TY  - JOUR
AU  - Pekmezović, Marina
AU  - Krusić, Melina Kalagasidis
AU  - Malagurski, Ivana
AU  - Milovanović, Jelena
AU  - Stepien, Karolina
AU  - Guzik, Maciej
AU  - Charifou, Romina
AU  - Babu, Ramesh
AU  - O'Connor, Kevin
AU  - Nikodinović-Runić, Jasmina
PY  - 2021
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1440
AB  - Novel biodegradable and biocompatible formulations of "old" but "gold" drugs such as nystatin (Nys) and amphotericin B (AmB) were made using a biopolymer as a matrix. Medium chain length polyhydroxyalkanoates (mcl-PHA) were used to formulate both polyenes (Nys and AmB) in the form of films (similar to 50 mu m). Thermal properties and stability of the materials were not significantly altered by the incorporation of polyenes in mcl-PHA, but polyene containing materials were more hydrophobic. These formulations were tested in vitro against a panel of pathogenic fungi and for antibiofilm properties. The films containing 0.1 to 2 weight % polyenes showed good activity and sustained polyene release for up to 4 days. A PHA monomer, namely 3-hydroxydecanoic acid (C10-OH), was added to the films to achieve an enhanced synergistic effect with polyenes against fungal growth. Mcl-PHA based polyene formulations showed excellent growth inhibitory activity against both Candida yeasts (C. albicans ATCC 1023, C. albicans SC5314 (ATCC MYA-2876), C. parapsilosis ATCC 22019) and filamentous fungi (Aspergillus fumigatus ATCC 13073; Trichophyton mentagrophytes ATCC 9533, Microsporum gypseum ATCC 24102). All antifungal PHA film preparations prevented the formation of a C. albicans biofilm, while they were not efficient in eradication of mature biofilms, rendering them suitable for the transdermal application or as coatings of implants.
PB  - MDPI, Basel
T2  - Antibiotics-Basel
T1  - Polyhydroxyalkanoate/Antifungal Polyene Formulations with Monomeric Hydroxyalkanoic Acids for Improved Antifungal Efficiency
IS  - 6
VL  - 10
DO  - 10.3390/antibiotics10060737
ER  - 

@article{
author = "Pekmezović, Marina and Krusić, Melina Kalagasidis and Malagurski, Ivana and Milovanović, Jelena and Stepien, Karolina and Guzik, Maciej and Charifou, Romina and Babu, Ramesh and O'Connor, Kevin and Nikodinović-Runić, Jasmina",
year = "2021",
abstract = "Novel biodegradable and biocompatible formulations of "old" but "gold" drugs such as nystatin (Nys) and amphotericin B (AmB) were made using a biopolymer as a matrix. Medium chain length polyhydroxyalkanoates (mcl-PHA) were used to formulate both polyenes (Nys and AmB) in the form of films (similar to 50 mu m). Thermal properties and stability of the materials were not significantly altered by the incorporation of polyenes in mcl-PHA, but polyene containing materials were more hydrophobic. These formulations were tested in vitro against a panel of pathogenic fungi and for antibiofilm properties. The films containing 0.1 to 2 weight % polyenes showed good activity and sustained polyene release for up to 4 days. A PHA monomer, namely 3-hydroxydecanoic acid (C10-OH), was added to the films to achieve an enhanced synergistic effect with polyenes against fungal growth. Mcl-PHA based polyene formulations showed excellent growth inhibitory activity against both Candida yeasts (C. albicans ATCC 1023, C. albicans SC5314 (ATCC MYA-2876), C. parapsilosis ATCC 22019) and filamentous fungi (Aspergillus fumigatus ATCC 13073; Trichophyton mentagrophytes ATCC 9533, Microsporum gypseum ATCC 24102). All antifungal PHA film preparations prevented the formation of a C. albicans biofilm, while they were not efficient in eradication of mature biofilms, rendering them suitable for the transdermal application or as coatings of implants.",
publisher = "MDPI, Basel",
journal = "Antibiotics-Basel",
title = "Polyhydroxyalkanoate/Antifungal Polyene Formulations with Monomeric Hydroxyalkanoic Acids for Improved Antifungal Efficiency",
number = "6",
volume = "10",
doi = "10.3390/antibiotics10060737"
}

Pekmezović, M., Krusić, M. K., Malagurski, I., Milovanović, J., Stepien, K., Guzik, M., Charifou, R., Babu, R., O'Connor, K.,& Nikodinović-Runić, J.. (2021). Polyhydroxyalkanoate/Antifungal Polyene Formulations with Monomeric Hydroxyalkanoic Acids for Improved Antifungal Efficiency. in Antibiotics-Basel
MDPI, Basel., 10(6).
https://doi.org/10.3390/antibiotics10060737

Pekmezović M, Krusić MK, Malagurski I, Milovanović J, Stepien K, Guzik M, Charifou R, Babu R, O'Connor K, Nikodinović-Runić J. Polyhydroxyalkanoate/Antifungal Polyene Formulations with Monomeric Hydroxyalkanoic Acids for Improved Antifungal Efficiency. in Antibiotics-Basel. 2021;10(6).
doi:10.3390/antibiotics10060737 .

Pekmezović, Marina, Krusić, Melina Kalagasidis, Malagurski, Ivana, Milovanović, Jelena, Stepien, Karolina, Guzik, Maciej, Charifou, Romina, Babu, Ramesh, O'Connor, Kevin, Nikodinović-Runić, Jasmina, "Polyhydroxyalkanoate/Antifungal Polyene Formulations with Monomeric Hydroxyalkanoic Acids for Improved Antifungal Efficiency" in Antibiotics-Basel, 10, no. 6 (2021),
https://doi.org/10.3390/antibiotics10060737 . .

TY  - JOUR
AU  - Ferrandi, Erica E.
AU  - Spasić, Jelena
AU  - Đokić, Lidija
AU  - Vainshtein, Yevhen
AU  - Senthamaraikannan, Ramsankar
AU  - Vojnović, Sandra
AU  - Grumaz, Christian
AU  - Monti, Daniela
AU  - Nikodinović-Runić, Jasmina
PY  - 2021
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1455
AB  - Three Streptomyces sp. strains with a multitude of target enzymatic activities confirmed by functional screening, namely BV129, BV286 and BV333, were subjected to genome sequencing aiming at the annotation of genes of interest, in-depth bioinformatics characterization and functional expression of the biocatalysts. A whole-genome shotgun sequencing followed by de novo genome assembly and annotation was performed revealing genomes of 6.4, 9.4 and 7.3 Mbp, respectively. Functional annotation of the proteins of interest resulted in between 2047 and 2763 putative targets. Among the various enzymatic activities that the three Streptomyces strains demonstrated to produce by functional screening, we focused our attention on transaminases (TAs) and laccases due to their high biocatalytic potential. Bioinformatics search allowed the identification of a putative TA from Streptomyces sp. BV333 as a potentially novel broad substrate scope TA and a putative laccase from Streptomyces sp. BV286 as potentially novel blue multicopper oxidase. The two sequences were cloned and overexpressed in Escherichia coli and the two novel enzymes, transaminase Sbv333-TA and laccase Sbv286-LAC, were characterized. Interestingly, both enzymes resulted to be exceptionally thermostable, Sbv333-TA showing a melting temperature (T-M = 85 degrees C) only slightly lower compared to the T-M of the most thermostable transaminases described to date (87-88 degrees C) and Sbv286-LAC being even thermoactivated at temperature  gt 60 degrees C. Moreover, Sbv333-TA showed a broad substrate scope and remarkably demonstrated to be active in the transamination of beta-ketoesters, which are rarely accepted by currently known TAs. On the other hand, Sbv286-LAC showed an improved activity in the presence of the cosolvent acetonitrile. Overall, it was shown that a combination of approaches from standard microbiological and biochemical screens to genome sequencing and analysis is required to afford novel and functional biocatalysts.
PB  - MDPI, Basel
T2  - Catalysts
T1  - Novel Transaminase and Laccase from Streptomyces spp. Using Combined Identification Approaches
IS  - 8
VL  - 11
DO  - 10.3390/catal11080919
ER  - 

@article{
author = "Ferrandi, Erica E. and Spasić, Jelena and Đokić, Lidija and Vainshtein, Yevhen and Senthamaraikannan, Ramsankar and Vojnović, Sandra and Grumaz, Christian and Monti, Daniela and Nikodinović-Runić, Jasmina",
year = "2021",
abstract = "Three Streptomyces sp. strains with a multitude of target enzymatic activities confirmed by functional screening, namely BV129, BV286 and BV333, were subjected to genome sequencing aiming at the annotation of genes of interest, in-depth bioinformatics characterization and functional expression of the biocatalysts. A whole-genome shotgun sequencing followed by de novo genome assembly and annotation was performed revealing genomes of 6.4, 9.4 and 7.3 Mbp, respectively. Functional annotation of the proteins of interest resulted in between 2047 and 2763 putative targets. Among the various enzymatic activities that the three Streptomyces strains demonstrated to produce by functional screening, we focused our attention on transaminases (TAs) and laccases due to their high biocatalytic potential. Bioinformatics search allowed the identification of a putative TA from Streptomyces sp. BV333 as a potentially novel broad substrate scope TA and a putative laccase from Streptomyces sp. BV286 as potentially novel blue multicopper oxidase. The two sequences were cloned and overexpressed in Escherichia coli and the two novel enzymes, transaminase Sbv333-TA and laccase Sbv286-LAC, were characterized. Interestingly, both enzymes resulted to be exceptionally thermostable, Sbv333-TA showing a melting temperature (T-M = 85 degrees C) only slightly lower compared to the T-M of the most thermostable transaminases described to date (87-88 degrees C) and Sbv286-LAC being even thermoactivated at temperature  gt 60 degrees C. Moreover, Sbv333-TA showed a broad substrate scope and remarkably demonstrated to be active in the transamination of beta-ketoesters, which are rarely accepted by currently known TAs. On the other hand, Sbv286-LAC showed an improved activity in the presence of the cosolvent acetonitrile. Overall, it was shown that a combination of approaches from standard microbiological and biochemical screens to genome sequencing and analysis is required to afford novel and functional biocatalysts.",
publisher = "MDPI, Basel",
journal = "Catalysts",
title = "Novel Transaminase and Laccase from Streptomyces spp. Using Combined Identification Approaches",
number = "8",
volume = "11",
doi = "10.3390/catal11080919"
}

Ferrandi, E. E., Spasić, J., Đokić, L., Vainshtein, Y., Senthamaraikannan, R., Vojnović, S., Grumaz, C., Monti, D.,& Nikodinović-Runić, J.. (2021). Novel Transaminase and Laccase from Streptomyces spp. Using Combined Identification Approaches. in Catalysts
MDPI, Basel., 11(8).
https://doi.org/10.3390/catal11080919

Ferrandi EE, Spasić J, Đokić L, Vainshtein Y, Senthamaraikannan R, Vojnović S, Grumaz C, Monti D, Nikodinović-Runić J. Novel Transaminase and Laccase from Streptomyces spp. Using Combined Identification Approaches. in Catalysts. 2021;11(8).
doi:10.3390/catal11080919 .

Ferrandi, Erica E., Spasić, Jelena, Đokić, Lidija, Vainshtein, Yevhen, Senthamaraikannan, Ramsankar, Vojnović, Sandra, Grumaz, Christian, Monti, Daniela, Nikodinović-Runić, Jasmina, "Novel Transaminase and Laccase from Streptomyces spp. Using Combined Identification Approaches" in Catalysts, 11, no. 8 (2021),
https://doi.org/10.3390/catal11080919 . .