Microbial Genome Engineering for Production of Natural Products and Biopolymers

A special issue of Genes (ISSN 2073-4425). This special issue belongs to the section "Microbial Genetics and Genomics".

Deadline for manuscript submissions: 25 June 2024 | Viewed by 527

Special Issue Editors

Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139 USA
Interests: genome editing; metabolic engineering; recombineering; microbial products; pathway engineering; heterologous protein expression; protein engineering
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Guest Editor
College of Biological Engineering, Henan University of Technology, Zhengzhou 450001, China
Interests: microbial engineering; industrial fermentation processes; regulation of mycotoxin synthesis
School of Biological Science and Engineering, South China University of Technology, Guangzhou 510640, China
Interests: antimicrobials; biofilm control; biofilm-associated proteins; exopolysaccharides
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

In recent years, tremendous progress has been made in synthetic biology, enabling the production of biochemicals, therapeutics, and food ingredients using a variety of host organisms. Synthetic biologists have enabled us to engineer microbial cells for useful purposes by rewriting and editing their genomes. With the emergence of a variety of powerful genome engineering techniques, such as the CRISPR/Cas systems, our ability to engineer microbial genomes has substantially improved in recent years.

However, rationally designing and reshaping a genome to produce the desired phenotype remains enormously difficult, and more genome engineering strategies need to be explored. To explore this fast-growing field, this Special Issue will cover the latest genome engineering tools, other synthetic biology techniques, and their application to give rise to improved or novel phenotypes in microorganisms for the production of natural products and biopolymers. New tools, methods, and future perspectives are of particular interest.

Dr. Cheng Li
Dr. Yangyong Lv
Dr. Yanrui Ye
Guest Editors

Manuscript Submission Information

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Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 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

  • metabolic engineering
  • synthetic biology
  • microbial cell factories
  • natural products
  • biopolymers
  • genome editing
  • CRISPR

Published Papers (1 paper)

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Research

18 pages, 7369 KiB  
Article
Expression and Characterization of an Efficient Alginate Lyase from Psychromonas sp. SP041 through Metagenomics Analysis of Rotten Kelp
by Ping Wang, Yi Cai, Hua Zhong, Ruiting Chen, Yuetao Yi, Yanrui Ye and Lili Li
Genes 2024, 15(5), 598; https://doi.org/10.3390/genes15050598 - 8 May 2024
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Abstract
Alginate is derived from brown algae, which can be cultivated in large quantities. It can be broken down by alginate lyase into alginate oligosaccharides (AOSs), which exhibit a higher added value and better bioactivity than alginate. In this study, metagenomic technology was used [...] Read more.
Alginate is derived from brown algae, which can be cultivated in large quantities. It can be broken down by alginate lyase into alginate oligosaccharides (AOSs), which exhibit a higher added value and better bioactivity than alginate. In this study, metagenomic technology was used to screen for genes that code for high-efficiency alginate lyases. The candidate alginate lyase gene alg169 was detected from Psychromonas sp. SP041, the most abundant species among alginate lyase bacteria on selected rotten kelps. The alginate lyase Alg169 was heterologously expressed in Escherichia coli BL21 (DE3), Ni-IDA-purified, and characterized. The optimum temperature and pH of Alg169 were 25 °C and 7.0, respectively. Metal ions including Mn2+, Co2+, Ca2+, Mg2+, Ni2+, and Ba2+ led to significantly increased enzyme activity. Alg169 exhibited a pronounced dependence on Na+, and upon treatment with Mn2+, its activity surged by 687.57%, resulting in the highest observed enzyme activity of 117,081 U/mg. Bioinformatic analysis predicted that Alg169 would be a double-domain lyase with a molecular weight of 65.58 kDa. It is a bifunctional enzyme with substrate specificity to polyguluronic acid (polyG) and polymannuronic acid (polyM). These results suggest that Alg169 is a promising candidate for the efficient manufacturing of AOSs from brown seaweed. Full article
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