Special Issue "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: 31 May 2020.

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
Fax: (+39)-(0)2-28-901-239
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
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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

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 papers will be 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. Catalysts 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 1800 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.


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

Published Papers (1 paper)

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Open AccessArticle
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
Catalysts 2020, 10(2), 215; https://doi.org/10.3390/catal10020215 - 10 Feb 2020
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)

Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Laccase did it again: clean regeneration system for NAD+ and application in the synthesis of 12-oxo-hydroxysteroids

Fabio Tonin, Elisabet Martì and Ulf Hanefeld

Abstract: The specific oxidation of 12α-OH group of hydroxysteroids is a fundamental reaction required for the preparation of Cheno and Ursodeoxycholic acid (CDCA and UDCA, respectively). These pharmaceutical compounds are widely applied in the treatment of cholesterol gallstones and hepatic diseases. The available chemical methods for the transformation of hydroxysteroids into 12-oxo derivatives require the use of toxic chemicals (eg. CrO3) and typically results in low yields (~30%).

On the other hand, biocatalytic methods offer the possibility to convert a range of hydroxysteroids into their 12-oxo derivatives with high selectivity, high yields and avoiding the use of toxic compounds.

Particularly, 12α-hydroxysteroid dehydrogenases specifically oxidize the 12α-OH group of hydroxysteroids with concomitant reduction of NAD(P)+. 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). However, this enzyme suffers of low activity, low stability, high price and the substrate loading is limited to 10 mM.

In order to solve these problems and develop a feasible preparative-scale reaction, the El12α-HSDH was coupled with a laccase in the presence of low molecular weight compounds, known as mediators.

The influence of several factors on the enzymatic activity and stability of the system have been tested (pH values, different mediator types and co-solvents, enzyme and mediator concentrations and substrate loading). A preparatory scaled-up reaction was carried out under optimized conditions: CA (20 g) was fully converted to 12-oxo-CDCA (90% isolated yield) by employing a substrate loading of 120 mM (corresponding to 50 g/L) and a final concentration of syringaldazine (mediator) of 150 μM. This laccase-mediator system shows higher productivity and scalability compared to the NOX system, achieving a 12-fold increase in substrate loading.
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