Ortega-Nieto, Clara

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  • Ortega-Nieto, Clara (2)

Author's Bibliography

Enzymatic Glycosylation Strategies in the Production of Bioactive Compounds

Andreu, Alicia; Ćorović, Marija; Garcia-Sanz, Carla; Santos, A. Sofia; Milivojević, Ana; Ortega-Nieto, Clara; Mateo, Cesar; Bezbradica, Dejan; Palomo, Jose M.

(MDPI, 2023)

TY  - JOUR
AU  - Andreu, Alicia
AU  - Ćorović, Marija
AU  - Garcia-Sanz, Carla
AU  - Santos, A. Sofia
AU  - Milivojević, Ana
AU  - Ortega-Nieto, Clara
AU  - Mateo, Cesar
AU  - Bezbradica, Dejan
AU  - Palomo, Jose M.
PY  - 2023
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6804
AB  - Enzymatic glycosylation is a versatile and sustainable biotechnological approach that plays a pivotal role in the production of bioactive compounds. This process involves the enzymatic transfer of sugar moieties onto various acceptor molecules, such as small molecules, peptides, or proteins, resulting in the synthesis of glycosides. These glycosides often exhibit enhanced bioactivity, improved solubility, and enhanced stability, making them valuable in pharmaceuticals, nutraceuticals, and the food industry. This review explores the diverse enzymatic glycosylation strategies employed in the synthesis of bioactive compounds. It highlights the enzymatic catalysts involved, including glycosyltransferases, glycosidases, glycophosphorylases, and glycosynthases. It considers the advantages and disadvantages of these biocatalysts in the stereoselective and regioselective synthesis of different types of glycosylated molecules, phenolic and aliphatic alcohols, oligosaccharides, polysaccharides, glycoderivatives, glycopeptides, and glycoproteins with a clear focus on food and pharmaceutical chemistry. Furthermore, the review outlines various sources of sugar donors, activated glycosides, and sugar nucleotides, as well as the utilization of engineered enzymes and microorganisms for glycosylation reactions. The advantages of enzymatic glycosylation, including its high regioselectivity, stereoselectivity, and sustainability, are emphasized. Therefore, these approaches combining the use of different catalytic systems, the improvement of tools such as immobilization technology or chemical or genetic modification to improve the glycosylation process, could be useful tools in continuous biotechnological advancements.
PB  - MDPI
T2  - Catalysts
T1  - Enzymatic Glycosylation Strategies in the Production of Bioactive Compounds
IS  - 10
SP  - 1359
VL  - 13
DO  - 10.3390/catal13101359
ER  - 
@article{
author = "Andreu, Alicia and Ćorović, Marija and Garcia-Sanz, Carla and Santos, A. Sofia and Milivojević, Ana and Ortega-Nieto, Clara and Mateo, Cesar and Bezbradica, Dejan and Palomo, Jose M.",
year = "2023",
abstract = "Enzymatic glycosylation is a versatile and sustainable biotechnological approach that plays a pivotal role in the production of bioactive compounds. This process involves the enzymatic transfer of sugar moieties onto various acceptor molecules, such as small molecules, peptides, or proteins, resulting in the synthesis of glycosides. These glycosides often exhibit enhanced bioactivity, improved solubility, and enhanced stability, making them valuable in pharmaceuticals, nutraceuticals, and the food industry. This review explores the diverse enzymatic glycosylation strategies employed in the synthesis of bioactive compounds. It highlights the enzymatic catalysts involved, including glycosyltransferases, glycosidases, glycophosphorylases, and glycosynthases. It considers the advantages and disadvantages of these biocatalysts in the stereoselective and regioselective synthesis of different types of glycosylated molecules, phenolic and aliphatic alcohols, oligosaccharides, polysaccharides, glycoderivatives, glycopeptides, and glycoproteins with a clear focus on food and pharmaceutical chemistry. Furthermore, the review outlines various sources of sugar donors, activated glycosides, and sugar nucleotides, as well as the utilization of engineered enzymes and microorganisms for glycosylation reactions. The advantages of enzymatic glycosylation, including its high regioselectivity, stereoselectivity, and sustainability, are emphasized. Therefore, these approaches combining the use of different catalytic systems, the improvement of tools such as immobilization technology or chemical or genetic modification to improve the glycosylation process, could be useful tools in continuous biotechnological advancements.",
publisher = "MDPI",
journal = "Catalysts",
title = "Enzymatic Glycosylation Strategies in the Production of Bioactive Compounds",
number = "10",
pages = "1359",
volume = "13",
doi = "10.3390/catal13101359"
}
Andreu, A., Ćorović, M., Garcia-Sanz, C., Santos, A. S., Milivojević, A., Ortega-Nieto, C., Mateo, C., Bezbradica, D.,& Palomo, J. M.. (2023). Enzymatic Glycosylation Strategies in the Production of Bioactive Compounds. in Catalysts
MDPI., 13(10), 1359.
https://doi.org/10.3390/catal13101359
Andreu A, Ćorović M, Garcia-Sanz C, Santos AS, Milivojević A, Ortega-Nieto C, Mateo C, Bezbradica D, Palomo JM. Enzymatic Glycosylation Strategies in the Production of Bioactive Compounds. in Catalysts. 2023;13(10):1359.
doi:10.3390/catal13101359 .
Andreu, Alicia, Ćorović, Marija, Garcia-Sanz, Carla, Santos, A. Sofia, Milivojević, Ana, Ortega-Nieto, Clara, Mateo, Cesar, Bezbradica, Dejan, Palomo, Jose M., "Enzymatic Glycosylation Strategies in the Production of Bioactive Compounds" in Catalysts, 13, no. 10 (2023):1359,
https://doi.org/10.3390/catal13101359 . .
2
2

NOVEL Cu/Ag-ENZYME BIOHYBRIDS AS ARTIFICIAL METALLOENZYME

Ortega-Nieto, Clara; Losada-Gracia, Noelia; Vukoičić, Ana; Milivojević, Ana; Bezbradica, Dejan; Palomo, Jose M.

(Belgrade : University, Faculty of Technology and Metallurgy, 2023)

TY  - CONF
AU  - Ortega-Nieto, Clara
AU  - Losada-Gracia, Noelia
AU  - Vukoičić, Ana
AU  - Milivojević, Ana
AU  - Bezbradica, Dejan
AU  - Palomo, Jose M.
PY  - 2023
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6959
AB  - In recent years, the synthesis of novel artificial metalloenzymes by the combination of
metal or complex organometallic systems and enzymes is rapidly growing field of research in
catalytic applications. In this study, new artificial metalloenzymes have been designed and
developed based on the combination of an enzyme and different metal salts. For this purpose,
novel synthesis method has been used, where the enzyme, Lipase B from Candida antarctica
(CALB), acts as an inducer of metal nanoparticles of copper and silver. Obtained biohybrids
show improved stability properties compared to natural enzymes. Moreover, the synergetic
effect between copper and silver has been evaluated, looking for an improvement in the
catalytic efficiency of an only copper-metalloenzyme previously developed.
The copper-silver-CALB metalloenzymes have been characterized by X-Ray
diffraction analysis, mass spectrometry, and SEM and TEM as microscopies techniques. After
that, their catalytic efficiency was tested in different reactions, in particular in the phloridzin
oligomerization as laccase-like activity.
PB  - Belgrade : University, Faculty of Technology and Metallurgy
C3  - Book of Abstracts / International Conference Biochemical Engineering and Biotechnology for Young Scientists, 7-8 December, 2023, Belgrade
T1  - NOVEL Cu/Ag-ENZYME BIOHYBRIDS AS ARTIFICIAL METALLOENZYME
SP  - 39
UR  - https://hdl.handle.net/21.15107/rcub_technorep_6959
ER  - 
@conference{
author = "Ortega-Nieto, Clara and Losada-Gracia, Noelia and Vukoičić, Ana and Milivojević, Ana and Bezbradica, Dejan and Palomo, Jose M.",
year = "2023",
abstract = "In recent years, the synthesis of novel artificial metalloenzymes by the combination of
metal or complex organometallic systems and enzymes is rapidly growing field of research in
catalytic applications. In this study, new artificial metalloenzymes have been designed and
developed based on the combination of an enzyme and different metal salts. For this purpose,
novel synthesis method has been used, where the enzyme, Lipase B from Candida antarctica
(CALB), acts as an inducer of metal nanoparticles of copper and silver. Obtained biohybrids
show improved stability properties compared to natural enzymes. Moreover, the synergetic
effect between copper and silver has been evaluated, looking for an improvement in the
catalytic efficiency of an only copper-metalloenzyme previously developed.
The copper-silver-CALB metalloenzymes have been characterized by X-Ray
diffraction analysis, mass spectrometry, and SEM and TEM as microscopies techniques. After
that, their catalytic efficiency was tested in different reactions, in particular in the phloridzin
oligomerization as laccase-like activity.",
publisher = "Belgrade : University, Faculty of Technology and Metallurgy",
journal = "Book of Abstracts / International Conference Biochemical Engineering and Biotechnology for Young Scientists, 7-8 December, 2023, Belgrade",
title = "NOVEL Cu/Ag-ENZYME BIOHYBRIDS AS ARTIFICIAL METALLOENZYME",
pages = "39",
url = "https://hdl.handle.net/21.15107/rcub_technorep_6959"
}
Ortega-Nieto, C., Losada-Gracia, N., Vukoičić, A., Milivojević, A., Bezbradica, D.,& Palomo, J. M.. (2023). NOVEL Cu/Ag-ENZYME BIOHYBRIDS AS ARTIFICIAL METALLOENZYME. in Book of Abstracts / International Conference Biochemical Engineering and Biotechnology for Young Scientists, 7-8 December, 2023, Belgrade
Belgrade : University, Faculty of Technology and Metallurgy., 39.
https://hdl.handle.net/21.15107/rcub_technorep_6959
Ortega-Nieto C, Losada-Gracia N, Vukoičić A, Milivojević A, Bezbradica D, Palomo JM. NOVEL Cu/Ag-ENZYME BIOHYBRIDS AS ARTIFICIAL METALLOENZYME. in Book of Abstracts / International Conference Biochemical Engineering and Biotechnology for Young Scientists, 7-8 December, 2023, Belgrade. 2023;:39.
https://hdl.handle.net/21.15107/rcub_technorep_6959 .
Ortega-Nieto, Clara, Losada-Gracia, Noelia, Vukoičić, Ana, Milivojević, Ana, Bezbradica, Dejan, Palomo, Jose M., "NOVEL Cu/Ag-ENZYME BIOHYBRIDS AS ARTIFICIAL METALLOENZYME" in Book of Abstracts / International Conference Biochemical Engineering and Biotechnology for Young Scientists, 7-8 December, 2023, Belgrade (2023):39,
https://hdl.handle.net/21.15107/rcub_technorep_6959 .