Isolation, identification, and stability of Ficin 1c isoform from fig latex
Само за регистроване кориснике
2020
Аутори
Milošević, JelicaVrhovac, Lidija
Đurković, Filip T.
Janković, Brankica
Malkov, Saša
Lah, Jurij
Polović, Natalija
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Latex of common fig (Ficus carica) is a rich protein source with a high level of proteolytic activity contributing to its defensive role. The divergent group of cysteine proteases known as ficin (EC 3.4.22.3) represents the majority of latex protein content and shows activity towards fig parasites. Both classical and novel biochemical techniques suggest the intricate pattern of ficin expression and activity profiles. Even though structurally related, different ficin isoforms show some differences in pI values enabling their separation using ion-exchangers. A single alkaline isoform was purified and identified based on the available transcriptomic data as Ficin 1c. This isoform shows both general proteolytic and gelatinolytic activity suggesting a biological role in the degradation of a broad range of natural substrates. The insight into the Ficin 1c structure also provided some functional clues. The secondary structure content and the overall fold are similar to related proteases of th...e same and other plant sources resulting in similar unfolding routes. Stability assessment of Ficin 1c in comparison to ficin isoform mixture showed that isoform diversity might lead to increased protease stability.
Извор:
New Journal of Chemistry, 2020, 44, 36, 15716-15723Издавач:
- Royal Society of Chemistry
Финансирање / пројекти:
Напомена:
- The peer-reviewed version: https://cherry.chem.bg.ac.rs/handle/123456789/4265
DOI: 10.1039/D0NJ02938F
ISSN: 1144-0546
WoS: 000571972400046
Scopus: 2-s2.0-85092756551
Колекције
Институција/група
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Milošević, Jelica AU - Vrhovac, Lidija AU - Đurković, Filip T. AU - Janković, Brankica AU - Malkov, Saša AU - Lah, Jurij AU - Polović, Natalija PY - 2020 UR - https://cherry.chem.bg.ac.rs/handle/123456789/4264 AB - Latex of common fig (Ficus carica) is a rich protein source with a high level of proteolytic activity contributing to its defensive role. The divergent group of cysteine proteases known as ficin (EC 3.4.22.3) represents the majority of latex protein content and shows activity towards fig parasites. Both classical and novel biochemical techniques suggest the intricate pattern of ficin expression and activity profiles. Even though structurally related, different ficin isoforms show some differences in pI values enabling their separation using ion-exchangers. A single alkaline isoform was purified and identified based on the available transcriptomic data as Ficin 1c. This isoform shows both general proteolytic and gelatinolytic activity suggesting a biological role in the degradation of a broad range of natural substrates. The insight into the Ficin 1c structure also provided some functional clues. The secondary structure content and the overall fold are similar to related proteases of the same and other plant sources resulting in similar unfolding routes. Stability assessment of Ficin 1c in comparison to ficin isoform mixture showed that isoform diversity might lead to increased protease stability. PB - Royal Society of Chemistry T2 - New Journal of Chemistry T1 - Isolation, identification, and stability of Ficin 1c isoform from fig latex VL - 44 IS - 36 SP - 15716 EP - 15723 DO - 10.1039/D0NJ02938F ER -
@article{ author = "Milošević, Jelica and Vrhovac, Lidija and Đurković, Filip T. and Janković, Brankica and Malkov, Saša and Lah, Jurij and Polović, Natalija", year = "2020", abstract = "Latex of common fig (Ficus carica) is a rich protein source with a high level of proteolytic activity contributing to its defensive role. The divergent group of cysteine proteases known as ficin (EC 3.4.22.3) represents the majority of latex protein content and shows activity towards fig parasites. Both classical and novel biochemical techniques suggest the intricate pattern of ficin expression and activity profiles. Even though structurally related, different ficin isoforms show some differences in pI values enabling their separation using ion-exchangers. A single alkaline isoform was purified and identified based on the available transcriptomic data as Ficin 1c. This isoform shows both general proteolytic and gelatinolytic activity suggesting a biological role in the degradation of a broad range of natural substrates. The insight into the Ficin 1c structure also provided some functional clues. The secondary structure content and the overall fold are similar to related proteases of the same and other plant sources resulting in similar unfolding routes. Stability assessment of Ficin 1c in comparison to ficin isoform mixture showed that isoform diversity might lead to increased protease stability.", publisher = "Royal Society of Chemistry", journal = "New Journal of Chemistry", title = "Isolation, identification, and stability of Ficin 1c isoform from fig latex", volume = "44", number = "36", pages = "15716-15723", doi = "10.1039/D0NJ02938F" }
Milošević, J., Vrhovac, L., Đurković, F. T., Janković, B., Malkov, S., Lah, J.,& Polović, N.. (2020). Isolation, identification, and stability of Ficin 1c isoform from fig latex. in New Journal of Chemistry Royal Society of Chemistry., 44(36), 15716-15723. https://doi.org/10.1039/D0NJ02938F
Milošević J, Vrhovac L, Đurković FT, Janković B, Malkov S, Lah J, Polović N. Isolation, identification, and stability of Ficin 1c isoform from fig latex. in New Journal of Chemistry. 2020;44(36):15716-15723. doi:10.1039/D0NJ02938F .
Milošević, Jelica, Vrhovac, Lidija, Đurković, Filip T., Janković, Brankica, Malkov, Saša, Lah, Jurij, Polović, Natalija, "Isolation, identification, and stability of Ficin 1c isoform from fig latex" in New Journal of Chemistry, 44, no. 36 (2020):15716-15723, https://doi.org/10.1039/D0NJ02938F . .