Synthesis of neryl acetate by free lipase-catalyzed transesterification in organic solvents and its kinetics

Detalhes bibliográficos
Autor(a) principal: SUN,Wenyuan
Data de Publicação: 2022
Outros Autores: XIONG,Jian, XU,Hanghang, MA,Mengyuan, HU,Yanyan
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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spelling 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
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