Synthesis of neryl acetate by free lipase-catalyzed transesterification in organic solvents and its kinetics
Autor(a) principal: | |
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Data de Publicação: | 2022 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Food Science and Technology (Campinas) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000101134 |
Resumo: | Abstract In this paper, the optimum conditions and kinetics of lipase-catalyzed transesterification reaction of nerol and vinyl acetate for the synthesis of neryl acetate were investigated in a solvent-free system. The optimum conditions were determined as follows: the reaction temperature was 40 °C, the amount of enzyme was 12 mg/mL, and there was no need to add water. Increasing the stirring speed to 200 r/min can eliminate the external diffusion limitations. There was no substrate inhibition when the substrate concentration was lower than 500 mmol/L. However, the experimental results indicated that the product inhibition effect should be considered. The results of the reaction kinetic analysis indicated that the reaction followed the ping-pong double-double reaction mechanism with product inhibition. Finally, the model parameters were calculated by MATLAB software and the results showed that the experimental values could be in good agreement with the simulated values, and the relative error was 6.98%. |
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Food Science and Technology (Campinas) |
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Synthesis of neryl acetate by free lipase-catalyzed transesterification in organic solvents and its kineticsneryl acetatelipasesolvent-free systemtransesterificationkineticsAbstract In this paper, the optimum conditions and kinetics of lipase-catalyzed transesterification reaction of nerol and vinyl acetate for the synthesis of neryl acetate were investigated in a solvent-free system. The optimum conditions were determined as follows: the reaction temperature was 40 °C, the amount of enzyme was 12 mg/mL, and there was no need to add water. Increasing the stirring speed to 200 r/min can eliminate the external diffusion limitations. There was no substrate inhibition when the substrate concentration was lower than 500 mmol/L. However, the experimental results indicated that the product inhibition effect should be considered. The results of the reaction kinetic analysis indicated that the reaction followed the ping-pong double-double reaction mechanism with product inhibition. Finally, the model parameters were calculated by MATLAB software and the results showed that the experimental values could be in good agreement with the simulated values, and the relative error was 6.98%.Sociedade Brasileira de Ciência e Tecnologia de Alimentos2022-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000101134Food Science and Technology v.42 2022reponame:Food Science and Technology (Campinas)instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)instacron:SBCTA10.1590/fst.26522info:eu-repo/semantics/openAccessSUN,WenyuanXIONG,JianXU,HanghangMA,MengyuanHU,Yanyaneng2022-06-20T00:00:00Zoai:scielo:S0101-20612022000101134Revistahttp://www.scielo.br/ctaONGhttps://old.scielo.br/oai/scielo-oai.php||revista@sbcta.org.br1678-457X0101-2061opendoar:2022-06-20T00:00Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)false |
dc.title.none.fl_str_mv |
Synthesis of neryl acetate by free lipase-catalyzed transesterification in organic solvents and its kinetics |
title |
Synthesis of neryl acetate by free lipase-catalyzed transesterification in organic solvents and its kinetics |
spellingShingle |
Synthesis of neryl acetate by free lipase-catalyzed transesterification in organic solvents and its kinetics SUN,Wenyuan neryl acetate lipase solvent-free system transesterification kinetics |
title_short |
Synthesis of neryl acetate by free lipase-catalyzed transesterification in organic solvents and its kinetics |
title_full |
Synthesis of neryl acetate by free lipase-catalyzed transesterification in organic solvents and its kinetics |
title_fullStr |
Synthesis of neryl acetate by free lipase-catalyzed transesterification in organic solvents and its kinetics |
title_full_unstemmed |
Synthesis of neryl acetate by free lipase-catalyzed transesterification in organic solvents and its kinetics |
title_sort |
Synthesis of neryl acetate by free lipase-catalyzed transesterification in organic solvents and its kinetics |
author |
SUN,Wenyuan |
author_facet |
SUN,Wenyuan XIONG,Jian XU,Hanghang MA,Mengyuan HU,Yanyan |
author_role |
author |
author2 |
XIONG,Jian XU,Hanghang MA,Mengyuan HU,Yanyan |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
SUN,Wenyuan XIONG,Jian XU,Hanghang MA,Mengyuan HU,Yanyan |
dc.subject.por.fl_str_mv |
neryl acetate lipase solvent-free system transesterification kinetics |
topic |
neryl acetate lipase solvent-free system transesterification kinetics |
description |
Abstract In this paper, the optimum conditions and kinetics of lipase-catalyzed transesterification reaction of nerol and vinyl acetate for the synthesis of neryl acetate were investigated in a solvent-free system. The optimum conditions were determined as follows: the reaction temperature was 40 °C, the amount of enzyme was 12 mg/mL, and there was no need to add water. Increasing the stirring speed to 200 r/min can eliminate the external diffusion limitations. There was no substrate inhibition when the substrate concentration was lower than 500 mmol/L. However, the experimental results indicated that the product inhibition effect should be considered. The results of the reaction kinetic analysis indicated that the reaction followed the ping-pong double-double reaction mechanism with product inhibition. Finally, the model parameters were calculated by MATLAB software and the results showed that the experimental values could be in good agreement with the simulated values, and the relative error was 6.98%. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-01-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000101134 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612022000101134 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/fst.26522 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos |
publisher.none.fl_str_mv |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos |
dc.source.none.fl_str_mv |
Food Science and Technology v.42 2022 reponame:Food Science and Technology (Campinas) instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) instacron:SBCTA |
instname_str |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) |
instacron_str |
SBCTA |
institution |
SBCTA |
reponame_str |
Food Science and Technology (Campinas) |
collection |
Food Science and Technology (Campinas) |
repository.name.fl_str_mv |
Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) |
repository.mail.fl_str_mv |
||revista@sbcta.org.br |
_version_ |
1752126334516068352 |