Special Issue "Biocatalysis: Chemical Biosynthesis"

A special issue of Catalysts (ISSN 2073-4344).

Deadline for manuscript submissions: 30 June 2019

Special Issue Editor

Guest Editor
Dr. Agatha Bastida Codina

CSIC, Inst Quim Organ Gen, C Juan de la Cierva 3, E-28006 Madrid, Spain
Website | E-Mail
Interests: Synthetic Biology, Biochemistry, Molecular biology, Biocatalysis, Biotechnology, Medical Chemistry, Molecular docking methodology

Special Issue Information

Dear Colleagues,

Biocatalysis is a topic based on the edge of biology and chemistry, which enroll together scientists from life sciences, engineers and computer field. Biocatalysis, cell free and whole cell systems, play an increasingly role in a broad range of applications, including food processing, materials, fine chemicals, and medicine. Applied biocatalysis is driven by advances in novel protein engineering tools, economic and environmental pollution. Compare to free biocatalyst, the immobilization techniques improve the stability/activity ration, purification, and the ability to recycle the catalyst consequently more efficient process in the industry. Compared to traditional organic synthesis the use of enzymes provide a way of producing enantiomerical pure compounds mainly through high chemoselectivity and streoselective properties and very mild reaction conditions which offers advantages such as minimizing side reactions or not requiring multiple protection/deprotection steps. The advances in directed evolution, molecular cloning, DNA synthesis, bioinformatic tools, high-throughput screening, and process scale-up have opened up a door to a great variety of enzymes as tools in the industry. By other hand, the use of biosynthetic enzymes can introduce structural diversities that are otherwise inaccessible by organic synthesis. Although biocatalysis have expanded in the industry, a lack of structural and mechanistic knowledge about enzymes has limited widespread use of enzymes. Then combination of the in silico methods for engineering physical properties into proteins and structural biology techniques can guide the understanding of biocatalytic mechanisms and the development of new ones in biology and biotechnology.

Dr. Agatha Bastida Codina
Guest Editor

Manuscript Submission Information

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Keywords

  • Biosynthetic enzymes
  • DNA synthesis
  • Protein engineering
  • Microbial enzymes
  • Biocatalysis
  • Organic synthesis
  • Pharmaceutical
  • Green chemistry
  • Synthetic biology
  • Biotransformation

Published Papers (2 papers)

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Research

Open AccessArticle Production of New Isoflavone Glucosides from Glycosylation of 8-Hydroxydaidzein by Glycosyltransferase from Bacillus subtilis ATCC 6633
Catalysts 2018, 8(9), 387; https://doi.org/10.3390/catal8090387
Received: 24 August 2018 / Revised: 4 September 2018 / Accepted: 7 September 2018 / Published: 10 September 2018
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Abstract
8-Hydroxydaidzein (8-OHDe) has been proven to possess some important bioactivities; however, the low aqueous solubility and stability of 8-OHDe limit its pharmaceutical and cosmeceutical applications. The present study focuses on glycosylation of 8-OHDe to improve its drawbacks in solubility and stability. According to
[...] Read more.
8-Hydroxydaidzein (8-OHDe) has been proven to possess some important bioactivities; however, the low aqueous solubility and stability of 8-OHDe limit its pharmaceutical and cosmeceutical applications. The present study focuses on glycosylation of 8-OHDe to improve its drawbacks in solubility and stability. According to the results of phylogenetic analysis with several identified flavonoid-catalyzing glycosyltransferases (GTs), three glycosyltransferase genes (BsGT110, BsGT292 and BsGT296) from the genome of the Bacillus subtilis ATCC 6633 strain were cloned and expressed in Escherichia coli. The three BsGTs were then purified and the glycosylation activity determined toward 8-OHDe. The results showed that only BsGT110 possesses glycosylation activity. The glycosylated metabolites were then isolated with preparative high-performance liquid chromatography and identified as two new isoflavone glucosides, 8-OHDe-7-O-β-glucoside and8-OHDe-8-O-β-glucoside, whose identity was confirmed by mass spectrometry and nuclear magnetic resonance spectroscopy. The aqueous solubility of 8-OHDe-7-O-β-glucoside and 8-OHDe-8-O-β-glucoside is 9.0- and 4.9-fold, respectively, higher than that of 8-OHDe. Moreover, more than 90% of the initial concentration of the two 8-OHDe glucoside derivatives remained after 96 h of incubation in 50 mM of Tris buffer at pH 8.0. In contrast, the concentration of 8-OHDe decreased to 0.8% of the initial concentration after 96 h of incubation. The two new isoflavone glucosides might have potential in pharmaceutical and cosmeceutical applications. Full article
(This article belongs to the Special Issue Biocatalysis: Chemical Biosynthesis)
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Open AccessArticle Developing a High-Temperature Solvent-Free System for Efficient Biocatalysis of Octyl Ferulate
Catalysts 2018, 8(8), 338; https://doi.org/10.3390/catal8080338
Received: 27 July 2018 / Revised: 14 August 2018 / Accepted: 16 August 2018 / Published: 20 August 2018
PDF Full-text (1950 KB) | HTML Full-text | XML Full-text
Abstract
Ferulic acid esters have been suggested as a group of natural chemicals that have the function of sunscreen. The study aimed to utilize an environmentally-friendly enzymatic method through the esterification of ferulic acid with octanol, producing octyl ferulate. The Box-Behnken experimental design for
[...] Read more.
Ferulic acid esters have been suggested as a group of natural chemicals that have the function of sunscreen. The study aimed to utilize an environmentally-friendly enzymatic method through the esterification of ferulic acid with octanol, producing octyl ferulate. The Box-Behnken experimental design for response surface methodology (RSM) was performed to determine the synthesis effects of variables, including enzyme amount (1000–2000 propyl laurate units (PLU)), reaction temperature (70–90 °C), and stir speed (50–150 rpm) on the molar conversion of octyl ferulate. According to the joint test, both the enzyme amount and reaction temperature had great impacts on the molar conversion. An RSM-developed second-order polynomial equation further showed a data-fitting ability. Using ridge max analysis, the optimal parameters of the biocatalyzed reaction were: 72 h reaction time, 92.2 °C reaction temperature, 1831 PLU enzyme amount, and 92.4 rpm stir speed, respectively. Finally, the molar conversion of octyl ferulate under optimum conditions was verified to be 93.2 ± 1.5%. In conclusion, it has been suggested that a high yield of octyl ferulate should be synthesized under elevated temperature conditions with a commercial immobilized lipase. Our findings could broaden the utilization of the lipase and provide a biocatalytic approach, instead of the chemical method, for ferulic acid ester synthesis. Full article
(This article belongs to the Special Issue Biocatalysis: Chemical Biosynthesis)
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