Removal of N-terminal peptides from β-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation
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2009
Authors
Stanić, Dragana
Radosavljevic, J.
Polović, Natalija

Jadranin, Milka

Popović, M.
Vuckovic, O.
Burazer, L.
Jankov, R.
Ćirković Veličković, Tanja

Article (Published version)

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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.
Source:
International Dairy Journal, 2009, 19, 12, 746-752Funding / projects:
- Ispitivanje strukture i funkcije biološki važnih makromolekula u fiziološkim i patološkim stanjima (RS-142020)
DOI: 10.1016/j.idairyj.2009.05.008
ISSN: 0958-6946
WoS: 000270752800006
Scopus: 2-s2.0-69949182410
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IHTMTY - 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 . .