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 . .

TY  - CONF
AU  - García-Sanz, Carla
AU  - Andreu, Alicia
AU  - de las Rivas, Blanca
AU  - Muñoz, Rosario
AU  - Vukoičić, Ana
AU  - Milivojević, Ana
AU  - Bezbradica, Dejan
AU  - Palomo, Jose Miguel
PY  - 2023
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6949
AB  - Laccase (EC 1.10.3.2, p-diphenol: dioxygen oxidoreductase) is a blue copper oxidase
of great industrial interest due to its ability to catalyseoxidation processes of phenols and
persistent organic pollutants. However, it is susceptible to denaturation by high temperatures,
and sensitive to pH and the presence of high concentrations of solvents, which is a problem
for industrial use. To solve this problem, this project develops the synthesis in aqueous
medium of a new Mn metalloenzyme with laccase oxidase mimetic catalytic activity. To do
this, Geobacillus thermocatenulatus lipase (GTL) is used as a "scaffold" enzyme, which is
mixed with a manganese salt at 50 ºC in an aqueous medium. In this way, the in situ
formation of manganese (IV) oxide nanowires is generated, interacting with the enzyme and
obtaining the GTL-Mn bioconjugate. On the other hand, its oxidative activity was evaluated
using the ABTS assay, obtaining a specificity 300 times greater than the laccase from
Trametes versicolor and 2 times more than the laccase from Myceliophthora thermophila
expressed in Aspergillus oryzae (Novozym 51003®). In addition, the new metalloenzyme
turned out to be 2 times more stable at 40 ºC, 3 times more stable in thepresence of 10% can,
and 10 times more stable at 20% and 30% AcN than laccase (Novozym 51003®) by
evaluating it at 2 hour incubation. Moreover, it was shown that the use of immobilization
strategies improves the stabilization of this artificial metalloenzyme two times more. Finally,
the novel Mn metalloenzymes were effective in the reaction of phlorizin oligomerization.
Future research will aim to extend this study for the use of flavonoids as prebiotic molecules
in the cosmetics industry.
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  - STUDY AND PREPARATION OF ARTIFICIAL MANGANESE METALLOENZYMES WITH LACCASE LIKE ACTIVITY
SP  - 35
UR  - https://hdl.handle.net/21.15107/rcub_technorep_6949
ER  - 

@conference{
author = "García-Sanz, Carla and Andreu, Alicia and de las Rivas, Blanca and Muñoz, Rosario and Vukoičić, Ana and Milivojević, Ana and Bezbradica, Dejan and Palomo, Jose Miguel",
year = "2023",
abstract = "Laccase (EC 1.10.3.2, p-diphenol: dioxygen oxidoreductase) is a blue copper oxidase
of great industrial interest due to its ability to catalyseoxidation processes of phenols and
persistent organic pollutants. However, it is susceptible to denaturation by high temperatures,
and sensitive to pH and the presence of high concentrations of solvents, which is a problem
for industrial use. To solve this problem, this project develops the synthesis in aqueous
medium of a new Mn metalloenzyme with laccase oxidase mimetic catalytic activity. To do
this, Geobacillus thermocatenulatus lipase (GTL) is used as a "scaffold" enzyme, which is
mixed with a manganese salt at 50 ºC in an aqueous medium. In this way, the in situ
formation of manganese (IV) oxide nanowires is generated, interacting with the enzyme and
obtaining the GTL-Mn bioconjugate. On the other hand, its oxidative activity was evaluated
using the ABTS assay, obtaining a specificity 300 times greater than the laccase from
Trametes versicolor and 2 times more than the laccase from Myceliophthora thermophila
expressed in Aspergillus oryzae (Novozym 51003®). In addition, the new metalloenzyme
turned out to be 2 times more stable at 40 ºC, 3 times more stable in thepresence of 10% can,
and 10 times more stable at 20% and 30% AcN than laccase (Novozym 51003®) by
evaluating it at 2 hour incubation. Moreover, it was shown that the use of immobilization
strategies improves the stabilization of this artificial metalloenzyme two times more. Finally,
the novel Mn metalloenzymes were effective in the reaction of phlorizin oligomerization.
Future research will aim to extend this study for the use of flavonoids as prebiotic molecules
in the cosmetics industry.",
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 = "STUDY AND PREPARATION OF ARTIFICIAL MANGANESE METALLOENZYMES WITH LACCASE LIKE ACTIVITY",
pages = "35",
url = "https://hdl.handle.net/21.15107/rcub_technorep_6949"
}

García-Sanz, C., Andreu, A., de las Rivas, B., Muñoz, R., Vukoičić, A., Milivojević, A., Bezbradica, D.,& Palomo, J. M.. (2023). STUDY AND PREPARATION OF ARTIFICIAL MANGANESE METALLOENZYMES WITH LACCASE LIKE ACTIVITY. 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., 35.
https://hdl.handle.net/21.15107/rcub_technorep_6949

García-Sanz C, Andreu A, de las Rivas B, Muñoz R, Vukoičić A, Milivojević A, Bezbradica D, Palomo JM. STUDY AND PREPARATION OF ARTIFICIAL MANGANESE METALLOENZYMES WITH LACCASE LIKE ACTIVITY. in Book of Abstracts / International Conference Biochemical Engineering and Biotechnology for Young Scientists, 7-8 December, 2023, Belgrade. 2023;:35.
https://hdl.handle.net/21.15107/rcub_technorep_6949 .

García-Sanz, Carla, Andreu, Alicia, de las Rivas, Blanca, Muñoz, Rosario, Vukoičić, Ana, Milivojević, Ana, Bezbradica, Dejan, Palomo, Jose Miguel, "STUDY AND PREPARATION OF ARTIFICIAL MANGANESE METALLOENZYMES WITH LACCASE LIKE ACTIVITY" in Book of Abstracts / International Conference Biochemical Engineering and Biotechnology for Young Scientists, 7-8 December, 2023, Belgrade (2023):35,
https://hdl.handle.net/21.15107/rcub_technorep_6949 .