Potato juice (a waste product from the starch industry) is a potential source of novel enzymes for food applications. For use in the production and improvement of food protein hydrolysates, commercially available exopeptidases, predominantly aminopeptidases, are recommended. The present study was performed to explore possible biotechnological interest of leucyl aminopeptidase (LAP) activity in the potato tuber. The LAP from potato tuber was purified and characterised. Specific LAP activity was increased 200-fold by purification of the crude extract. The purified enzyme had a pH optimum of 9.0 and temperature optimum of 45 degrees C. LAP hydrolysed leucine-, alanine- and lysine-p-nitroanilide to a similar degree. The most efficient inhibitor was 1,10-phenanthroline. Almost all divalent cations tested inhibited the enzyme activity, while Co2+ stimulated LAP activity by over 100%. The purified LAP had a molecular weight of 90 kDa with an isoelectric point of 5.45. Sodium dodecylsulfate-po...lyacrylamide gel electrophoresis revealed one band of 48 kDa.
TY - JOUR
AU - Vujčić, Zoran
AU - Lončar, Nikola
AU - Dojnov, Biljana
AU - Milovanović, Aleksandra
AU - Vujčić, Miroslava
AU - Božić, Nataša
PY - 2010
UR - http://cer.ihtm.bg.ac.rs/handle/123456789/698
AB - Potato juice (a waste product from the starch industry) is a potential source of novel enzymes for food applications. For use in the production and improvement of food protein hydrolysates, commercially available exopeptidases, predominantly aminopeptidases, are recommended. The present study was performed to explore possible biotechnological interest of leucyl aminopeptidase (LAP) activity in the potato tuber. The LAP from potato tuber was purified and characterised. Specific LAP activity was increased 200-fold by purification of the crude extract. The purified enzyme had a pH optimum of 9.0 and temperature optimum of 45 degrees C. LAP hydrolysed leucine-, alanine- and lysine-p-nitroanilide to a similar degree. The most efficient inhibitor was 1,10-phenanthroline. Almost all divalent cations tested inhibited the enzyme activity, while Co2+ stimulated LAP activity by over 100%. The purified LAP had a molecular weight of 90 kDa with an isoelectric point of 5.45. Sodium dodecylsulfate-polyacrylamide gel electrophoresis revealed one band of 48 kDa.
PB - Elsevier Sci Ltd, Oxford
T2 - Food Chemistry
T1 - Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber
VL - 121
IS - 2
SP - 418
EP - 423
DO - 10.1016/j.foodchem.2009.12.058
ER -
@article{
author = "Vujčić, Zoran and Lončar, Nikola and Dojnov, Biljana and Milovanović, Aleksandra and Vujčić, Miroslava and Božić, Nataša",
year = "2010",
url = "http://cer.ihtm.bg.ac.rs/handle/123456789/698",
abstract = "Potato juice (a waste product from the starch industry) is a potential source of novel enzymes for food applications. For use in the production and improvement of food protein hydrolysates, commercially available exopeptidases, predominantly aminopeptidases, are recommended. The present study was performed to explore possible biotechnological interest of leucyl aminopeptidase (LAP) activity in the potato tuber. The LAP from potato tuber was purified and characterised. Specific LAP activity was increased 200-fold by purification of the crude extract. The purified enzyme had a pH optimum of 9.0 and temperature optimum of 45 degrees C. LAP hydrolysed leucine-, alanine- and lysine-p-nitroanilide to a similar degree. The most efficient inhibitor was 1,10-phenanthroline. Almost all divalent cations tested inhibited the enzyme activity, while Co2+ stimulated LAP activity by over 100%. The purified LAP had a molecular weight of 90 kDa with an isoelectric point of 5.45. Sodium dodecylsulfate-polyacrylamide gel electrophoresis revealed one band of 48 kDa.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber",
volume = "121",
number = "2",
pages = "418-423",
doi = "10.1016/j.foodchem.2009.12.058"
}
Vujčić, Z., Lončar, N., Dojnov, B., Milovanović, A., Vujčić, M.,& Božić, N. (2010). Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber.
Food Chemistry
Elsevier Sci Ltd, Oxford., 121(2), 418-423.
https://doi.org/10.1016/j.foodchem.2009.12.058
Vujčić Z, Lončar N, Dojnov B, Milovanović A, Vujčić M, Božić N. Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber. Food Chemistry. 2010;121(2):418-423
