Frontiers of Biocatalysis and Biotransformation

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

Deadline for manuscript submissions: closed (20 April 2022) | Viewed by 1749

Special Issue Editor


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Guest Editor
Key Laboratory of Biopesticide and Chemical Biology, Ministry of Education, College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou, Fujian 350002, China
Interests: Biocatalysis and Biotransformation; Protein Engineering; Synthetic Biology

Special Issue Information

Dear Colleagues,

Biocatalysis and biotransformation (BCBT) is a cross disciplinary area of research that integrates biology, chemistry and process engineering. The core goal is to produce chemicals, medicines, materials and energy using biological or enzymatic processes. BCBT is becoming an important way to replace and expand traditional organic synthesis for significant advantages such as high efficiency, high selectivity, moderate reaction conditions and environmental friendliness. However, several barriers, such as discovery tools of new biocatalysts, the theory and technology of biocatalyst improvement, biocatalytic efficiency under industrial conditions and principles and applications of mutual adaptation between biocatalysts and bioprocesses, need to be explored and solved.

This Special Issue collects original research papers, reviews and opinions focused on frontiers of biocatalysis and biotransformation. Submissions are also welcome from outside the areas presented above.

Prof. Dr. Liaoyuan Zhang
Guest Editor

Manuscript Submission Information

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Keywords

  • enzyme production
  • enzyme purification
  • enzyme discovery
  • enzyme immobilization
  • enzyme improvement
  • bioprocess optimization
  • adaptive laboratory evolution
  • ionic liquid
  • multiple enzyme reactions
  • whole-cell biocatalysis
  • coenzyme regeneration

Published Papers (1 paper)

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Research

14 pages, 3349 KiB  
Article
Characterization of a New Marine Leucine Dehydrogenase from Pseudomonas balearica and Its Application for L-tert-Leucine Production
by Zewang Guo, Denghui Chen, Qi Xiong, Miao Liang, Pengfei Li, Zehui Gong, Junzhi Qiu and Liaoyuan Zhang
Catalysts 2022, 12(9), 971; https://0-doi-org.brum.beds.ac.uk/10.3390/catal12090971 - 30 Aug 2022
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Abstract
Leucine dehydrogenase (LeuDH) has emerged as the most promising biocatalyst for L-tert-leucine (L-Tle) production via asymmetric reduction in trimethylpyruvate (TMP). In this study, a new LeuDH named PbLeuDH from marine Pseudomonas balearica was heterologously over-expressed in Escherichia coli, followed [...] Read more.
Leucine dehydrogenase (LeuDH) has emerged as the most promising biocatalyst for L-tert-leucine (L-Tle) production via asymmetric reduction in trimethylpyruvate (TMP). In this study, a new LeuDH named PbLeuDH from marine Pseudomonas balearica was heterologously over-expressed in Escherichia coli, followed by purification and characterization. PbLeuDH possessed a broad substrate scope, displaying activities toward numerous L-amino acids and α-keto acids. Notably, compared with those reported LeuDHs, PbLeuDH exhibited excellent catalytic efficiency for TMP with a Km value of 4.92 mM and a kcat/Km value of 24.49 s−1 mM−1. Subsequently, L-Tle efficient production was implemented from TMP by whole-cell biocatalysis using recombinant E. coli as a catalyst, which co-expressed PbLeuDH and glucose dehydrogenase (GDH). Ultimately, using a fed-batch feeding strategy, 273 mM (35.8 g L−1) L-Tle was achieved with a 96.1% yield and 2.39 g L−1 h−1 productivity. In summary, our research provides a competitive biocatalyst for L-Tle green biosynthesis and lays a solid foundation for the realization of large-scale L-Tle industrial production. Full article
(This article belongs to the Special Issue Frontiers of Biocatalysis and Biotransformation)
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