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Journals
Processes
Special Issues
Application of Enzymes in Sustainable Biocatalysis
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Application of Enzymes in Sustainable Biocatalysis

A special issue of Processes (ISSN 2227-9717). This special issue belongs to the section "Biological Processes and Systems".

Deadline for manuscript submissions: 10 December 2025 | Viewed by 3653

Special Issue Editors

Dr. Carminna Ottone

E-Mail Website
Guest Editor
School of Biochemistry Engineering, Pontifical Catholic University of Valparaiso, Valparaiso 2340025, Chile
Interests: bioengineering; materials science; electrochemistry; nanomaterials; enzyme; biocatalysis; environmental chemistry
Prof. Dr. Lorena Wilson

E-Mail Website
Guest Editor
School of Biochemistry Engineering, Pontifical Catholic University of Valparaiso, 2340025 Valparaiso, Chile
Interests: wine; biochemical engineering; biotechnology; enzyme engineering; advanced bioreactors, enzymatic biocatalysis; industrial application
Dr. Paulina Urrutia

E-Mail Website
Guest Editor
School of Biochemistry Engineering, Pontifical Catholic University of Valparaiso, 2340025 Valparaiso, Chile
Interests: biocatalysis; enzymes; biological processes; biochemical engineering

Special Issue Information

Dear Colleagues,

Enzyme-catalyzed reactions offer a wide range of solutions for sustainable processes because they require mild operating conditions when compared to their chemical counterparts. In addition, protein engineering and directed evolution technologies permit the modification of the properties of native enzymes by directing their qualities toward the requirements of the applications of interest. The selectivity offered by enzymes and their great variety together with the advances related to enzyme immobilization make them interesting candidates to replace operations that currently require several purification steps. It should be noted that, in recent years, enzymes have been successfully coupled to other systems, such as electrochemical and photochemical systems, which confirms that the processes catalyzed by enzymes are highly adaptable to new industry requirements.

This Special Issue on “Application of Enzymes in Sustainable Biocatalysis” will address aspects spanning from the production of these catalysts to their applications in technological purposes. Many different industries will benefit from this, but the most relevant industries are biopharma, food production, biofuels, and bioremediation industries.

Topics of the Special Issue include, but are not limited to, the following:

  • Enzyme production;
  • Enzyme immobilization strategies;
  • Enzyme assisted extraction methods;
  • Photobiocatalysis;
  • Enzymatic CO2 conversion;
  • Enzymatic biotransformations.

Dr. Carminna Ottone
Prof. Dr. Lorena Wilson
Dr. Paulina Urrutia
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. Processes 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 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

  • biocatalysis
  • immobilisation strategies
  • biorefinery
  • bioactive compounds
  • food waste valorization
  • climate change
  • biotechnology
  • bioenergy

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Further information on MDPI's Special Issue policies can be found here.

Published Papers (3 papers)

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Research

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16 pages, 1662 KiB  
Article
Immobilisation of Sucrase A from Bacillus subtilis on the Surface of Escherichia coli Mediated by the AIDA-I Autotransporter: Application on the Homolactic Fermentation
by Jorge Sánchez-Andrade, Victor E. Balderas-Hernández, Ana P. Barba de la Rosa and Antonio De Leon-Rodriguez
Processes 2025, 13(2), 470; https://doi.org/10.3390/pr13020470 - 8 Feb 2025
Viewed by 629
Abstract
This study aimed to immobilise sucrase A (SacA) from Bacillus subtilis in E. coli using the AIDA-I system for the whole-cell biocatalysis to transform sucrose to lactate. The pAIDA-sacA plasmid, containing the sacA gene, was fused to the signal peptide of the [...] Read more.
This study aimed to immobilise sucrase A (SacA) from Bacillus subtilis in E. coli using the AIDA-I system for the whole-cell biocatalysis to transform sucrose to lactate. The pAIDA-sacA plasmid, containing the sacA gene, was fused to the signal peptide of the toxin subunit B from Vibrio cholerae (ctxB) and the autotransporter of the aida gene, encoding a connector peptide and the β-barrel domain of the AIDA-I system. This plasmid was employed to transform E. coli strains W3110, WDHFAK, and WDHFAP, which are unable to naturally use sucrose. These strains were anaerobically cultured in batch fermentations using 10 g L−1 sucrose as the sole carbon source. All strains successfully hydrolysed and fermented sucrose, exhibiting a homolactic profile. Among them, WDHFAP/pAIDA-sacA achieved the highest lactic acid titre of 9.84 ± 0.15 g L−1 and a yield of 0.89 ± 0.02 g g−1. Deletion of the mgsA gene in WDHFAP/pAIDA-sacA confirmed that lactic acid production occurred via the methylglyoxal bypass pathway, as lactic acid titres were reduced by over 80%, while ethanol production increased to 4.27 ± 0.26 g L−1. Adaptive laboratory evolution of WDHFAK/pAIDA-sacA was conducted to improve its capacity and fermentation efficiency under elevated sucrose concentrations. The resultant strain, designated as WDHFAKEV/pAIDA-sacA, consumed up to 65 g L−1 sucrose, achieving 64.61 ± 1.65 g L−1 lactic acid with a yield of 0.99 ± 0.03 g g−1. These findings underscore AIDA-I-mediated SacA immobilisation as a robust strategy for whole-cell biocatalysis, enabling E. coli strains to efficiently ferment sucrose. Full article
(This article belongs to the Special Issue Application of Enzymes in Sustainable Biocatalysis)
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13 pages, 2606 KiB  
Article
Catalytic Potential-Guided Design of Multi-Enzymatic System for DHA Production from Glycerol
by Carolina Fernández-Pizarro, Lorena Wilson and Oscar Romero
Processes 2024, 12(9), 2014; https://doi.org/10.3390/pr12092014 - 19 Sep 2024
Viewed by 1070
Abstract
The growing demand for sustainable chemical production has spurred significant interest in biocatalysis. This study is framed within the biocatalytic production of 1,3-dihydroxyacetone (DHA) from glycerol, a byproduct of biodiesel manufacturing. The main goal of this study is to address the challenge of [...] Read more.
The growing demand for sustainable chemical production has spurred significant interest in biocatalysis. This study is framed within the biocatalytic production of 1,3-dihydroxyacetone (DHA) from glycerol, a byproduct of biodiesel manufacturing. The main goal of this study is to address the challenge of identifying the optimal operating conditions. To achieve this, catalytic potential, a lumped parameter that considers both the activity and stability of immobilized biocatalysts, was used to guide the design of a multi-enzymatic system. The multi-enzymatic system comprises glycerol dehydrogenase (GlyDH) and NADH oxidase (NOX). The enzymatic oxidation of glycerol to DHA catalyzed by GlyDH requires the cofactor NAD+. The integration of NOX into a one-pot reactor allows for the in situ regeneration of NAD+, enhancing the overall efficiency of the process. Furthermore, immobilization on Ni+2 agarose chelated supports, combined with post-immobilization modifications (glutaraldehyde crosslinking for GlyDH), significantly improved the stability and activity of both enzymes. The catalytic potential enabled the identification of the optimal operating conditions, which were 30 °C and pH 7.5, favoring NOX stability. This work establishes a framework for the rational design and optimization of multi-enzymatic systems. It highlights the crucial interplay between individual enzyme properties and process conditions to achieve efficient and sustainable biocatalytic transformations. Full article
(This article belongs to the Special Issue Application of Enzymes in Sustainable Biocatalysis)
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Review

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27 pages, 2689 KiB  
Review
Novel Approach of Tackling Wax Deposition Problems in Pipeline Using Enzymatic Degradation Process: Challenges and Potential Solutions
by Shazleen Saadon, Raja Noor Zaliha Raja Abd Rahman, Nor Hafizah Ahmad Kamarudin, Sara Shahruddin, Siti Rohaida Mohd Shafian, Norhidayah Ahmad Wazir and Mohd Shukuri Mohamad Ali
Processes 2024, 12(10), 2074; https://doi.org/10.3390/pr12102074 - 25 Sep 2024
Cited by 2 | Viewed by 1471
Abstract
Anthropogenic activities have led to hydrocarbon spills, and while traditional bioremediation methods are costly and time-consuming, recent research has focused on engineered enzymes for managing pollutant. The potential of enzymes for resolving wax flow problems in the petroleum industry remains unexplored. This paper [...] Read more.
Anthropogenic activities have led to hydrocarbon spills, and while traditional bioremediation methods are costly and time-consuming, recent research has focused on engineered enzymes for managing pollutant. The potential of enzymes for resolving wax flow problems in the petroleum industry remains unexplored. This paper offers a comprehensive review of the current state of research activities related to the bioremediation of petroleum-polluted sites and the biodegradation of specific petroleum hydrocarbons. The assayed enzymes that took part in the degradation were discussed in detail. Lipase, laccase, alkane hydroxylase, alcohol dehydrogenase, esterase, AlkB homologs and cytochrome P450 monooxygenase are among the enzymes responsible for the degradation of more than 50% of the hydrocarbons in contaminated soil and wastewater and found to be active on carbon C8 to C40. The possible biodegradation mechanism of petroleum hydrocarbons was also elucidated. The enzymes’ primary metabolic pathways include terminal, subterminal, and ω-oxidation. Next, given the successful evidence of the hydrocarbon treatment efficiency, the authors analyzed the opportunity for the enzymatic degradation approach if it were to be applied to a different scenario: managing wax deposition in petroleum-production lines. With properties such as high transformation efficiency and high specificity, enzymes can be utilized for the treatment of viscous heavy oil for transportability, evidenced by the 20 to 99% removal of hydrocarbons. The challenges associated with the new approach are also discussed. The production cost of enzymes, the characteristics of hydrocarbons and the operating conditions of the production line may affect the biocatalysis reaction to some extent. However, the challenges can be overcome by the usage of extremophilic enzymes. The combination of technological advancement and deployment strategies such as the immobilization of a consortium of highly thermophilic and halotolerant enzymes is suggested. Recovering and reusing enzymes offers an excellent strategy to improve the economics of the technology. This paper provides insights into the opportunity for the enzymatic degradation approach to be expanded for wax deposition problems in pipelines. Full article
(This article belongs to the Special Issue Application of Enzymes in Sustainable Biocatalysis)
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