TY  - JOUR
AU  - Stanić, Dragana
AU  - Radosavljevic, J.
AU  - Polović, Natalija
AU  - Jadranin, Milka
AU  - Popović, M.
AU  - Vuckovic, O.
AU  - Burazer, L.
AU  - Jankov, R.
AU  - Ćirković Veličković, Tanja
PY  - 2009
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/608
AB  - The use of enzymes may improve the functional properties of various food ingredients. The aim of this study was to examine the effects of proteolytic contaminants in phenol oxidases on β-lactoglobulin (BLG). In the presence of Trametes versicolor laccase and Agaricus bisporus tyrosinase, both variants of BLG (A and B) underwent removal of a peptide from the N-terminus. The truncated forms were more susceptible to digestion by pepsin. The truncation of BLG resulted from contaminating proteases and not due to the action of phenol oxidases. The removal of N-terminal peptides proceeded quickly, while the rest of the globular protein remained resistant to proteolysis for up to 3 h. In the case of the application of enzymes in food bioprocessing, it may be important to carefully monitor the effects of contaminating proteases in enzyme preparations used.
T2  - International Dairy Journal
T1  - Removal of N-terminal peptides from β-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation
VL  - 19
IS  - 12
SP  - 746
EP  - 752
DO  - 10.1016/j.idairyj.2009.05.008
ER  - 

@article{
author = "Stanić, Dragana and Radosavljevic, J. and Polović, Natalija and Jadranin, Milka and Popović, M. and Vuckovic, O. and Burazer, L. and Jankov, R. and Ćirković Veličković, Tanja",
year = "2009",
abstract = "The use of enzymes may improve the functional properties of various food ingredients. The aim of this study was to examine the effects of proteolytic contaminants in phenol oxidases on β-lactoglobulin (BLG). In the presence of Trametes versicolor laccase and Agaricus bisporus tyrosinase, both variants of BLG (A and B) underwent removal of a peptide from the N-terminus. The truncated forms were more susceptible to digestion by pepsin. The truncation of BLG resulted from contaminating proteases and not due to the action of phenol oxidases. The removal of N-terminal peptides proceeded quickly, while the rest of the globular protein remained resistant to proteolysis for up to 3 h. In the case of the application of enzymes in food bioprocessing, it may be important to carefully monitor the effects of contaminating proteases in enzyme preparations used.",
journal = "International Dairy Journal",
title = "Removal of N-terminal peptides from β-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation",
volume = "19",
number = "12",
pages = "746-752",
doi = "10.1016/j.idairyj.2009.05.008"
}

Stanić, D., Radosavljevic, J., Polović, N., Jadranin, M., Popović, M., Vuckovic, O., Burazer, L., Jankov, R.,& Ćirković Veličković, T.. (2009). Removal of N-terminal peptides from β-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation. in International Dairy Journal, 19(12), 746-752.
https://doi.org/10.1016/j.idairyj.2009.05.008

Stanić D, Radosavljevic J, Polović N, Jadranin M, Popović M, Vuckovic O, Burazer L, Jankov R, Ćirković Veličković T. Removal of N-terminal peptides from β-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation. in International Dairy Journal. 2009;19(12):746-752.
doi:10.1016/j.idairyj.2009.05.008 .

Stanić, Dragana, Radosavljevic, J., Polović, Natalija, Jadranin, Milka, Popović, M., Vuckovic, O., Burazer, L., Jankov, R., Ćirković Veličković, Tanja, "Removal of N-terminal peptides from β-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation" in International Dairy Journal, 19, no. 12 (2009):746-752,
https://doi.org/10.1016/j.idairyj.2009.05.008 . .