terms of the reaction conditions. Kinetics was adjusted using empirical and mechanistic models that describe reaction rate as a function of substrate concentration, temperature, and pH, resulting in R2 values higher than 90%. EMYR kinetics differed significantly from those of BMYR and SMYR probably due to the absence of glycosylations in the enzyme produced in E. coli. BMYR and SMYR were subjected to substrate inhibition but followed different kinetic mechanisms attributed to different glycosylation patterns. EMYR (inactivation Ea = 76.1 kJ/mol) was more thermolabile than BMYR and SMYR. BMYR showed the highest thermostability (inactivation Ea = 52.8 kJ/mol). BMYR and EMYR showed similar behavior regarding pH, with similar pK1 (3.4 and 3.1, respectively) and pK2 (5.4 and 5.0, respectively), but differed considerably from SMYR. Full article
(This article belongs to the Special Issue Current State-of-the-Art of Biocatalysts)
Show Figures

Graphical abstract

14 pages, 3262 KiB  
Article
Engineering the Activity of Old Yellow Enzyme NemR-PS for Efficient Reduction of (E/Z)-Citral to (S)-Citronellol
Catalysts 2022, 12(6), 631; https://doi.org/10.3390/catal12060631 - 09 Jun 2022
Cited by 2 | Viewed by 1701
Abstract
The cascade catalysis of old yellow enzyme, alcohol dehydrogenase and glucose dehydrogenase has become a promising approach for one pot, two-step reduction of (E/Z)-citral to (S)-citronellol, serving as a chiral alcohol with rose fragrance. During the multi-enzymatic [...] Read more.
The cascade catalysis of old yellow enzyme, alcohol dehydrogenase and glucose dehydrogenase has become a promising approach for one pot, two-step reduction of (E/Z)-citral to (S)-citronellol, serving as a chiral alcohol with rose fragrance. During the multi-enzymatic cascade catalysis, old yellow enzyme is responsible for the reduction of the conjugated C=C and the introduction of the chiral center, requiring high activity and (S)-enantioselectiviy. Herein, to improve the activity of the old yellow enzyme from Providencia stuartii (NemR-PS) with strict (S)-enantioselectivity, the semi-rational design on its substrate binding pocket was performed through a combination of homology modeling, molecular docking analysis, alanine scanning and iterative saturation mutagenesis. The NemR-PS variant D275G/F351A with improved activity was obtained and then purified for characterization, obeying the substrate inhibition kinetics. Compared with the wild type, the parameters Ki and Kcat/Km were increased from 39.79 mM and 2.09 s−1mM−1 to 128.50 mM and 5.01 s−1mM−1, respectively. Moreover, the variant D275G/F351A maintained strict (S)-enantioselectivity, avoiding the trade-off effect between activity and enantioselectivity. Either the enzyme NemR-PS or the variant D275G/F351A was co-expressed with alcohol dehydrogenase from Yokenella sp. WZY002 (YsADH) and glucose dehydrogenase from Bacillus megaterium (BmGDHM6). In contrast to the whole-cell biocatalyst co-expressing NemR-PS, that co-expressing the variant D275G/F351A shortened the reaction time from 36 h to 12 h in the reduction of 400 mM (E/Z)-citral. In the manner of substrate constant feeding, the accumulated product concentration reached up to 500 mM and completely eliminate the residual intermediate and by-product, suggesting the effectiveness of protein engineering and substrate engineering to improve catalytic efficiency. Full article
(This article belongs to the Special Issue Current State-of-the-Art of Biocatalysts)
Show Figures

Figure 1

Back to TopTop