The kinetics of L-ascorbyl oleate synthesis catalyzed by immobilized lipase from Candida antarctica in acetone was investigated. Significant inhibition of synthesis with an excess of ascorbic acid was observed. Experimental data were successfully fitted with a ping-pong bi-bi kinetic model with substrate inhibition, and related kinetic constants were determined. The kinetic study was performed at optimum experimental factors (temperature, initial water content, and enzyme concentration), which were determined using response surface methodology. Then, a model for predicting product-time progress curves was developed by expanding the obtained ping-pang model with terms describing ester hydrolysis. Kinetic constants of the reverse reaction were determined, and good congruence between the model and experimental data was achieved. Calculated kinetic constants revealed that lipase has the highest affinity for ascorbyl oleate, slightly lower activity with ascorbic acid, and the lowest activit...y with oleic acid. The obtained results are valuable for elucidating the reaction mechanism and represent an important contribution for reaction optimization and creating strategies to increase the productivity of vitamin C ester synthesis.
TY - JOUR
AU - Bezbradica, Dejan
AU - Stojanović, Marija
AU - Veličković, Dušan
AU - Dimitrijević, Aleksandra
AU - Carević, Milica
AU - Mihailović, Mladen
AU - Milosavić, Nenad
PY - 2013
UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2550
AB - The kinetics of L-ascorbyl oleate synthesis catalyzed by immobilized lipase from Candida antarctica in acetone was investigated. Significant inhibition of synthesis with an excess of ascorbic acid was observed. Experimental data were successfully fitted with a ping-pong bi-bi kinetic model with substrate inhibition, and related kinetic constants were determined. The kinetic study was performed at optimum experimental factors (temperature, initial water content, and enzyme concentration), which were determined using response surface methodology. Then, a model for predicting product-time progress curves was developed by expanding the obtained ping-pang model with terms describing ester hydrolysis. Kinetic constants of the reverse reaction were determined, and good congruence between the model and experimental data was achieved. Calculated kinetic constants revealed that lipase has the highest affinity for ascorbyl oleate, slightly lower activity with ascorbic acid, and the lowest activity with oleic acid. The obtained results are valuable for elucidating the reaction mechanism and represent an important contribution for reaction optimization and creating strategies to increase the productivity of vitamin C ester synthesis.
PB - Elsevier Science Sa, Lausanne
T2 - Biochemical Engineering Journal
T1 - Kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin C ester
EP - 96
SP - 89
VL - 71
DO - 10.1016/j.bej.2012.12.001
ER -
@article{
author = "Bezbradica, Dejan and Stojanović, Marija and Veličković, Dušan and Dimitrijević, Aleksandra and Carević, Milica and Mihailović, Mladen and Milosavić, Nenad",
year = "2013",
abstract = "The kinetics of L-ascorbyl oleate synthesis catalyzed by immobilized lipase from Candida antarctica in acetone was investigated. Significant inhibition of synthesis with an excess of ascorbic acid was observed. Experimental data were successfully fitted with a ping-pong bi-bi kinetic model with substrate inhibition, and related kinetic constants were determined. The kinetic study was performed at optimum experimental factors (temperature, initial water content, and enzyme concentration), which were determined using response surface methodology. Then, a model for predicting product-time progress curves was developed by expanding the obtained ping-pang model with terms describing ester hydrolysis. Kinetic constants of the reverse reaction were determined, and good congruence between the model and experimental data was achieved. Calculated kinetic constants revealed that lipase has the highest affinity for ascorbyl oleate, slightly lower activity with ascorbic acid, and the lowest activity with oleic acid. The obtained results are valuable for elucidating the reaction mechanism and represent an important contribution for reaction optimization and creating strategies to increase the productivity of vitamin C ester synthesis.",
publisher = "Elsevier Science Sa, Lausanne",
journal = "Biochemical Engineering Journal",
title = "Kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin C ester",
pages = "96-89",
volume = "71",
doi = "10.1016/j.bej.2012.12.001"
}
Bezbradica, D., Stojanović, M., Veličković, D., Dimitrijević, A., Carević, M., Mihailović, M.,& Milosavić, N.. (2013). Kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin C ester. in Biochemical Engineering Journal
Elsevier Science Sa, Lausanne., 71, 89-96.
https://doi.org/10.1016/j.bej.2012.12.001
Bezbradica D, Stojanović M, Veličković D, Dimitrijević A, Carević M, Mihailović M, Milosavić N. Kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin C ester. in Biochemical Engineering Journal. 2013;71:89-96.
doi:10.1016/j.bej.2012.12.001 .
Bezbradica, Dejan, Stojanović, Marija, Veličković, Dušan, Dimitrijević, Aleksandra, Carević, Milica, Mihailović, Mladen, Milosavić, Nenad, "Kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin C ester" in Biochemical Engineering Journal, 71 (2013):89-96,
https://doi.org/10.1016/j.bej.2012.12.001 . .
