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Fermentation
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Research on Microbial Transformation and Biosynthesis of Enzymes
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Research on Microbial Transformation and Biosynthesis of Enzymes

A special issue of Fermentation (ISSN 2311-5637). This special issue belongs to the section "Microbial Metabolism, Physiology & Genetics".

Deadline for manuscript submissions: closed (31 October 2023) | Viewed by 2896

Special Issue Editors

Dr. Guoqiang Zhang

E-Mail Website
Guest Editor
National Engineering Research Center of Cereal Fermentation and Food Biomanufacturing, Jiangnan University, Wuxi 214122, China
Interests: enzyme engineering; synthetic biology
Prof. Dr. Jianghua Li

E-Mail Website
Guest Editor
Science Center for Future Foods, Jiangnan University, Wuxi 214122, China
Interests: fermentation engineering; enzyme engineering

Special Issue Information

Dear Colleagues,

Microbial transformation has proved to be an imperative tool in mitigating the production of various chemicals in food, pharmaceutical, and agrochemical industries, among others. They offer efficient and economical ways to generate an enormous variety of structurally diversified organic compounds via biocatalysis. Microorganisms such as bacteria, yeast, and fungi could specifically catalyze substrates to diverse products that are extremely difficult to produce by chemical routes. In recent years, considerable research on computational biology, enzyme engineering,  and synthetic biology has promoted the development of microbial transformation to obtain more biologically active molecules with diverse structural and functional features.

This Special Issue aims to publish both recent innovative research as well as review papers on the microbial transformation and biosynthesis of enzymes, such as the biocatalysis, enzyme engineering, and cell factory construction for enzyme biosynthesis. Reviews and research papers on cell-free systems for protein biosynthesis are also of interest.

Dr. Guoqiang Zhang
Prof. Dr. Jianghua Li
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. Fermentation 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 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

  • microbial transformation
  • enzyme engineering
  • protein engineering
  • synthetic biology
  • protein expression
  • fermentation engineering
  • microbial breeding

Published Papers (2 papers)

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Research

12 pages, 11523 KiB  
Article
Engineering the C3N Pathway as a Short Detour for De Novo NAD+ Biosynthesis in Saccharomyces cerevisiae
by Xinli Li, Yue Tang, Yong Ding, Pengwei Li and Yihua Chen
Fermentation 2023, 9(10), 886; https://doi.org/10.3390/fermentation9100886 - 29 Sep 2023
Viewed by 925
Abstract
As a life-essential coenzyme, nicotinamide adenine dinucleotide (NAD+) has been explored for more than a century. In Saccharomyces, the natural NAD+de novo biosynthetic pathway initiating from tryptophan has been well elucidated. To bypass this stringently controlled natural pathway [...] Read more.
As a life-essential coenzyme, nicotinamide adenine dinucleotide (NAD+) has been explored for more than a century. In Saccharomyces, the natural NAD+de novo biosynthetic pathway initiating from tryptophan has been well elucidated. To bypass this stringently controlled natural pathway in yeast, an economical C3N pathway that was developed in Escherichia coli previously was constructed in Saccharomyces as a short detour for de novo NAD+ biosynthesis. After the functional expressions of the C3N genes were identified in Saccharomyces cerevisiae BY4741 by in vitro enzymatic assays, the C3N module was introduced into an NAD+ auxotrophic S. cerevisiae strain BY01, in which the BNA2 gene encoding tryptophan 2,3-dioxygenase was inactivated. The efficient NAD+ synthesis via the C3N pathway was confirmed by both plate assays and fermentation analysis. The applicability of the C3N pathway in cofactor engineering was tested by introducing it into S. cerevisiae BY4741, which improved the cellular NAD(H) level considerably. Consequently, this study proved that the de novo NAD+ biosynthetic pathway can be replaced by an artificial pathway in yeast, which paves a way to design more promising schemes in eukaryotes for rational manipulation of the cellular NAD(H) levels. Full article
(This article belongs to the Special Issue Research on Microbial Transformation and Biosynthesis of Enzymes)
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17 pages, 9454 KiB  
Article
Characterization of a Metallic-Ions-Independent L-Arabinose Isomerase from Endophytic Bacillus amyloliquefaciens for Production of D-Tagatose as a Functional Sweetener
by Hoda M. Shehata, Mohamed N. Abd El-Ghany, Salwa A. Hamdi, Mosleh M. Abomughaid, Khaled I. Ghaleb, Zeinat Kamel and Mohamed G. Farahat
Fermentation 2023, 9(8), 749; https://doi.org/10.3390/fermentation9080749 - 12 Aug 2023
Viewed by 1403
Abstract
D-Tagatose is a low-calorie sugar substitute that has gained increased attention as a functional sweetener owing to its nutraceutical and prebiotic properties. Traditionally, D-tagatose is produced via the enzymatic conversion of L-galactose to D-tagatose by L-arabinose isomerase (L-AI). Nonetheless, the most reported L-AI [...] Read more.
D-Tagatose is a low-calorie sugar substitute that has gained increased attention as a functional sweetener owing to its nutraceutical and prebiotic properties. Traditionally, D-tagatose is produced via the enzymatic conversion of L-galactose to D-tagatose by L-arabinose isomerase (L-AI). Nonetheless, the most reported L-AI enzymes are ion-dependent enzymes requiring Mn2+ and/or Co2+ as cofactors for their reactions, which limits their application due to safety and health concerns. Herein, we addressed the facile bioconversion of L-galactose to D-tagatose using a novel recombinant metallic-ions-independent L-AI derived from endophytic Bacillus amyloliquefaciens CAAI isolated from cantaloupe fruits. The ORF (1500 bp) of the L-arabinose isomerase gene (araA) was cloned and over-expressed in Escherichia coli. The recombinant enzyme (BAAI) was purified to homogeneity using Ni-NTA affinity chromatography, yielding a single distinct band with an apparent molecular mass of approximately 59 kDa as deduced from SDS-PAGE analysis. The purified enzyme showed optimum activity at pH and temperature of 7.5 and 45 °C, respectively, with obvious enzymatic activity in the presence of ethylenediaminetetraacetic acid (EDTA), indicating the metallic-ions independence from BAAI. The Km values of BAAI for D-galactose and L-arabinose were 251.6 mM and 92.8 mM, respectively. The catalytic efficiency (kcat/Km) values for D-galactose and L-arabinose were found to be 2.34 and 46.85 mM–1 min–1, respectively. The results revealed the production of 47.2 g/L D-tagatose from D-galactose (100 g/L) with 47.2% bioconversion efficiency in a metallic-ions-free reaction system that could be implemented in safe-production of food-grade low-calorie sweetener, D-tagatose. Full article
(This article belongs to the Special Issue Research on Microbial Transformation and Biosynthesis of Enzymes)
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