Optimization of the Enzymatic Synthesis of Pentyl Oleate with Lipase Immobilized onto Novel Structured Support

The term biorefinery is related to the sustainable production of value-added bioproducts and bioenergy from biomass. Esters from fatty acids are important compounds synthesized from by-products of the oleochemical industry. In agreement with the biorefinery concept, it is important to search for cat...

Full description

Bibliographic Details
Published in:Fermentation
Main Authors: Valeria Cavallaro, Gabriela Tonetto, María Luján Ferreira
Format: Text
Language:English
Published: Multidisciplinary Digital Publishing Institute 2019
Subjects:
RSM
Online Access:https://doi.org/10.3390/fermentation5020048
id ftmdpi:oai:mdpi.com:/2311-5637/5/2/48/
record_format openpolar
spelling ftmdpi:oai:mdpi.com:/2311-5637/5/2/48/ 2023-08-20T04:01:51+02:00 Optimization of the Enzymatic Synthesis of Pentyl Oleate with Lipase Immobilized onto Novel Structured Support Valeria Cavallaro Gabriela Tonetto María Luján Ferreira agris 2019-06-14 application/pdf https://doi.org/10.3390/fermentation5020048 EN eng Multidisciplinary Digital Publishing Institute Fermentation Process Design https://dx.doi.org/10.3390/fermentation5020048 https://creativecommons.org/licenses/by/4.0/ Fermentation; Volume 5; Issue 2; Pages: 48 biorefinery RSM CALB esterification enzyme inhibition ping-pong bi-bi mechanism Text 2019 ftmdpi https://doi.org/10.3390/fermentation5020048 2023-07-31T22:21:23Z The term biorefinery is related to the sustainable production of value-added bioproducts and bioenergy from biomass. Esters from fatty acids are important compounds synthesized from by-products of the oleochemical industry. In agreement with the biorefinery concept, it is important to search for catalysts that reduce the consumption of energy and water, using moderate operation conditions and low reaction times. In this work, response surface methodology (RSM) was used to optimize the enzymatic synthesis of pentyl oleate using Candida antarctica lipase B (CALB) immobilized on a polyethylene-aluminum structured support. A factorial design was employed to evaluate the effects of several parameters on the ester yield. To obtain a model with a good fit, an approach to reaction mechanism and enzyme kinetics was taken into consideration. Experimental findings were correlated and explained using equations of a ping-pong bi-bi kinetic model and considering the inhibitory effects of both substrates. The developed model was consistent with the experimental data predicting an increase in pentyl oleate production with increasing temperature and a decrease with higher oleic acid amounts and alcohol to acid molar ratios. This model could be useful in a future industrial application of CALB/LLDPE/Al to minimize the costs in oleochemical biorefineries. Text Antarc* Antarctica MDPI Open Access Publishing Fermentation 5 2 48
institution Open Polar
collection MDPI Open Access Publishing
op_collection_id ftmdpi
language English
topic biorefinery
RSM
CALB
esterification
enzyme inhibition
ping-pong bi-bi mechanism
spellingShingle biorefinery
RSM
CALB
esterification
enzyme inhibition
ping-pong bi-bi mechanism
Valeria Cavallaro
Gabriela Tonetto
María Luján Ferreira
Optimization of the Enzymatic Synthesis of Pentyl Oleate with Lipase Immobilized onto Novel Structured Support
topic_facet biorefinery
RSM
CALB
esterification
enzyme inhibition
ping-pong bi-bi mechanism
description The term biorefinery is related to the sustainable production of value-added bioproducts and bioenergy from biomass. Esters from fatty acids are important compounds synthesized from by-products of the oleochemical industry. In agreement with the biorefinery concept, it is important to search for catalysts that reduce the consumption of energy and water, using moderate operation conditions and low reaction times. In this work, response surface methodology (RSM) was used to optimize the enzymatic synthesis of pentyl oleate using Candida antarctica lipase B (CALB) immobilized on a polyethylene-aluminum structured support. A factorial design was employed to evaluate the effects of several parameters on the ester yield. To obtain a model with a good fit, an approach to reaction mechanism and enzyme kinetics was taken into consideration. Experimental findings were correlated and explained using equations of a ping-pong bi-bi kinetic model and considering the inhibitory effects of both substrates. The developed model was consistent with the experimental data predicting an increase in pentyl oleate production with increasing temperature and a decrease with higher oleic acid amounts and alcohol to acid molar ratios. This model could be useful in a future industrial application of CALB/LLDPE/Al to minimize the costs in oleochemical biorefineries.
format Text
author Valeria Cavallaro
Gabriela Tonetto
María Luján Ferreira
author_facet Valeria Cavallaro
Gabriela Tonetto
María Luján Ferreira
author_sort Valeria Cavallaro
title Optimization of the Enzymatic Synthesis of Pentyl Oleate with Lipase Immobilized onto Novel Structured Support
title_short Optimization of the Enzymatic Synthesis of Pentyl Oleate with Lipase Immobilized onto Novel Structured Support
title_full Optimization of the Enzymatic Synthesis of Pentyl Oleate with Lipase Immobilized onto Novel Structured Support
title_fullStr Optimization of the Enzymatic Synthesis of Pentyl Oleate with Lipase Immobilized onto Novel Structured Support
title_full_unstemmed Optimization of the Enzymatic Synthesis of Pentyl Oleate with Lipase Immobilized onto Novel Structured Support
title_sort optimization of the enzymatic synthesis of pentyl oleate with lipase immobilized onto novel structured support
publisher Multidisciplinary Digital Publishing Institute
publishDate 2019
url https://doi.org/10.3390/fermentation5020048
op_coverage agris
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source Fermentation; Volume 5; Issue 2; Pages: 48
op_relation Fermentation Process Design
https://dx.doi.org/10.3390/fermentation5020048
op_rights https://creativecommons.org/licenses/by/4.0/
op_doi https://doi.org/10.3390/fermentation5020048
container_title Fermentation
container_volume 5
container_issue 2
container_start_page 48
_version_ 1774712220833284096