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.
TY - 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 . .
