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Biocatalysis, a Life Companion for Green Chemistry: Biomolecular Aspects of Bioprocesses 2.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Microbiology".

Deadline for manuscript submissions: closed (28 February 2022) | Viewed by 11157

Special Issue Editor

Istituto di Chimica Biomolecolare, Consiglio Nazionale delle Ricerche, Comprensorio Olivetti, Edificio 70, Via Campi Flegrei 34, I-80078 Pozzuoli, Napoli, Italy
Interests: biocatalysis; marine enzymes; marine glycosidases; marine biotechnology; oligosaccharides
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

In a historical perspective for food and drink production, biocatalysis has roots that are lost in the mists of time in Western Asiatic regions and probably in other parts of the ancient world; modern usage goes in accord with the knowledge of protein structure, enzymatic kinetics, and reactor design coming throughout chemistry, and biochemistry successes in the last century up to all insights in current molecular research.

In modern literature, the asset of biocatalysis is of great value in a biobased economy for the valorization of easily accessible starting materials from renewables (agricultural residues, food wastes, marine residues, macro and microalgae, etc). The aim is to replace, in the near future, oil-based chemistry to obtain high-value products as well as functional molecules of biotechnological interest, low-cost production of biocatalysts, detoxification and nutritional enrichment in animal feed production or for other chemical conversions for energy and chemical production. As this represents the interface of green chemistry and industrial biotechnology, it embraces a range of industrial fields with many potential contributions from academic and industry scholars in the need of environmental preservation and improvement of occupational health. However, although enzymatic catalysis at a laboratory scale can be efficiently optimized from the perspective of green chemistry, often limitations are present in terms of economic potential. The inherent multidisciplinary perspective of this journal represents the right place for the hosting of this Special Issue, with the multifaceted audience covering all modern aspects of molecular research.

In this Special Issue, articles or reviews will discuss more recent successes in the investigations of biocatalytic processes used in green chemistry covering all fields of applications and fitting into most of the sections of this journal. All novel advances of biocatalytic approach used to reduce the environmental impact are welcome. Sources of enzymes, biochemistry basis, molecular mechanisms, bioreactors, biobased green pretreatments, enzymatic engineering and molecular biology tools, and study of all applicative aspects of biocatalysis will be acknowledged, including quantitative assessment of bioprocesses.

Dr. Antonio Trincone
Guest Editor

Manuscript Submission Information

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Keywords

  • biocatalysis
  • green chemistry
  • biomasses biorefinery
  • enzyme engineering
  • industrial enzymes

Related Special Issue

Published Papers (3 papers)

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Research

12 pages, 1843 KiB  
Article
In Vitro One-Pot 3-Hydroxypropanal Production from Cheap C1 and C2 Compounds
by Su-Bin Ju, Min-Ju Seo and Soo-Jin Yeom
Int. J. Mol. Sci. 2022, 23(7), 3990; https://doi.org/10.3390/ijms23073990 - 03 Apr 2022
Cited by 2 | Viewed by 2268
Abstract
One- or two-carbon (C1 or C2) compounds have been considered attractive substrates because they are inexpensive and abundant. Methanol and ethanol are representative C1 and C2 compounds, which can be used as bio-renewable platform feedstocks for the biotechnological production of value-added natural chemicals. [...] Read more.
One- or two-carbon (C1 or C2) compounds have been considered attractive substrates because they are inexpensive and abundant. Methanol and ethanol are representative C1 and C2 compounds, which can be used as bio-renewable platform feedstocks for the biotechnological production of value-added natural chemicals. Methanol-derived formaldehyde and ethanol-derived acetaldehyde can be converted to 3-hydroxypropanal (3-HPA) via aldol condensation. 3-HPA is used in food preservation and as a precursor for 3-hydroxypropionic acid and 1,3-propanediol that are starting materials for manufacturing biocompatible plastic and polytrimethylene terephthalate. In this study, 3-HPA was biosynthesized from formaldehyde and acetaldehyde using deoxyribose-5-phosphate aldolase from Thermotoga maritima (DERATma) and cloned and expressed in Escherichia coli for 3-HPA production. Under optimum conditions, DERATma produced 7 mM 3-HPA from 25 mM substrate (formaldehyde and acetaldehyde) for 60 min with 520 mg/L/h productivity. To demonstrate the one-pot 3-HPA production from methanol and ethanol, we used methanol dehydrogenase from Lysinibacillus xylanilyticus (MDHLx) and DERATma. One-pot 3-HPA production via aldol condensation of formaldehyde and acetaldehyde from methanol and ethanol, respectively, was investigated under optimized reaction conditions. This is the first report on 3-HPA production from inexpensive alcohol substrates (methanol and ethanol) by cascade reaction using DERATma and MDHLx. Full article
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15 pages, 1687 KiB  
Article
Xylitol as a Hydrophilization Moiety for a Biocatalytically Synthesized Ibuprofen Prodrug
by Federico Zappaterra, Chiara Tupini, Daniela Summa, Virginia Cristofori, Stefania Costa, Claudio Trapella, Ilaria Lampronti and Elena Tamburini
Int. J. Mol. Sci. 2022, 23(4), 2026; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23042026 - 11 Feb 2022
Cited by 6 | Viewed by 1870
Abstract
Biocatalyzed synthesis can be exploited to produce high-value products, such as prodrugs. The replacement of chemical approaches with biocatalytic processes is advantageous in terms of environmental prevention, embracing the principles of green chemistry. In this work, we propose the covalent attachment of xylitol [...] Read more.
Biocatalyzed synthesis can be exploited to produce high-value products, such as prodrugs. The replacement of chemical approaches with biocatalytic processes is advantageous in terms of environmental prevention, embracing the principles of green chemistry. In this work, we propose the covalent attachment of xylitol to ibuprofen to produce an IBU-xylitol ester prodrug. Xylitol was chosen as a hydrophilizer for the final prodrug, enhancing the water solubility of ibuprofen. Ibuprofen is a nonsteroidal anti-inflammatory drug (NSAID) extensively used as an analgesic, anti-inflammatory, and antipyretic. Despite being the third-most-prescribed medicine in the world, the aqueous solubility of ibuprofen is just 21 mg/L. This poor water solubility greatly limits the bioavailability of ibuprofen. We aimed to functionalize ibuprofen with xylitol using the reusable immobilized N435 biocatalyst. Instead of a biphasic media, we proposed a monophasic reaction environment. The characterization of the IBU-xylitol ester was performed by 1H, 13C-NMR, DEPT, COSY, HMQC, HMBC, FTIR, and MS spectroscopy. Preliminary in vitro tests showed that this enzymatically synthesized prodrug of ibuprofen reduced the expression of the interleukin 8 genes in human bronchial epithelial cells (IB3-1) from cystic fibrosis (CF) patients. Full article
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15 pages, 2096 KiB  
Article
An Efficient Protein Evolution Workflow for the Improvement of Bacterial PET Hydrolyzing Enzymes
by Valentina Pirillo, Marco Orlando, Davide Tessaro, Loredano Pollegioni and Gianluca Molla
Int. J. Mol. Sci. 2022, 23(1), 264; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23010264 - 27 Dec 2021
Cited by 13 | Viewed by 6426
Abstract
Enzymatic degradation is a promising green approach to bioremediation and recycling of the polymer poly(ethylene terephthalate) (PET). In the past few years, several PET-hydrolysing enzymes (PHEs) have been discovered, and new variants have been evolved by protein engineering. Here, we report on a [...] Read more.
Enzymatic degradation is a promising green approach to bioremediation and recycling of the polymer poly(ethylene terephthalate) (PET). In the past few years, several PET-hydrolysing enzymes (PHEs) have been discovered, and new variants have been evolved by protein engineering. Here, we report on a straightforward workflow employing semi-rational protein engineering combined to a high-throughput screening of variant libraries for their activity on PET nanoparticles. Using this approach, starting from the double variant W159H/S238F of Ideonella sakaiensis 201-F6 PETase, the W159H/F238A-ΔIsPET variant, possessing a higher hydrolytic activity on PET, was identified. This variant was stabilized by introducing two additional known substitutions (S121E and D186H) generating the TS-ΔIsPET variant. By using 0.1 mg mL−1 of TS-ΔIsPET, ~10.6 mM of degradation products were produced in 2 days from 9 mg mL−1 PET microparticles (~26% depolymerization yield). Indeed, TS-ΔIsPET allowed a massive degradation of PET nanoparticles (>80% depolymerization yield) in 1.5 h using only 20 μg of enzyme mL−1. The rationale underlying the effect on the catalytic parameters due to the F238A substitution was studied by enzymatic investigation and molecular dynamics/docking analysis. The present workflow is a well-suited protocol for the evolution of PHEs to help generate an efficient enzymatic toolbox for polyester degradation. Full article
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