Bioprocess Engineering: Sustainable Manufacturing for a Green Society

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

Deadline for manuscript submissions: 31 January 2025 | Viewed by 17426

Special Issue Editors


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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

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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,

The current production processes are mostly still linear and are highly demanding in terms of raw materials and energy while also generating significant waste. These features have contributed to the depletion of resources as well as the increase in overall pollution levels and greenhouse gas emissions, to name just the major undisputed drawbacks of the dominant production pattern. There is growing public awareness that persistence of this very trend would be unsustainable in the medium—if not, short—term and would seriously compromise future generations’ expectations of a good quality of life, and this has served as a major driver for the quest toward sustainable and cost-effective production processes. The mild operational conditions typically required by biobased production processes, together with the selective nature of biocatalysts, microbial diversity and tunability, and the century-long record of fermentation, clearly place bioprocesses as the primary contenders, by far, in achieving the generalized implementation of efficient, green manufacturing strategies. Moreover, by overlapping with the biorefinery approach, the foundations needed for bioprocesses to embrace the circular economy concept are set. Hence, bioprocesses can also become sustainable and more environmentally friendly.

This Special Issue aims to provide insight into the move toward bioproducts and concomitant bioengineering approaches in achieving a sustainable and environmentally friendly economy, the obstacles that were met and overcome throughout this path, and to critically evaluate the challenges that still remain. Accordingly, it will foster contributions addressing the biobased production of building blocks/final products including chemicals, flavors, foods, fuels, nutraceuticals, or pharmaceuticals, preferably favoring the use of cheap, plentiful, and/or easily renewable raw materials. The scope of the Special Issue is intended to be of interest for those already involved in the field as well as highly appealing for those readers aiming for an overview of existing knowledge within the framework of sustainable production processes and on foreseeable prospective developments.

Dr. Pedro Fernandes
Dr. Carla C. C. R. de Carvalho
Guest Editors

Manuscript Submission Information

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Published Papers (4 papers)

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Research

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18 pages, 2229 KiB  
Article
Thermal Stabilization of Lipases Bound to Solid-Phase Triazine-Scaffolded Biomimetic Ligands: A Preliminary Assessment
by Diogo Ferreira-Faria and M. Ângela Taipa
Processes 2024, 12(2), 371; https://doi.org/10.3390/pr12020371 - 11 Feb 2024
Viewed by 978
Abstract
Biomimetic ligands are synthetic compounds that mimic the structure and binding properties of natural biological ligands. The first uses of textile dyes as pseudo-affinity ligands paved the way for the rational design and de novo synthesis of low-cost, non-toxic and highly stable [...] Read more.
Biomimetic ligands are synthetic compounds that mimic the structure and binding properties of natural biological ligands. The first uses of textile dyes as pseudo-affinity ligands paved the way for the rational design and de novo synthesis of low-cost, non-toxic and highly stable triazine-scaffolded affinity ligands. A novel method to assess and enhance protein stability, employing triazine-based biomimetic ligands and using cutinase from Fusarium solani pisi as a protein model, has been previously reported. This innovative approach combined the concepts of molecular modeling and solid-phase combinatorial chemistry to design, synthesize and screen biomimetic compounds able to bind cutinase through complementary affinity-like interactions while maintaining its biological functionality. The screening of a 36-member biased combinatorial library enabled the identification of promising lead ligands. The immobilization/adsorption of cutinase onto a particular lead (ligand 3′/11) led to a noteworthy enhancement in thermal stability within the temperature range of 60–80 °C. In the present study, similar triazine-based compounds, sourced from the same combinatorial library and mimicking dipeptides of diverse amino acids, were selected and studied to determine their effectiveness in binding and/or improving the thermal stability of several lipases, enzymes which are closely related in function to cutinases. Three ligands with different compositions were screened for their potential thermostabilizing effect on different lipolytic enzymes at 60 °C. An entirely distinct enzyme, invertase from Saccharomyces cerevisiae, was also assessed for binding to the same ligands and functioned as a ‘control’ for the experiments with lipases. The high binding yield of ligand 3′/11 [4-({4-chloro-6-[(2-methylbutyl)amino]-1,3,5-triazin-2-yl}amino)benzoic acid] to cutinase was confirmed, and the same ligand was tested for its ability to bind lipases from Aspergillus oryzae (AOL), Candida rugosa (CRL), Chromobacterium viscosum (CVL), Rhizomucor miehei (RML) and Rhizopus niveus (RNL). The enzymes CRL, CVL, RNL and invertase showed significant adsorption yields to ligand 3′/11—32, 29, 36 and 94%, respectively, and the thermal stability at 60 °C of free and adsorbed enzymes was studied. CVL and RNL were also stabilized by adsorption to ligand 3′/11. In the case of CRL and invertase, which bound but were not stabilized by ligand (3′/11), other ligands from the original combinatorial library were tested. Between the two alternative ligands, one was effective at stabilizing C. rugosa lipase, while none stabilized invertase. Full article
(This article belongs to the Special Issue Bioprocess Engineering: Sustainable Manufacturing for a Green Society)
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16 pages, 3194 KiB  
Article
Quality Monitoring of Biodiesel and Diesel/Biodiesel Blends: A Comparison between Benchtop FT-NIR versus a Portable Miniaturized NIR Spectroscopic Analysis
by Luísa L. Monteiro, Paulo Zoio, Bernardo B. Carvalho, Luís P. Fonseca and Cecília R. C. Calado
Processes 2023, 11(4), 1071; https://doi.org/10.3390/pr11041071 - 3 Apr 2023
Cited by 1 | Viewed by 1806
Abstract
A methodology such as near-infrared (NIR) spectroscopy, which enables in situ and in real-time analysis, is crucial to perform quality control of biodiesel, since it is blended into diesel fuel and the presence of contaminants can hinder its performance. This work aimed to [...] Read more.
A methodology such as near-infrared (NIR) spectroscopy, which enables in situ and in real-time analysis, is crucial to perform quality control of biodiesel, since it is blended into diesel fuel and the presence of contaminants can hinder its performance. This work aimed to compare the performance of a benchtop Fourier Transform (FT) NIR spectrometer with a prototype of a portable, miniaturized near-infrared spectrometer (miniNIR) to detect and quantify contaminants in biodiesel and biodiesel in diesel. In general, good models based on principal component analysis-linear discriminant analysis (PCA-LDA) of FT-NIR spectra were obtained, predicting with high accuracies biodiesel contaminants and biodiesel in diesel (between 75% to 95%), as well as good partial least square (PLS) regression models to predict contaminants concentration in biodiesel and biodiesel concentration in diesel/biodiesel blends, with high coefficients of determination (between 0.83 and 0.99) and low prediction errors. The miniNIR prototype’s PCA-LDA models enabled the prediction of target contaminants with good accuracies (between 66% and 86%), and a PLS model enabled the prediction of biodiesel concentration in diesel with a reasonable coefficient of determination (0.68), pointing to the device’s potential for preliminary analysis of biodiesel which, associated with its potential low cost and portability, could increase biodiesel quality control. Full article
(This article belongs to the Special Issue Bioprocess Engineering: Sustainable Manufacturing for a Green Society)
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11 pages, 12652 KiB  
Article
Isolation and Molecular Identification of Xylanase-Producing Bacteria from Ulva flexuosa of the Persian Gulf
by Adnan Pasalari and Ahmad Homaei
Processes 2022, 10(9), 1834; https://doi.org/10.3390/pr10091834 - 12 Sep 2022
Cited by 7 | Viewed by 1857
Abstract
The marine ecosystem is one of the richest sources of biologically active compounds, such as enzymes, among which seaweed is one of the most diverse marine species and has a rich diversity of bacteria that produce different enzymes. Among these, the bacteria-derived xylanase [...] Read more.
The marine ecosystem is one of the richest sources of biologically active compounds, such as enzymes, among which seaweed is one of the most diverse marine species and has a rich diversity of bacteria that produce different enzymes. Among these, the bacteria-derived xylanase enzyme has many applications in the fruit juice, paper, and baking industries; so, to consider the economic value of the xylanase enzyme and the isolation and identification of xylanase-producing bacteria is of particular importance. In this study, specimens of the alga Ulva flexuosa species were collected from the coasts of Bandar Abbas and Qeshm Island. The bacteria coexisting with the algae were isolated using a nutrient agar medium. The bacteria producing the xylanase enzyme were then screened by a specific solid culture medium containing xylan, and the activity of the xylanase enzyme isolated from the bacteria was measured using a xylan substrate. The bacteria with the highest enzymatic activity were selected and identified by 16S rRNA gene sequence analysis, and the culture medium conditions for the enzyme production by the selected bacterial strains were optimized. Among the bacterial community, two strains with the highest xylanase activity, which belonged to the genera Bacillus and Shewanella, were identified as Bacillus subtilis strain HR05 and Shewanella algae strain HR06, respectively. The two selected bacteria were registered in the NCBI gene database. The results demonstrated that the two selected strains had different optimal growing conditions in terms of pH and temperature, as well as the sources of carbon and nitrogen for enzyme production. It seems that the xylanase enzyme isolated from the bacterial strains HR05 and HR06, which coexist with alga Ulva flexousa, could be potential candidates for biotechnology and various industries, such as pulp production, paper, and food manufacture, due to their high activity and optimal alkaline pH. Full article
(This article belongs to the Special Issue Bioprocess Engineering: Sustainable Manufacturing for a Green Society)
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Review

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31 pages, 1195 KiB  
Review
Enzyme Immobilization and Co-Immobilization: Main Framework, Advances and Some Applications
by Joaquim Bié, Bruno Sepodes, Pedro C. B. Fernandes and Maria H. L. Ribeiro
Processes 2022, 10(3), 494; https://doi.org/10.3390/pr10030494 - 1 Mar 2022
Cited by 57 | Viewed by 11572
Abstract
Enzymes are outstanding (bio)catalysts, not solely on account of their ability to increase reaction rates by up to several orders of magnitude but also for the high degree of substrate specificity, regiospecificity and stereospecificity. The use and development of enzymes as robust biocatalysts [...] Read more.
Enzymes are outstanding (bio)catalysts, not solely on account of their ability to increase reaction rates by up to several orders of magnitude but also for the high degree of substrate specificity, regiospecificity and stereospecificity. The use and development of enzymes as robust biocatalysts is one of the main challenges in biotechnology. However, despite the high specificities and turnover of enzymes, there are also drawbacks. At the industrial level, these drawbacks are typically overcome by resorting to immobilized enzymes to enhance stability. Immobilization of biocatalysts allows their reuse, increases stability, facilitates process control, eases product recovery, and enhances product yield and quality. This is especially important for expensive enzymes, for those obtained in low fermentation yield and with relatively low activity. This review provides an integrated perspective on (multi)enzyme immobilization that abridges a critical evaluation of immobilization methods and carriers, biocatalyst metrics, impact of key carrier features on biocatalyst performance, trends towards miniaturization and detailed illustrative examples that are representative of biocatalytic applications promoting sustainability. Full article
(This article belongs to the Special Issue Bioprocess Engineering: Sustainable Manufacturing for a Green Society)
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