Journal Menu► ▼ Journal Menu
Journal Browser► ▼ Journal Browser
Special Issue "Industrial Biocatalysis: Challenges and Opportunities"
Deadline for manuscript submissions: 31 May 2020.
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 and Collections in MDPI journals
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
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.
- Industrial applications
- Sustainable chemistry
- Enzyme discovery
- Biocatalyst development
- Process development
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.