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Processes
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Biocatalysis, Enzyme and Process Engineering
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Biocatalysis, Enzyme and Process Engineering

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

Deadline for manuscript submissions: closed (31 December 2020) | Viewed by 22103

Special Issue Editors

Dr. Pedro Fernandes

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Guest Editor
1. Faculty of Engineering, Universidade Lusófona, 1749-024 Lisboa, Portugal
2. iBB – Institute for Bioengineering and Biosciences, Department of Bioengineering, Instituto Superior Técnico, Universidade de Lisboa, 1649-004 Lisboa, Portugal
Interests: biocatalysis; bioreactors; bioprocess engineering
Special Issues, Collections and Topics in MDPI journals
Dr. Carla C. C. R. de Carvalho

E-Mail Website
Guest Editor
iBB – Institute for Bioengineering and Biosciences, Department of Bioengineering, Instituto Superior Técnico, Universidade de Lisboa, Lisbon, Portugal
Interests: bacterial adaptation; marine biotechnology; biocatalysis; bioreactors; bioprocess engineering
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear colleagues,

Enzymes are acknowledged as effective catalysts, namely, on account of their selectivity, high turnover, and ability to operate under mild conditions. Despite these advantageous features, the industrial application of enzymes still lags behind their use on a laboratory scale. This pattern may be partly assigned to the intrinsic nature of enzymes: these biocatalysts have been optimized throughout the ages to be mostly active in aqueous media and to operate in environments where substrate and product concentrations are much lower than those required for industrial processes to be commercially feasible. Hence, high concentrations of substrates or products can be toxic or inhibitory. Moreover, the compounds involved in several of these industrial processes, namely, in the pharmaceutic industry, are often sparingly water-soluble, hence the need to use non-aqueous media, which can pose limitations on several enzymes. Enzyme engineering, often coupled to process engineering, has been shown to provide a sound approach to tackle these issues and improve the catalytic and stability features of several enzymes. In addition, methodologies such as continuous flow, already well-established in chemical processes, have been increasingly used in biocatalysis, given their potential to increase overall bioconversion rates due to increased mass transfer and enhanced throughput of material.

This Special Issue on “Biocatalysis, Enzyme, and Process Engineering” aims to address novel advances in the development and application of enzymes in the production of goods of interest for large-scale production. Topics include but are not limited to the following:

  • Enzyme engineering towards improved biocatalysts;
  • The development of novel process designs for biocatalysis;
  • Multienzyme cascade reactions.

Dr. Pedro Fernandes
Dr. Carla C. C. R. de Carvalho
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
  • bioprocesses
  • cascade reactions
  • continuous flow
  • directed evolution
  • enzyme engineering
  • miniaturization
  • multiphase systems
  • rational design
  • white biotechnology

Published Papers (7 papers)

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Editorial

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4 pages, 201 KiB  
Editorial
Special Issue on “Biocatalysis, Enzyme and Process Engineering”
by Pedro Fernandes and Carla C. C. R. de Carvalho
Processes 2023, 11(3), 740; https://doi.org/10.3390/pr11030740 - 2 Mar 2023
Viewed by 1091
Abstract
Biocatalysis entails the use of enzymes, which are catalytically active proteins, to speed up reactions so that products can be obtained swiftly and accurately [...] Full article
(This article belongs to the Special Issue Biocatalysis, Enzyme and Process Engineering)

Research

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25 pages, 2433 KiB  
Article
Biodegradable Polyester Synthesis in Renewed Aqueous Polycondensation Media: The Core of the New Greener Polymer-5B Technology
by Ana C. D. Pfluck, Dragana P.C. de Barros and Luis P. Fonseca
Processes 2021, 9(2), 365; https://doi.org/10.3390/pr9020365 - 16 Feb 2021
Cited by 6 | Viewed by 2728
Abstract
An innovative enzymatic polycondensation of dicarboxylic acids and dialcohols in aqueous polymerization media using free and immobilized lipases was developed. Various parameters (type of lipases, temperature, pH, stirring type and rate, and monomer carbon chain length) of the polycondensation in an oil-in-water ( [...] Read more.
An innovative enzymatic polycondensation of dicarboxylic acids and dialcohols in aqueous polymerization media using free and immobilized lipases was developed. Various parameters (type of lipases, temperature, pH, stirring type and rate, and monomer carbon chain length) of the polycondensation in an oil-in-water (o/w) miniemulsion (>80% in water) were evaluated. The best results for polycondensation were achieved with an equimolar monomer concentration (0.5 M) of octanedioic acid and 1,8-octanediol in the miniemulsion and water, both at initial pH 5.0 with immobilized Pseudozyma antarctica lipase B (PBLI). The synthesized poly(octamethylene suberate) (POS) in the miniemulsion is characterized by a molecular weight of 7800 g mol−1 and a conversion of 98% at 45 °C after 48 h of polycondensation in batch operation mode. A comparative study of polycondensation using different operation modes (batch and fed-batch), stirring type, and biocatalyst reutilization in the miniemulsion, water, and an organic solvent (cyclohexane:tetrahydrofuran 5:1 v/v) was performed. Regarding the polymer molecular weight and conversion (%), batch operation mode was more appropriate for the synthesis of POS in the miniemulsion and water, and fed-batch operation mode showed better results for polycondensation in the organic solvent. The miniemulsion and water used as polymerization media showed promising potential for enzymatic polycondensation since they presented no enzyme inhibition for high monomer concentrations and excellent POS synthesis reproducibility. The PBLI biocatalyst presented high reutilization capability over seven cycles (conversion > 90%) and high stability equivalent to 72 h at 60 °C on polycondensation in the miniemulsion and water. The benefits of polycondensation in aqueous media using an o/w miniemulsion or water are the origin of the new concept strategy of the green process with a green product that constitutes the core of the new greener polymer-5B technology. Full article
(This article belongs to the Special Issue Biocatalysis, Enzyme and Process Engineering)
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17 pages, 12144 KiB  
Article
Synthesis of Dietetic Structured Lipids from Spent Coffee Grounds Crude Oil Catalyzed by Commercial Immobilized Lipases and Immobilized Rhizopus oryzae Lipase on Biochar and Hybrid Support
by Danyelle A. Mota, Jefferson C. B. Santos, Diana Faria, Álvaro S. Lima, Laiza C. Krause, Cleide M. F. Soares and Suzana Ferreira-Dias
Processes 2020, 8(12), 1542; https://doi.org/10.3390/pr8121542 - 26 Nov 2020
Cited by 13 | Viewed by 2578
Abstract
The aim of this study was the valorization of coffee industry residues, namely spent coffee grounds (SCG) as a source of oil, and silverskin (CS) as a source of both oil and biomass, under the concept of the circular economy. Therefore, crude oil [...] Read more.
The aim of this study was the valorization of coffee industry residues, namely spent coffee grounds (SCG) as a source of oil, and silverskin (CS) as a source of both oil and biomass, under the concept of the circular economy. Therefore, crude oil from SCG was used to produce low-calorie structured lipids (SL) for food and pharmaceutical industries, and CS to produce biochar by pyrolysis for biotechnological uses. SL were obtained by acidolysis with caprylic or capric acid, or interesterification with ethyl caprylate or ethyl caprate, in solvent-free media, catalyzed by immobilized sn-1,3 regioselective lipases. Silverskin biochar (BIO) was directly used as enzyme carrier or to produce hybrid organic-silica (HB) supports for enzyme immobilization. Rhizopus oryzae lipase (ROL) immobilized on Amberlite (AMB), silica (SIL), BIO or HB, and the commercial immobilized Thermomyces lanuginosus (Lipozyme TL IM) and Rhizomucor miehei (Lipozyme RM IM) lipases were tested. Lipozyme RM IM showed better results in SL production than Lipozyme TLIM or ROL on BIO, SIL or HB. About 90% triacylglycerol conversion was attained after 7 h acidolysis or interesterification. Lipozyme RM IM was more stable in interesterification (80% and 65% activity with ethyl caprylate or ethyl caprate) than in acidolysis (first-order decay) after 10 reuses. Full article
(This article belongs to the Special Issue Biocatalysis, Enzyme and Process Engineering)
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Graphical abstract

7 pages, 1043 KiB  
Communication
Rapid and Enhanced Liquefaction of Pulp from Mango (Mangifera indica L.) cv. Totapuri Using Ultrasound-Assisted Enzyme Pretreatment
by Lebaka Veeranjaneya Reddy, Young-Min Kim and Young-Jung Wee
Processes 2020, 8(6), 718; https://doi.org/10.3390/pr8060718 - 20 Jun 2020
Cited by 6 | Viewed by 3622
Abstract
The effect of ultrasound and enzyme pretreatment (with pectinase, amylase, and cellulase) on the physicochemical properties (yield, viscosity, total soluble solids, and total phenolics) of mango juice was evaluated through a set of six experiments. Ultrasonication treatment alone showed no influence on juice [...] Read more.
The effect of ultrasound and enzyme pretreatment (with pectinase, amylase, and cellulase) on the physicochemical properties (yield, viscosity, total soluble solids, and total phenolics) of mango juice was evaluated through a set of six experiments. Ultrasonication treatment alone showed no influence on juice yield (54.6 ± 1.1%). However, the combined uses of ultrasonication with a pectinase or the enzyme mixture significantly increased the yield (94.1 ± 1.4% and 80.0 ± 2.1%, respectively) and decreased the enzyme pretreatment time (from 2 h to 1 h). Pectinase treatment assisted by ultrasonication was more effective with regard to juice yield, viscosity reduction, and the clarity of the juice than the enzyme mixture treatment with ultrasonication. Ultrasonication alone significantly increased the amount of total phenolics (65.5 ± 1.0 mg/100 mL) and showed a slight reduction of viscosity and improvement of clarity compared to the control. Full article
(This article belongs to the Special Issue Biocatalysis, Enzyme and Process Engineering)
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15 pages, 2870 KiB  
Article
Improved Catalytic Properties of Thermomyces lanuginosus Lipase Immobilized onto Newly Fabricated Polydopamine-Functionalized Magnetic Fe3O4 Nanoparticles
by Yanhong Bi, Zhaoyu Wang, Rui Zhang, Yihan Diao, Yaoqi Tian and Zhengyu Jin
Processes 2020, 8(5), 629; https://doi.org/10.3390/pr8050629 - 24 May 2020
Cited by 11 | Viewed by 3087
Abstract
In this study, magnetic Fe3O4 nanoparticles coated with polydopamine possessing abundant amino groups (Fe3O4@PDA) were conveniently prepared, detailed, and characterized, and then firstly used as a supporting matrix for immobilizing Thermomyces lanuginosus lipase (Fe3O [...] Read more.
In this study, magnetic Fe3O4 nanoparticles coated with polydopamine possessing abundant amino groups (Fe3O4@PDA) were conveniently prepared, detailed, and characterized, and then firstly used as a supporting matrix for immobilizing Thermomyces lanuginosus lipase (Fe3O4@PDA@TLL). The effects of some crucial factors on the immobilization efficiency were investigated and the optimal protein loading and activity recovery were found to be 156.4 mg/g and 90.9%, respectively. Characterization studies revealed that Fe3O4@PDA@TLL displayed a broader pH and temperature adaptability as compared to the free TLL, which allows its use at wider ranges of reaction conditions. With regard to the stabilities, the immobilized TLL clearly displayed improved pH, thermal, and solvent tolerance stabilities compared to the free enzyme, suggesting that the biocompatible Fe3O4@PDA might be an outstanding material for immobilizing TLL and acting as alternative support for different enzymes. Full article
(This article belongs to the Special Issue Biocatalysis, Enzyme and Process Engineering)
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14 pages, 979 KiB  
Article
Manufacturing Process, In Vivo and In Vitro Digestibility Assessment of an Enteral Feeding Product Hydrolyzed from Locally Available Ingredients Using Commercial Enzymes
by Nguyen Thi Quynh Hoa, Luu Ngan Tam, Luu Van Thien Phu, Than Van Thai, Duy Chinh Nguyen and Dong Thi Anh Dao
Processes 2019, 7(6), 347; https://doi.org/10.3390/pr7060347 - 6 Jun 2019
Cited by 3 | Viewed by 3749
Abstract
A ready-for-use enteral feeding product was manufactured based on energy standard mixing using hydrolyzed products from local foods (i.e., loin pork, carrot, pumpkin, soybean, rice, and potato). When compared to enteral foods based on defined ingredients, the manufactured product is more cost-effective, appropriately [...] Read more.
A ready-for-use enteral feeding product was manufactured based on energy standard mixing using hydrolyzed products from local foods (i.e., loin pork, carrot, pumpkin, soybean, rice, and potato). When compared to enteral foods based on defined ingredients, the manufactured product is more cost-effective, appropriately functional and has similar physicochemical properties. Relative protein digestibility for in vitro value was tested by using enzyme pepsin, pH-drop and pH-stat method with three different enzymes. The product was shown to be easily digested with an in vivo digestibility value of 89.7%. Molecule sizes of components in the product ranged from 3.5 to 8.5 kDa, determined by SDS-PAGE, and the average molecular weight was 1.52 kDa, determined by Gel Permeation Chromatography (GPC) method. In terms of nutritional value, the product achieved a caloric density of 1 kcal/mL, dietary fibers of 1.48 g per 100 mL and provided both oligomeric and monomeric forms of protein. In addition, the product has the leucine: isoleucine: valine ratio of 2:1:1, thus facilitating the absorption of the protein. In conclusion, the manufactured enteral feeding product has been shown to be appropriate for providing nutritional support for patients. Full article
(This article belongs to the Special Issue Biocatalysis, Enzyme and Process Engineering)
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Review

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26 pages, 6850 KiB  
Review
Multi-Enzyme Systems in Flow Chemistry
by Pedro Fernandes and Carla C. C. R. de Carvalho
Processes 2021, 9(2), 225; https://doi.org/10.3390/pr9020225 - 25 Jan 2021
Cited by 25 | Viewed by 4002
Abstract
Recent years have witnessed a growing interest in the use of biocatalysts in flow reactors. This merging combines the high selectivity and mild operation conditions typical of biocatalysis with enhanced mass transfer and resource efficiency associated to flow chemistry. Additionally, it provides a [...] Read more.
Recent years have witnessed a growing interest in the use of biocatalysts in flow reactors. This merging combines the high selectivity and mild operation conditions typical of biocatalysis with enhanced mass transfer and resource efficiency associated to flow chemistry. Additionally, it provides a sound environment to emulate Nature by mimicking metabolic pathways in living cells and to produce goods through the systematic organization of enzymes towards efficient cascade reactions. Moreover, by enabling the combination of enzymes from different hosts, this approach paves the way for novel pathways. The present review aims to present recent developments within the scope of flow chemistry involving multi-enzymatic cascade reactions. The types of reactors used are briefly addressed. Immobilization methodologies and strategies for the application of the immobilized biocatalysts are presented and discussed. Key aspects related to the use of whole cells in flow chemistry are presented. The combination of chemocatalysis and biocatalysis is also addressed and relevant aspects are highlighted. Challenges faced in the transition from microscale to industrial scale are presented and discussed. Full article
(This article belongs to the Special Issue Biocatalysis, Enzyme and Process Engineering)
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