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Catalysts
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Industrial Biocatalysis: Challenges and Opportunities
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Industrial Biocatalysis: Challenges and Opportunities

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

Deadline for manuscript submissions: closed (31 May 2020) | Viewed by 34396

Special Issue Editor

Dr. Daniela Monti

E-Mail Website
Guest Editor
Istituto di Chimica del Riconoscimento Molecolare, C.N.R.–Via Mario Bianco 9, 20131 Milano, Italy
Interests: biocatalysis; applications of different classes of enzymes (hydrolases, phospholipases, glycosidases, glycosyltransferases, oxidoreductases) in organic synthesis; multienzymatic and chemo-enzymatic cascade systems; free and immobilized enzymes in industrial applications; discovery and characterization of novel enzymes; metagenomics; optimization of protein expression in heterologous hosts; improvement of biocatalyst performances
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

During the last few decades, industrial biocatalysis has largely demonstrated its huge potential as a green alternative to traditional production methods by allowing the development of several biocatalyzed sustainable and selective manufacturing processes in the chemical, pharmaceutical, food, and cosmetics industry. The widespread application of biocatalysis has been also encouraged by the impressive advances in the availability of both native and tailor-made enzymes that can be obtained today by (meta)genomes mining and biocatalyst engineering. However, the development of novel biocatalytic applications and their integration in existing manufacturing processes still poses several challenges to be faced. In particular, significant efforts will be required (a) to speed up the “sequence-to-function” identification of biocatalysts with the desired activity as well as suitable operational stability; (b) to benchmark the developed processes to estimate the “real” sustainability improvement when compared to existing processes; and (c) to develop novel and more efficient process design methods capable of reducing both time and resources needed for the implementation of the biocatalytic alternatives in the industrial context.

This Special Issue on “Industrial Biocatalysis: Challenges and Opportunities” will offer an attractive forum to present recent advances in the development of industrially-relevant biocatalyzed processes, as well as in related technologies aimed at the optimization of enzyme discovery and production, biocatalyst immobilization and recycling, and process and sustainability design and metrics.

Dr. Daniela Monti
Guest Editor

Manuscript Submission Information

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Keywords

  • Biocatalysis
  • Industrial applications
  • Sustainable chemistry
  • Enzyme discovery
  • Biocatalyst development
  • Process development

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Published Papers (5 papers)

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Research

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14 pages, 2127 KiB  
Article
Laccase Did It again: A Scalable and Clean Regeneration System for NAD+ and Its Application in the Synthesis of 12-oxo-Hydroxysteroids
by Fabio Tonin, Elisabet Martì, Isabel W. C. E. Arends and Ulf Hanefeld
Catalysts 2020, 10(6), 677; https://doi.org/10.3390/catal10060677 - 16 Jun 2020
Cited by 10 | Viewed by 3630
Abstract
The specific oxidation of 12α-OH group of hydroxysteroids is required for the preparation of cheno- and ursodeoxycholic acid (CDCA and UDCA, respectively). The C12 oxidation of hydroxysteroids into their 12-oxo derivatives can selectively be performed by employing 12α-hydroxysteroid dehydrogenases. These enzymes use [...] Read more.
The specific oxidation of 12α-OH group of hydroxysteroids is required for the preparation of cheno- and ursodeoxycholic acid (CDCA and UDCA, respectively). The C12 oxidation of hydroxysteroids into their 12-oxo derivatives can selectively be performed by employing 12α-hydroxysteroid dehydrogenases. These enzymes use NAD(P)+ as an electron acceptor, which has to be re-oxidized in a so-called “regeneration system”. Recently, the enzyme NAD(P)H oxidase (NOX) was applied for the regeneration of NAD+ in the enzymatic preparation of 12-oxo-CDCA from cholic acid (CA), which allows air to be used as an oxidant. However, the NOX system suffers from low activity and low stability. Moreover, the substrate loading is limited to 10 mM. In this study, the laccase/mediator system was investigated as a possible alternative to NOX, employing air as an oxidant. The laccase/mediator system shows higher productivity and scalability than the NOX system. This was proven with a preparative biotransformation of 20 g of CA into 12-oxo-CDCA (92% isolated yield) by employing a substrate loading of 120 mM (corresponding to 50 g/L). Additionally, the performance of the laccase/mediator system was compared with a classical ADH/acetone regeneration system and with other regeneration systems reported in literature. Full article
(This article belongs to the Special Issue Industrial Biocatalysis: Challenges and Opportunities)
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12 pages, 2219 KiB  
Article
Biotransformation of Phytosterols to Androst-1,4-Diene-3,17-Dione by Mycobacterium sp. ZFZ Expressing 3-Ketosteroid-Δ1-Dehydrogenase
by Xiangcen Liu, Ruijie Zhang, Zhiwei Bao, Chenyang Yuan, Huijin Cao, Jiping Shi, Junsong Sun and Baoguo Zhang
Catalysts 2020, 10(6), 663; https://doi.org/10.3390/catal10060663 - 12 Jun 2020
Cited by 6 | Viewed by 3298
Abstract
As an important hormone drug intermediate, androst-1,4-diene-3,17-dione can be bio-converted from phytosterols. However, separation and purification in the downstream process are very difficult due to the similarity in structure and physiological characteristics between ADD and androstenedione (AD). This phenomenon was correlated to the [...] Read more.
As an important hormone drug intermediate, androst-1,4-diene-3,17-dione can be bio-converted from phytosterols. However, separation and purification in the downstream process are very difficult due to the similarity in structure and physiological characteristics between ADD and androstenedione (AD). This phenomenon was correlated to the insufficient enzyme activity of 3-ketosteroid-Δ1-dehydrogenase (KSDD), which specifically catalyzes the C1,2 dehydrogenation of AD. In order to obtain a highly purified ADD from phytosterols, the dehydrogenation effect of different kinds of KSDDs and the transcription effect of four promoter sequences on ksdd were analyzed in Mycobacterium sp. ZFZ (ZFZ), the cell host that transform phytosterols to AD in the oil-aqueous system. A tandem KSDD expression cassette containing strain ZFZ-2111 yielded 2.06 ± 0.09 g L−1 ADD, with a molar ratio of ADD/AD at 41.47:1.00 in 120 h. In waste cooking oil-aqueous media, the proportion of ADD in the fermentation by ZFZ-2111 was 92%. The present study provides a reliable theoretical basis for the step-by-step transformation of phytosterols to ADD. Full article
(This article belongs to the Special Issue Industrial Biocatalysis: Challenges and Opportunities)
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11 pages, 2311 KiB  
Article
Active Expression of Membrane-Bound L-Amino Acid Deaminase from Proteus mirabilis in Recombinant Escherichia coli by Fusion with Maltose-Binding Protein for Enhanced Catalytic Performance
by Dan-Ping Zhang, Xiao-Ran Jing, An-Wen Fan, Huan Liu, Yao Nie and Yan Xu
Catalysts 2020, 10(2), 215; https://doi.org/10.3390/catal10020215 - 10 Feb 2020
Cited by 3 | Viewed by 3408
Abstract
L-amino acid deaminases (LAADs) are membrane flavoenzymes that catalyze the deamination of neutral and aromatic L-amino acids to α-keto acids and ammonia. LAADs can be used to develop many important biotechnological applications. However, the transmembrane α-helix of LAADs restricts its soluble active expression [...] Read more.
L-amino acid deaminases (LAADs) are membrane flavoenzymes that catalyze the deamination of neutral and aromatic L-amino acids to α-keto acids and ammonia. LAADs can be used to develop many important biotechnological applications. However, the transmembrane α-helix of LAADs restricts its soluble active expression and purification from a heterologous host, such as Escherichia coli. Herein, through fusion with the maltose-binding protein (MBP) tag, the recombinant E. coli BL21 (DE3)/pET-21b-MBP-PmLAAD was constructed and the LAAD from Proteus mirabilis (PmLAAD) was actively expressed as a soluble protein. After purification, the purified MBP-PmLAAD was obtained. Then, the catalytic activity of the MBP-PmLAAD fusion protein was determined and compared with the non-fused PmLAAD. After fusion with the MBP-tag, the catalytic efficiency of the MBP-PmLAAD cell lysate was much higher than that of the membrane-bound PmLAAD whole cells. The soluble MBP-PmLAAD cell lysate catalyzed the conversion of 100 mM L-phenylalanine (L-Phe) to phenylpyruvic acid (PPA) with a 100% yield in 6 h. Therefore, the fusion of the MBP-tag not only improved the soluble expression of the PmLAAD membrane-bound protein, but also increased its catalytic performance. Full article
(This article belongs to the Special Issue Industrial Biocatalysis: Challenges and Opportunities)
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Review

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30 pages, 11068 KiB  
Review
Biocatalysis with Laccases: An Updated Overview
by Ivan Bassanini, Erica Elisa Ferrandi, Sergio Riva and Daniela Monti
Catalysts 2021, 11(1), 26; https://doi.org/10.3390/catal11010026 - 28 Dec 2020
Cited by 93 | Viewed by 9512
Abstract
Laccases are multicopper oxidases, which have been widely investigated in recent decades thanks to their ability to oxidize organic substrates to the corresponding radicals while producing water at the expense of molecular oxygen. Besides their successful (bio)technological applications, for example, in textile, petrochemical, [...] Read more.
Laccases are multicopper oxidases, which have been widely investigated in recent decades thanks to their ability to oxidize organic substrates to the corresponding radicals while producing water at the expense of molecular oxygen. Besides their successful (bio)technological applications, for example, in textile, petrochemical, and detoxifications/bioremediations industrial processes, their synthetic potentialities for the mild and green preparation or selective modification of fine chemicals are of outstanding value in biocatalyzed organic synthesis. Accordingly, this review is focused on reporting and rationalizing some of the most recent and interesting synthetic exploitations of laccases. Applications of the so-called laccase-mediator system (LMS) for alcohol oxidation are discussed with a focus on carbohydrate chemistry and natural products modification as well as on bio- and chemo-integrated processes. The laccase-catalyzed Csp2-H bonds activation via monoelectronic oxidation is also discussed by reporting examples of enzymatic C-C and C-O radical homo- and hetero-couplings, as well as of aromatic nucleophilic substitutions of hydroquinones or quinoids. Finally, the laccase-initiated domino/cascade synthesis of valuable aromatic (hetero)cycles, elegant strategies widely documented in the literature across more than three decades, is also presented. Full article
(This article belongs to the Special Issue Industrial Biocatalysis: Challenges and Opportunities)
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33 pages, 2245 KiB  
Review
Advances in Recombinant Lipases: Production, Engineering, Immobilization and Application in the Pharmaceutical Industry
by Fabiano Jares Contesini, Marcelo Gomes Davanço, Gustavo Pagotto Borin, Katherina Garcia Vanegas, João Pedro Gonçalves Cirino, Ricardo Rodrigues de Melo, Uffe Hasbro Mortensen, Kristiina Hildén, Daniel Rossi Campos and Patricia de Oliveira Carvalho
Catalysts 2020, 10(9), 1032; https://doi.org/10.3390/catal10091032 - 9 Sep 2020
Cited by 63 | Viewed by 13685
Abstract
Lipases are one of the most used enzymes in the pharmaceutical industry due to their efficiency in organic syntheses, mainly in the production of enantiopure drugs. From an industrial viewpoint, the selection of an efficient expression system and host for recombinant lipase production [...] Read more.
Lipases are one of the most used enzymes in the pharmaceutical industry due to their efficiency in organic syntheses, mainly in the production of enantiopure drugs. From an industrial viewpoint, the selection of an efficient expression system and host for recombinant lipase production is highly important. The most used hosts are Escherichia coli and Komagataella phaffii (previously known as Pichia pastoris) and less often reported Bacillus and Aspergillus strains. The use of efficient expression systems to overproduce homologous or heterologous lipases often require the use of strong promoters and the co-expression of chaperones. Protein engineering techniques, including rational design and directed evolution, are the most reported strategies for improving lipase characteristics. Additionally, lipases can be immobilized in different supports that enable improved properties and enzyme reuse. Here, we review approaches for strain and protein engineering, immobilization and the application of lipases in the pharmaceutical industry. Full article
(This article belongs to the Special Issue Industrial Biocatalysis: Challenges and Opportunities)
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