Kinetic modeling of lipase-catalyzed esterification reaction between oleic acid and trimethylolpropane: A simplified model for multi-substrate multi-product ping-pong mechanisms.
Bornadel, Amin LU ; Orellana Coca Åkerman, Cecilia LU ; Borg, Niklas LU ; Adlercreutz, Patrick LU
and Hatti-Kaul, Rajni
LU
(2013)
In Biotechnology Progress
29(6).
p.1422-1429
- Abstract
- Kinetic models are among the tools that can be used for optimization of biocatalytic reactions as well as for facilitating process design and upscaling in order to improve productivity and economy of these processes. Mechanism pathways for multi-substrate multi-product enzyme-catalyzed reactions can become very complex and lead to kinetic models comprising several tens of terms. Hence the models comprise too many parameters, which are in general highly correlated and their estimations are often prone to huge errors. In this study, Novozym® 435 catalyzed esterification reaction between oleic acid (OA) and trimethylolpropane (TMP) with continuous removal of side-product (water) was carried out as an example for reactions that follow... (More)
- Kinetic models are among the tools that can be used for optimization of biocatalytic reactions as well as for facilitating process design and upscaling in order to improve productivity and economy of these processes. Mechanism pathways for multi-substrate multi-product enzyme-catalyzed reactions can become very complex and lead to kinetic models comprising several tens of terms. Hence the models comprise too many parameters, which are in general highly correlated and their estimations are often prone to huge errors. In this study, Novozym® 435 catalyzed esterification reaction between oleic acid (OA) and trimethylolpropane (TMP) with continuous removal of side-product (water) was carried out as an example for reactions that follow multi-substrate multi-product ping-pong mechanisms. A kinetic model was developed based on a simplified ping-pong mechanism proposed for the reaction. The model considered both enzymatic and spontaneous reactions involved and also the effect of product removal during the reaction. The kinetic model parameters were estimated using nonlinear curve fitting through unconstrained optimization methodology and the model was verified by using empirical data from different experiments and showed good predictability of the reaction under different conditions. This approach can be applied to similar biocatalytic processes to facilitate their optimization and design. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4066183
- author
- Bornadel, Amin
LU
; Orellana Coca Åkerman, Cecilia
LU
; Borg, Niklas
LU
; Adlercreutz, Patrick
LU
and Hatti-Kaul, Rajni
LU
- organization
- publishing date
- 2013
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Biocatalytic processes, NovozymVR 435, substituted-enzyme mechanism, side-product removal, nonlinear curve fitting
- in
- Biotechnology Progress
- volume
- 29
- issue
- 6
- pages
- 1422 - 1429
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000328217100009
- pmid:24013935
- scopus:84890187681
- pmid:24013935
- ISSN
- 1520-6033
- DOI
- 10.1002/btpr.1806
- language
- English
- LU publication?
- yes
- id
- 89598b13-c797-4caa-823c-7729696d9bc8 (old id 4066183)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/24013935?dopt=Abstract
- date added to LUP
- 2016-04-01 10:42:05
- date last changed
- 2023-11-10 03:03:28
@article{89598b13-c797-4caa-823c-7729696d9bc8,
abstract = {{Kinetic models are among the tools that can be used for optimization of biocatalytic reactions as well as for facilitating process design and upscaling in order to improve productivity and economy of these processes. Mechanism pathways for multi-substrate multi-product enzyme-catalyzed reactions can become very complex and lead to kinetic models comprising several tens of terms. Hence the models comprise too many parameters, which are in general highly correlated and their estimations are often prone to huge errors. In this study, Novozym® 435 catalyzed esterification reaction between oleic acid (OA) and trimethylolpropane (TMP) with continuous removal of side-product (water) was carried out as an example for reactions that follow multi-substrate multi-product ping-pong mechanisms. A kinetic model was developed based on a simplified ping-pong mechanism proposed for the reaction. The model considered both enzymatic and spontaneous reactions involved and also the effect of product removal during the reaction. The kinetic model parameters were estimated using nonlinear curve fitting through unconstrained optimization methodology and the model was verified by using empirical data from different experiments and showed good predictability of the reaction under different conditions. This approach can be applied to similar biocatalytic processes to facilitate their optimization and design.}},
author = {{Bornadel, Amin and Orellana Coca Åkerman, Cecilia and Borg, Niklas and Adlercreutz, Patrick and Hatti-Kaul, Rajni}},
issn = {{1520-6033}},
keywords = {{Biocatalytic processes; NovozymVR 435; substituted-enzyme mechanism; side-product removal; nonlinear curve fitting}},
language = {{eng}},
number = {{6}},
pages = {{1422--1429}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Biotechnology Progress}},
title = {{Kinetic modeling of lipase-catalyzed esterification reaction between oleic acid and trimethylolpropane: A simplified model for multi-substrate multi-product ping-pong mechanisms.}},
url = {{http://dx.doi.org/10.1002/btpr.1806}},
doi = {{10.1002/btpr.1806}},
volume = {{29}},
year = {{2013}},
}