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Catalysts
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Recent Developments and Challenges of Biocatalytic Processes in the Pharmaceutical...
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Recent Developments and Challenges of Biocatalytic Processes in the Pharmaceutical Industry

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

Deadline for manuscript submissions: closed (10 April 2022) | Viewed by 4235

Special Issue Editors

Prof. Dr. Dunming Zhu

E-Mail Website
Guest Editor
National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering Research Center of Biocatalytic Technology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China
Interests: synthetic chemistry; synthetic biology; biocatalysis; enzyme engineering
Prof. Dr. Jinhui Feng

E-Mail Website
Guest Editor
National Engineering Laboratory for Industrial Enzymes and Tianjin Engineering Research Center of Biocatalytic Technology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China
Interests: biocatalysis; biosynthesis and biotransformation of steroids

Special Issue Information

Dear Colleagues,

Biocatalysis offers high selectivity and mild reactions, and thus has been increasingly applied in the pharmaceutical industry. The integration of biocatalysis into the synthetic route of active pharmaceutical ingredients (APIs) not only makes the manufacturing processes greener and more sustainable by shortening the synthetic route, avoiding the use of harmful reagents and generating fewer wastes, it also expands the chemical space for the discovery of new drugs by synthesizing new compounds that are otherwise not available from traditional chemical reactions. In the past two decades we have witnessed great advances in this area, and many excellent chemoenzymatic processes have been developed on industrial scales for the production of APIs and intermediates. We highly encourage submissions of both research articles and reviews that show the advancement and address the challenges of biocatalytic processes in the pharmaceutical industry.

Prof. Dr. Dunming Zhu
Prof. Dr. Jinhui Feng
Guest Editors

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 submissions that pass pre-check are 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 2700 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.

Keywords

  • biocatalysis
  • chemo-enzymatic synthesis
  • biocatalytic processes
  • APIs
  • pharmaceutical intermediates

Published Papers (2 papers)

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Research

12 pages, 1139 KiB  
Article
Asymmetric Synthesis of Both Enantiomers of Dimethyl 2-Methylsuccinate by the Ene-Reductase-Catalyzed Reduction at High Substrate Concentration
by Jiacheng Li, Jianjiong Li, Yunfeng Cui, Min Wang, Jinhui Feng, Peiyuan Yao, Qiaqing Wu and Dunming Zhu
Catalysts 2022, 12(10), 1133; https://0-doi-org.brum.beds.ac.uk/10.3390/catal12101133 - 28 Sep 2022
Viewed by 1353
Abstract
Chiral dimethyl 2-methylsuccinate (1) is a very important building block for the manufacturing of many active pharmaceutical ingredients and fine chemicals. The asymmetric reduction of C=C double bond of dimethyl citraconate (2), dimethyl mesaconate (3) or dimethyl [...] Read more.
Chiral dimethyl 2-methylsuccinate (1) is a very important building block for the manufacturing of many active pharmaceutical ingredients and fine chemicals. The asymmetric reduction of C=C double bond of dimethyl citraconate (2), dimethyl mesaconate (3) or dimethyl itaconate (4) by ene-reductases (ERs) represents an attractive straightforward approach, but lack of high-performance ERs, especially (S)-selective ones, has limited implementing this method to prepare the optically pure dimethyl 2-methylsuccinate. Herein, three ERs (Bac-OYE1 from Bacillus sp., SeER from Saccharomyces eubayanus and AfER from Aspergillus flavus) with high substrate tolerance and stereoselectivity towards 2, 3 and 4 have been identified. Up to 500 mM of 3 was converted to (S)-dimethyl 2-methylsuccinate ((S)-1) by SeER in high yields (80%) and enantioselectivity (98% ee), and 700 mM of 2 and 400 mM of 4 were converted to (R)-1 by Bac-OYE1 and AfER, respectively, in high yields (86% and 77%) with excellent enantioselectivity (99% ee). The reductions of diethyl citraconate (5), diethyl mesaconate (6) and diethyl itaconate (7) were also tested with the three ERs. Although up to 500 mM of 5 was completely converted to (R)-diethyl 2-methylsuccinate ((R)-8) by Bac-OYE1 with excellent enantioselectivity (99% ee), the alcohol moiety of the esters had a great effect on the activity and enantioselectivity of ERs. This work provides an efficient methodology for the enantiocomplementary production of optically pure dimethyl 2-methylsuccinate from dimethyl itaconate and its isomers at high titer. Full article
(This article belongs to the Special Issue Recent Developments and Challenges of Biocatalytic Processes in the Pharmaceutical Industry)
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10 pages, 1468 KiB  
Article
Semi-Rational Design of Proteus mirabilis l-Amino Acid Deaminase for Expanding Its Substrate Specificity in α-Keto Acid Synthesis from l-Amino Acids
by Anwen Fan, Ziyao Wang, Haojie Qu, Yao Nie and Yan Xu
Catalysts 2022, 12(2), 175; https://0-doi-org.brum.beds.ac.uk/10.3390/catal12020175 - 29 Jan 2022
Cited by 1 | Viewed by 2536
Abstract
l-amino acid deaminases (LAADs) are flavoenzymes that catalyze the stereospecific oxidative deamination of l-amino acids into α-keto acids, which are widely used in the pharmaceutical, food, chemical, and cosmetic industries. However, the substrate specificity of available LAADs is limited, and most [...] Read more.
l-amino acid deaminases (LAADs) are flavoenzymes that catalyze the stereospecific oxidative deamination of l-amino acids into α-keto acids, which are widely used in the pharmaceutical, food, chemical, and cosmetic industries. However, the substrate specificity of available LAADs is limited, and most substrates are concentrated on several bulky or basic l-amino acids. In this study, we employed a LAAD from Proteus mirabilis (PmiLAAD) and broadened its substrate specificity using a semi-rational design strategy. Molecular docking and alanine scanning identified F96, Q278, and E417 as key residues around the substrate-binding pocket of PmiLAAD. Site-directed saturation mutagenesis identified E417 as the key site for substrate specificity expansion. Expansion of the substrate channel with mutations of E417 (E417L, E417A) improved activity toward the bulky substrate l-Trp, and mutation of E417 to basic amino acids (E417K, E417H, E417R) enhanced the universal activity toward various l-amino acid substrates. The variant PmiLAADE417K showed remarkable catalytic activity improvement on seven substrates (l-Ala, l-Asp, l-Ile, l-Leu, l-Phe, l-Trp, and l-Val). The catalytic efficiency improvement obtained by E417 mutation may be attributed to the expansion of the entrance channel and its electrostatic interactions. These PmiLAAD variants with a broadened substrate spectrum can extend the application potential of LAADs. Full article
(This article belongs to the Special Issue Recent Developments and Challenges of Biocatalytic Processes in the Pharmaceutical Industry)
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