Comparison of the lipase activity in hydrolysis and acyl transfer reactions of two latex plant extracts from babaco (Vasconcellea x Heilbornii Cv.) and Plumeria rubra : Effect of the aqueous microenvironment
The enzymatic properties of Plumeria rubra latex have been evaluated for the first time, showing a high activity in both hydrolysis and synthesis reactions, and compared to the biocatalytic behavior of babaco (Vasconcellea x Heilbornii cv.) latex. Both biocatalysts have been optimized by studying the various parameters that influence reaction kinetics. The optimum temperatures for hydrolysis reactions were 50 and 55°C for babaco and Plumeria, respectively. The optimum pH for babaco latex was 7, whereas for Plumeria latex, two optimal pH values (4 and 7) were observed. With regard to esterification and acyl transfer reactions such as alcoholysis and interesterification, the influence of thermodynamic water activity on reaction yields was determined and correlated with water sorption and desorption isotherms. When babaco latex is used as a biocatalyst, optimal synthesis reaction yields are obtained when the enzymatic extract is stabilized at a water activity value of 0.38, which corresponds to a water content of 5.7%. This optimal level of hydration is located on the linear portion of the biocatalyst's sorption isotherm, where the water molecules exhibit high-energy interactions with the protein network. In synthesis reactions (esterification, alcoholysis, and interesterification) biocatalyzed by Plumeria latex, correlation between best reaction yields and water activity cannot be done. Indeed, the sorption isotherm plot has an atypical shape, indicating that water might be trapped in the latex matrix and, consequently, that the water content of the biocatalyst is highly dependent on the hydration history of the latex.
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Language: | eng |
Subjects: | Q60 - Traitement des produits agricoles non alimentaires, latex, estérase, activité enzymatique, hydrolyse enzymatique, acylation, catalyseur, lipase, Plumeria rubra, http://aims.fao.org/aos/agrovoc/c_4214, http://aims.fao.org/aos/agrovoc/c_2670, http://aims.fao.org/aos/agrovoc/c_2604, http://aims.fao.org/aos/agrovoc/c_27512, http://aims.fao.org/aos/agrovoc/c_28220, http://aims.fao.org/aos/agrovoc/c_27480, http://aims.fao.org/aos/agrovoc/c_12194, http://aims.fao.org/aos/agrovoc/c_6027, |
Online Access: | http://agritrop.cirad.fr/532465/ http://agritrop.cirad.fr/532465/1/document_532465.pdf |
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dig-cirad-fr-5324652024-01-28T14:34:11Z http://agritrop.cirad.fr/532465/ http://agritrop.cirad.fr/532465/ Comparison of the lipase activity in hydrolysis and acyl transfer reactions of two latex plant extracts from babaco (Vasconcellea x Heilbornii Cv.) and Plumeria rubra : Effect of the aqueous microenvironment. Cambon Emmanuelle, Gouzou Fanny, Pina Michel, Baréa Bruno, Barouh Nathalie, Lago Regina C.A., Ruales Jenny, Shau-Wei Tsai, Villeneuve Pierre. 2006. Journal of Agricultural and Food Chemistry, 54 (7) : 2726-2731.https://doi.org/10.1021/jf052505k <https://doi.org/10.1021/jf052505k> Comparison of the lipase activity in hydrolysis and acyl transfer reactions of two latex plant extracts from babaco (Vasconcellea x Heilbornii Cv.) and Plumeria rubra : Effect of the aqueous microenvironment Cambon, Emmanuelle Gouzou, Fanny Pina, Michel Baréa, Bruno Barouh, Nathalie Lago, Regina C.A. Ruales, Jenny Shau-Wei Tsai, Villeneuve, Pierre eng 2006 Journal of Agricultural and Food Chemistry Q60 - Traitement des produits agricoles non alimentaires latex estérase activité enzymatique hydrolyse enzymatique acylation catalyseur lipase Plumeria rubra http://aims.fao.org/aos/agrovoc/c_4214 http://aims.fao.org/aos/agrovoc/c_2670 http://aims.fao.org/aos/agrovoc/c_2604 http://aims.fao.org/aos/agrovoc/c_27512 http://aims.fao.org/aos/agrovoc/c_28220 http://aims.fao.org/aos/agrovoc/c_27480 http://aims.fao.org/aos/agrovoc/c_12194 http://aims.fao.org/aos/agrovoc/c_6027 The enzymatic properties of Plumeria rubra latex have been evaluated for the first time, showing a high activity in both hydrolysis and synthesis reactions, and compared to the biocatalytic behavior of babaco (Vasconcellea x Heilbornii cv.) latex. Both biocatalysts have been optimized by studying the various parameters that influence reaction kinetics. The optimum temperatures for hydrolysis reactions were 50 and 55°C for babaco and Plumeria, respectively. The optimum pH for babaco latex was 7, whereas for Plumeria latex, two optimal pH values (4 and 7) were observed. With regard to esterification and acyl transfer reactions such as alcoholysis and interesterification, the influence of thermodynamic water activity on reaction yields was determined and correlated with water sorption and desorption isotherms. When babaco latex is used as a biocatalyst, optimal synthesis reaction yields are obtained when the enzymatic extract is stabilized at a water activity value of 0.38, which corresponds to a water content of 5.7%. This optimal level of hydration is located on the linear portion of the biocatalyst's sorption isotherm, where the water molecules exhibit high-energy interactions with the protein network. In synthesis reactions (esterification, alcoholysis, and interesterification) biocatalyzed by Plumeria latex, correlation between best reaction yields and water activity cannot be done. Indeed, the sorption isotherm plot has an atypical shape, indicating that water might be trapped in the latex matrix and, consequently, that the water content of the biocatalyst is highly dependent on the hydration history of the latex. article info:eu-repo/semantics/article Journal Article info:eu-repo/semantics/publishedVersion http://agritrop.cirad.fr/532465/1/document_532465.pdf application/pdf Cirad license info:eu-repo/semantics/restrictedAccess https://agritrop.cirad.fr/mention_legale.html https://doi.org/10.1021/jf052505k 10.1021/jf052505k http://catalogue-bibliotheques.cirad.fr/cgi-bin/koha/opac-detail.pl?biblionumber=191298 info:eu-repo/semantics/altIdentifier/doi/10.1021/jf052505k info:eu-repo/semantics/altIdentifier/purl/https://doi.org/10.1021/jf052505k |
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Q60 - Traitement des produits agricoles non alimentaires latex estérase activité enzymatique hydrolyse enzymatique acylation catalyseur lipase Plumeria rubra http://aims.fao.org/aos/agrovoc/c_4214 http://aims.fao.org/aos/agrovoc/c_2670 http://aims.fao.org/aos/agrovoc/c_2604 http://aims.fao.org/aos/agrovoc/c_27512 http://aims.fao.org/aos/agrovoc/c_28220 http://aims.fao.org/aos/agrovoc/c_27480 http://aims.fao.org/aos/agrovoc/c_12194 http://aims.fao.org/aos/agrovoc/c_6027 Q60 - Traitement des produits agricoles non alimentaires latex estérase activité enzymatique hydrolyse enzymatique acylation catalyseur lipase Plumeria rubra http://aims.fao.org/aos/agrovoc/c_4214 http://aims.fao.org/aos/agrovoc/c_2670 http://aims.fao.org/aos/agrovoc/c_2604 http://aims.fao.org/aos/agrovoc/c_27512 http://aims.fao.org/aos/agrovoc/c_28220 http://aims.fao.org/aos/agrovoc/c_27480 http://aims.fao.org/aos/agrovoc/c_12194 http://aims.fao.org/aos/agrovoc/c_6027 |
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Q60 - Traitement des produits agricoles non alimentaires latex estérase activité enzymatique hydrolyse enzymatique acylation catalyseur lipase Plumeria rubra http://aims.fao.org/aos/agrovoc/c_4214 http://aims.fao.org/aos/agrovoc/c_2670 http://aims.fao.org/aos/agrovoc/c_2604 http://aims.fao.org/aos/agrovoc/c_27512 http://aims.fao.org/aos/agrovoc/c_28220 http://aims.fao.org/aos/agrovoc/c_27480 http://aims.fao.org/aos/agrovoc/c_12194 http://aims.fao.org/aos/agrovoc/c_6027 Q60 - Traitement des produits agricoles non alimentaires latex estérase activité enzymatique hydrolyse enzymatique acylation catalyseur lipase Plumeria rubra http://aims.fao.org/aos/agrovoc/c_4214 http://aims.fao.org/aos/agrovoc/c_2670 http://aims.fao.org/aos/agrovoc/c_2604 http://aims.fao.org/aos/agrovoc/c_27512 http://aims.fao.org/aos/agrovoc/c_28220 http://aims.fao.org/aos/agrovoc/c_27480 http://aims.fao.org/aos/agrovoc/c_12194 http://aims.fao.org/aos/agrovoc/c_6027 Cambon, Emmanuelle Gouzou, Fanny Pina, Michel Baréa, Bruno Barouh, Nathalie Lago, Regina C.A. Ruales, Jenny Shau-Wei Tsai, Villeneuve, Pierre Comparison of the lipase activity in hydrolysis and acyl transfer reactions of two latex plant extracts from babaco (Vasconcellea x Heilbornii Cv.) and Plumeria rubra : Effect of the aqueous microenvironment |
description |
The enzymatic properties of Plumeria rubra latex have been evaluated for the first time, showing a high activity in both hydrolysis and synthesis reactions, and compared to the biocatalytic behavior of babaco (Vasconcellea x Heilbornii cv.) latex. Both biocatalysts have been optimized by studying the various parameters that influence reaction kinetics. The optimum temperatures for hydrolysis reactions were 50 and 55°C for babaco and Plumeria, respectively. The optimum pH for babaco latex was 7, whereas for Plumeria latex, two optimal pH values (4 and 7) were observed. With regard to esterification and acyl transfer reactions such as alcoholysis and interesterification, the influence of thermodynamic water activity on reaction yields was determined and correlated with water sorption and desorption isotherms. When babaco latex is used as a biocatalyst, optimal synthesis reaction yields are obtained when the enzymatic extract is stabilized at a water activity value of 0.38, which corresponds to a water content of 5.7%. This optimal level of hydration is located on the linear portion of the biocatalyst's sorption isotherm, where the water molecules exhibit high-energy interactions with the protein network. In synthesis reactions (esterification, alcoholysis, and interesterification) biocatalyzed by Plumeria latex, correlation between best reaction yields and water activity cannot be done. Indeed, the sorption isotherm plot has an atypical shape, indicating that water might be trapped in the latex matrix and, consequently, that the water content of the biocatalyst is highly dependent on the hydration history of the latex. |
format |
article |
topic_facet |
Q60 - Traitement des produits agricoles non alimentaires latex estérase activité enzymatique hydrolyse enzymatique acylation catalyseur lipase Plumeria rubra http://aims.fao.org/aos/agrovoc/c_4214 http://aims.fao.org/aos/agrovoc/c_2670 http://aims.fao.org/aos/agrovoc/c_2604 http://aims.fao.org/aos/agrovoc/c_27512 http://aims.fao.org/aos/agrovoc/c_28220 http://aims.fao.org/aos/agrovoc/c_27480 http://aims.fao.org/aos/agrovoc/c_12194 http://aims.fao.org/aos/agrovoc/c_6027 |
author |
Cambon, Emmanuelle Gouzou, Fanny Pina, Michel Baréa, Bruno Barouh, Nathalie Lago, Regina C.A. Ruales, Jenny Shau-Wei Tsai, Villeneuve, Pierre |
author_facet |
Cambon, Emmanuelle Gouzou, Fanny Pina, Michel Baréa, Bruno Barouh, Nathalie Lago, Regina C.A. Ruales, Jenny Shau-Wei Tsai, Villeneuve, Pierre |
author_sort |
Cambon, Emmanuelle |
title |
Comparison of the lipase activity in hydrolysis and acyl transfer reactions of two latex plant extracts from babaco (Vasconcellea x Heilbornii Cv.) and Plumeria rubra : Effect of the aqueous microenvironment |
title_short |
Comparison of the lipase activity in hydrolysis and acyl transfer reactions of two latex plant extracts from babaco (Vasconcellea x Heilbornii Cv.) and Plumeria rubra : Effect of the aqueous microenvironment |
title_full |
Comparison of the lipase activity in hydrolysis and acyl transfer reactions of two latex plant extracts from babaco (Vasconcellea x Heilbornii Cv.) and Plumeria rubra : Effect of the aqueous microenvironment |
title_fullStr |
Comparison of the lipase activity in hydrolysis and acyl transfer reactions of two latex plant extracts from babaco (Vasconcellea x Heilbornii Cv.) and Plumeria rubra : Effect of the aqueous microenvironment |
title_full_unstemmed |
Comparison of the lipase activity in hydrolysis and acyl transfer reactions of two latex plant extracts from babaco (Vasconcellea x Heilbornii Cv.) and Plumeria rubra : Effect of the aqueous microenvironment |
title_sort |
comparison of the lipase activity in hydrolysis and acyl transfer reactions of two latex plant extracts from babaco (vasconcellea x heilbornii cv.) and plumeria rubra : effect of the aqueous microenvironment |
url |
http://agritrop.cirad.fr/532465/ http://agritrop.cirad.fr/532465/1/document_532465.pdf |
work_keys_str_mv |
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