Catalysis in the Synthesis of Phospholipids for Industrial Applications

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Catalysis in Organic and Polymer Chemistry".

Deadline for manuscript submissions: closed (10 November 2021) | Viewed by 3121

Special Issue Editor


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Guest Editor
Department of Chemistry, Wrocław University of Environmental and Life Sciences, Norwida 25, 50-375 Wrocław, Poland
Interests: biocatalysis; chemoenzymatic modifications of phospholipids; phospholipids as the carriers of active molecules; lipid delivery systems; food and pharmaceutical biotechnology; biotransformations of xenobiotics; natural products
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Special Issue Information

Dear Colleagues,

In recent years, there has been rapid progress in the field of bioengineering and phospholipids technology. Many new discoveries in this area have completely changed the idea that phospholipids are just the integral components of biomembrane ensuring their integrity and functionality and energetic and supplementary material. It is currently known that phospholipids are involved in many metabolic and neurological reactions. They regulate fundamental biological processes and play an important role in the transmission of information as intracellular mediators. They are a very important part of the human diet, strongly influencing people’s health. Some of them are essential to life and proper functions of human organism. In the food industry, phospholipids are used because of their amphiphilic nature as natural surfactants. Commercial phospholipids are employed as baking improvers to ameliorate fat dispersion and anti-staling, as additives to reduce viscosity and prevent crystallization, as wetting enhancers to improve the wetting stabilization of instant products, and as stabilizers. In the pharmaceutical industry, phospholipids are used as carriers in the transport of drugs through biological membranes and skin-moisturizing substances. Clinical studies have also verified their positive impact on enhanced concentration and memory performance of the aging brain, the activation of the liver metabolism, and detoxication and anticancer properties.

Today, chemoenzymatic modifications of phospholipids are under extensive studies. Many strategies are used for production of new multifunctional derivatives/conjugates of phospholipids. This Special Issue on “Catalysis in the Synthesis of Phospholipids for Industrial Applications” is dedicated to recent developments in the field of phospholipids and biocatalytic processes in which they are involved or can be applied for production of new therapeutics, nutraceuticals, biosurfactants, food additives or agents active in the prevention of civilization diseases. Colleagues are invited to participate by proposing original research papers, reviews, and opinions focused on biocatalytic methodologies or biocatalysts useful in the design of structured phospholipids with industrial applications.

Dr. Anna Gliszczyńska
Guest Editor

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Keywords

  • Enzyme
  • Biocatalysis
  • Modifications of phospholipids catalyzed by lipases/phospholipases
  • Structured phospholipids
  • Process optimization
  • Phospholipid conjugates
  • Phospholipid carriers

Published Papers (1 paper)

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Research

15 pages, 2361 KiB  
Article
Highly Efficient Extracellular Production of Recombinant Streptomyces PMF Phospholipase D in Escherichia coli
by Jing Wang, Sheng Xu, Yang Pang, Xin Wang, Kequan Chen and Pingkai Ouyang
Catalysts 2020, 10(9), 1057; https://doi.org/10.3390/catal10091057 - 14 Sep 2020
Cited by 4 | Viewed by 2669
Abstract
To achieve efficient bio-production of phospholipase D (PLD), PLDs from different organisms were expressed in E.coli. An efficient secretory expression system was thereby developed for PLD. First, PLDs from Streptomyces PMF and Streptomyces racemochromogenes were separately over-expressed in E.coli to [...] Read more.
To achieve efficient bio-production of phospholipase D (PLD), PLDs from different organisms were expressed in E.coli. An efficient secretory expression system was thereby developed for PLD. First, PLDs from Streptomyces PMF and Streptomyces racemochromogenes were separately over-expressed in E.coli to compare their transphosphatidylation activity based on the synthesis of phosphatidylserine (PS), and PLDPMF was determined to have higher activity. To further improve PLDPMF synthesis, a secretory expression system suitable for PLDPMF was constructed and optimized with different signal peptides. The highest secretory efficiency was observed when the PLD * (PLDPMF with the native signal peptide Nat removed) was expressed fused with the fusion signal peptide PelB-Nat in E. coli. The fermentation conditions were also investigated to increase the production of recombinant PLD and 10.5 U/mL PLD was ultimately obtained under the optimized conditions. For the application of recombinant PLD to PS synthesis, the PLD properties were characterized and 30.2 g/L of PS was produced after 24 h of bioconversion when 50 g/L phosphatidylcholine (PC) was added. Full article
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