Comparative stability of ficin and papain in acidic conditions and the presence of ethanol
Samo za registrovane korisnike
2019
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
Proteolytic enzymes are used for proteolysis and peptide synthesis which can be run in various conditions including low pH value and the presence of ethanol. The most common cysteine protease applied in acidic-alcoholic conditions is well-characterized papain. Ficin, which is closely related to papain in terms of proteolytic activity and substrate specificity, could potentially be applied in the alcoholic beverage industry and peptide synthesis. The aim of this study was to compare papain and ficin stability in process conditions. Comparative stability study showed that ficin as a mixture of different isoforms has a broader range of stability in respect of pH and cold storage stability, in comparison to papain. It retains about 70% of initial activity after 3-week cold storage at low pH and in the presence of ethanol. Unlike ficin, papain loses about 70% of initial activity in the same incubation period as it is more prone to non-native aggregation that was confirmed by FTIR analysis. ...The presence of multiple isoforms of ficin stabilizes the protease against cold denaturation and aggregation, making it more suitable for biotechnological and laboratory usage than single papain isoform. It is more cold-stable in alcoholic-acidic and acidic conditions suggesting possible replacement of papain with even lower enzyme concentration.
Ključne reči:
Acidic conditions / Cold stability / Ethanol / Ficin / Papain / Acids / Ficain / Humans / Hydrogen-Ion Concentration / Kinetics / Protein StabilityIzvor:
Amino Acids, 2019, 51, 5, 829-838Izdavač:
- Springer
Finansiranje / projekti:
- Alergeni, antitela, enzimi i mali fiziološki značajni molekuli: dizajn, struktura, funkcija i značaj (RS-MESTD-Basic Research (BR or ON)-172049)
Napomena:
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3933
DOI: 10.1007/s00726-019-02724-3
ISSN: 1438-2199
WoS: 000465375900008
Scopus: 2-s2.0-85063086804
Kolekcije
Institucija/grupa
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Milošević, Jelica AU - Janković, Brankica AU - Prodanović, Radivoje AU - Polović, Natalija PY - 2019 UR - https://cherry.chem.bg.ac.rs/handle/123456789/3932 AB - Proteolytic enzymes are used for proteolysis and peptide synthesis which can be run in various conditions including low pH value and the presence of ethanol. The most common cysteine protease applied in acidic-alcoholic conditions is well-characterized papain. Ficin, which is closely related to papain in terms of proteolytic activity and substrate specificity, could potentially be applied in the alcoholic beverage industry and peptide synthesis. The aim of this study was to compare papain and ficin stability in process conditions. Comparative stability study showed that ficin as a mixture of different isoforms has a broader range of stability in respect of pH and cold storage stability, in comparison to papain. It retains about 70% of initial activity after 3-week cold storage at low pH and in the presence of ethanol. Unlike ficin, papain loses about 70% of initial activity in the same incubation period as it is more prone to non-native aggregation that was confirmed by FTIR analysis. The presence of multiple isoforms of ficin stabilizes the protease against cold denaturation and aggregation, making it more suitable for biotechnological and laboratory usage than single papain isoform. It is more cold-stable in alcoholic-acidic and acidic conditions suggesting possible replacement of papain with even lower enzyme concentration. PB - Springer T2 - Amino Acids T1 - Comparative stability of ficin and papain in acidic conditions and the presence of ethanol VL - 51 IS - 5 SP - 829 EP - 838 DO - 10.1007/s00726-019-02724-3 ER -
@article{ author = "Milošević, Jelica and Janković, Brankica and Prodanović, Radivoje and Polović, Natalija", year = "2019", abstract = "Proteolytic enzymes are used for proteolysis and peptide synthesis which can be run in various conditions including low pH value and the presence of ethanol. The most common cysteine protease applied in acidic-alcoholic conditions is well-characterized papain. Ficin, which is closely related to papain in terms of proteolytic activity and substrate specificity, could potentially be applied in the alcoholic beverage industry and peptide synthesis. The aim of this study was to compare papain and ficin stability in process conditions. Comparative stability study showed that ficin as a mixture of different isoforms has a broader range of stability in respect of pH and cold storage stability, in comparison to papain. It retains about 70% of initial activity after 3-week cold storage at low pH and in the presence of ethanol. Unlike ficin, papain loses about 70% of initial activity in the same incubation period as it is more prone to non-native aggregation that was confirmed by FTIR analysis. The presence of multiple isoforms of ficin stabilizes the protease against cold denaturation and aggregation, making it more suitable for biotechnological and laboratory usage than single papain isoform. It is more cold-stable in alcoholic-acidic and acidic conditions suggesting possible replacement of papain with even lower enzyme concentration.", publisher = "Springer", journal = "Amino Acids", title = "Comparative stability of ficin and papain in acidic conditions and the presence of ethanol", volume = "51", number = "5", pages = "829-838", doi = "10.1007/s00726-019-02724-3" }
Milošević, J., Janković, B., Prodanović, R.,& Polović, N.. (2019). Comparative stability of ficin and papain in acidic conditions and the presence of ethanol. in Amino Acids Springer., 51(5), 829-838. https://doi.org/10.1007/s00726-019-02724-3
Milošević J, Janković B, Prodanović R, Polović N. Comparative stability of ficin and papain in acidic conditions and the presence of ethanol. in Amino Acids. 2019;51(5):829-838. doi:10.1007/s00726-019-02724-3 .
Milošević, Jelica, Janković, Brankica, Prodanović, Radivoje, Polović, Natalija, "Comparative stability of ficin and papain in acidic conditions and the presence of ethanol" in Amino Acids, 51, no. 5 (2019):829-838, https://doi.org/10.1007/s00726-019-02724-3 . .