Kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin C ester
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 subs...
Published in: | Biochemical Engineering Journal |
---|---|
Main Authors: | , , , , , , |
Format: | Article in Journal/Newspaper |
Language: | unknown |
Published: |
Elsevier Science Sa, Lausanne
2013
|
Subjects: | |
Online Access: | http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2550 https://doi.org/10.1016/j.bej.2012.12.001 |
id |
ftunivbelgradftm:oai:TechnoRep.tmf.bg.ac.rs:123456789/2550 |
---|---|
record_format |
openpolar |
spelling |
ftunivbelgradftm:oai:TechnoRep.tmf.bg.ac.rs:123456789/2550 2023-12-24T10:08:54+01:00 Kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin C ester Bezbradica, Dejan Stojanović, Marija Veličković, Dušan Dimitrijević, Aleksandra Carević, Milica Mihailović, Mladen Milosavić, Nenad 2013 http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2550 https://doi.org/10.1016/j.bej.2012.12.001 unknown Elsevier Science Sa, Lausanne info:eu-repo/grantAgreement/MESTD/Integrated and Interdisciplinary Research (IIR or III)/46010/RS// 1369-703X http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2550 doi:10.1016/j.bej.2012.12.001 2-s2.0-84872407885 000315016800012 restrictedAccess ARR Biochemical Engineering Journal Ascorbyl oleate Lipase Candida antarctica Kinetic parameters Substrate inhibition Production kinetics article publishedVersion 2013 ftunivbelgradftm https://doi.org/10.1016/j.bej.2012.12.001 2023-11-28T17:19:52Z 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. Article in Journal/Newspaper Antarc* Antarctica TechnoRep - Faculty of Technology and Metallurgy Repository Biochemical Engineering Journal 71 89 96 |
institution |
Open Polar |
collection |
TechnoRep - Faculty of Technology and Metallurgy Repository |
op_collection_id |
ftunivbelgradftm |
language |
unknown |
topic |
Ascorbyl oleate Lipase Candida antarctica Kinetic parameters Substrate inhibition Production kinetics |
spellingShingle |
Ascorbyl oleate Lipase Candida antarctica Kinetic parameters Substrate inhibition Production kinetics 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 |
topic_facet |
Ascorbyl oleate Lipase Candida antarctica Kinetic parameters Substrate inhibition Production kinetics |
description |
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. |
format |
Article in Journal/Newspaper |
author |
Bezbradica, Dejan Stojanović, Marija Veličković, Dušan Dimitrijević, Aleksandra Carević, Milica Mihailović, Mladen Milosavić, Nenad |
author_facet |
Bezbradica, Dejan Stojanović, Marija Veličković, Dušan Dimitrijević, Aleksandra Carević, Milica Mihailović, Mladen Milosavić, Nenad |
author_sort |
Bezbradica, Dejan |
title |
Kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin C ester |
title_short |
Kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin C ester |
title_full |
Kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin C ester |
title_fullStr |
Kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin C ester |
title_full_unstemmed |
Kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin C ester |
title_sort |
kinetic model of lipase-catalyzed conversion of ascorbic acid and oleic acid to liposoluble vitamin c ester |
publisher |
Elsevier Science Sa, Lausanne |
publishDate |
2013 |
url |
http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2550 https://doi.org/10.1016/j.bej.2012.12.001 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Biochemical Engineering Journal |
op_relation |
info:eu-repo/grantAgreement/MESTD/Integrated and Interdisciplinary Research (IIR or III)/46010/RS// 1369-703X http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2550 doi:10.1016/j.bej.2012.12.001 2-s2.0-84872407885 000315016800012 |
op_rights |
restrictedAccess ARR |
op_doi |
https://doi.org/10.1016/j.bej.2012.12.001 |
container_title |
Biochemical Engineering Journal |
container_volume |
71 |
container_start_page |
89 |
op_container_end_page |
96 |
_version_ |
1786204710144835584 |