Fractionation of Apis mellifera venom by means of ultrafiltration: removal of phospholipase A 2

Detalhes bibliográficos
Autor(a) principal: Brito,Júlio César Moreira de
Data de Publicação: 2018
Outros Autores: Bastos,Esther Margarida Alves Ferreira, Heneine,Luiz Guilherme Dias, Figueiredo,Kátia Cecília de Souza
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Journal of Chemical Engineering
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322018000100229
Resumo: Abstract The fractionation of apitoxin (bee venom) by means of a commercial 10 kDa ultrafiltration membrane was investigated aiming at the removal of phospholipase A2, the main allergenic substance. The feed content was varied from 1 to 50 g apitoxin/L, in deionized water, and caused changes in membrane flux and rejection, due to concentration polarization. The increase in pressure difference and stirring rate improved the flux through the membrane. The best result was achieved for 1 g apitoxin/L in feed stream, with a pressure difference of 220 kPa, and 750 rpm, with a permeate flux of 103 kg/m2h. The use of ultrafiltration was efficient to improve the permeate safety since biological tests revealed that the remaining enzyme lost its ability to catalyze the hydrolysis of phospholipids.
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spelling Fractionation of Apis mellifera venom by means of ultrafiltration: removal of phospholipase A 2apitoxinmelittinmembranephospholipase A2ultrafiltrationAbstract The fractionation of apitoxin (bee venom) by means of a commercial 10 kDa ultrafiltration membrane was investigated aiming at the removal of phospholipase A2, the main allergenic substance. The feed content was varied from 1 to 50 g apitoxin/L, in deionized water, and caused changes in membrane flux and rejection, due to concentration polarization. The increase in pressure difference and stirring rate improved the flux through the membrane. The best result was achieved for 1 g apitoxin/L in feed stream, with a pressure difference of 220 kPa, and 750 rpm, with a permeate flux of 103 kg/m2h. The use of ultrafiltration was efficient to improve the permeate safety since biological tests revealed that the remaining enzyme lost its ability to catalyze the hydrolysis of phospholipids.Brazilian Society of Chemical Engineering2018-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322018000100229Brazilian Journal of Chemical Engineering v.35 n.1 2018reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/0104-6632.20180351s20160171info:eu-repo/semantics/openAccessBrito,Júlio César Moreira deBastos,Esther Margarida Alves FerreiraHeneine,Luiz Guilherme DiasFigueiredo,Kátia Cecília de Souzaeng2018-04-19T00:00:00Zoai:scielo:S0104-66322018000100229Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:2018-04-19T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false
dc.title.none.fl_str_mv Fractionation of Apis mellifera venom by means of ultrafiltration: removal of phospholipase A 2
title Fractionation of Apis mellifera venom by means of ultrafiltration: removal of phospholipase A 2
spellingShingle Fractionation of Apis mellifera venom by means of ultrafiltration: removal of phospholipase A 2
Brito,Júlio César Moreira de
apitoxin
melittin
membrane
phospholipase A2
ultrafiltration
title_short Fractionation of Apis mellifera venom by means of ultrafiltration: removal of phospholipase A 2
title_full Fractionation of Apis mellifera venom by means of ultrafiltration: removal of phospholipase A 2
title_fullStr Fractionation of Apis mellifera venom by means of ultrafiltration: removal of phospholipase A 2
title_full_unstemmed Fractionation of Apis mellifera venom by means of ultrafiltration: removal of phospholipase A 2
title_sort Fractionation of Apis mellifera venom by means of ultrafiltration: removal of phospholipase A 2
author Brito,Júlio César Moreira de
author_facet Brito,Júlio César Moreira de
Bastos,Esther Margarida Alves Ferreira
Heneine,Luiz Guilherme Dias
Figueiredo,Kátia Cecília de Souza
author_role author
author2 Bastos,Esther Margarida Alves Ferreira
Heneine,Luiz Guilherme Dias
Figueiredo,Kátia Cecília de Souza
author2_role author
author
author
dc.contributor.author.fl_str_mv Brito,Júlio César Moreira de
Bastos,Esther Margarida Alves Ferreira
Heneine,Luiz Guilherme Dias
Figueiredo,Kátia Cecília de Souza
dc.subject.por.fl_str_mv apitoxin
melittin
membrane
phospholipase A2
ultrafiltration
topic apitoxin
melittin
membrane
phospholipase A2
ultrafiltration
description Abstract The fractionation of apitoxin (bee venom) by means of a commercial 10 kDa ultrafiltration membrane was investigated aiming at the removal of phospholipase A2, the main allergenic substance. The feed content was varied from 1 to 50 g apitoxin/L, in deionized water, and caused changes in membrane flux and rejection, due to concentration polarization. The increase in pressure difference and stirring rate improved the flux through the membrane. The best result was achieved for 1 g apitoxin/L in feed stream, with a pressure difference of 220 kPa, and 750 rpm, with a permeate flux of 103 kg/m2h. The use of ultrafiltration was efficient to improve the permeate safety since biological tests revealed that the remaining enzyme lost its ability to catalyze the hydrolysis of phospholipids.
publishDate 2018
dc.date.none.fl_str_mv 2018-01-01
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=S0104-66322018000100229
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322018000100229
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/0104-6632.20180351s20160171
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 Brazilian Society of Chemical Engineering
publisher.none.fl_str_mv Brazilian Society of Chemical Engineering
dc.source.none.fl_str_mv Brazilian Journal of Chemical Engineering v.35 n.1 2018
reponame:Brazilian Journal of Chemical Engineering
instname:Associação Brasileira de Engenharia Química (ABEQ)
instacron:ABEQ
instname_str Associação Brasileira de Engenharia Química (ABEQ)
instacron_str ABEQ
institution ABEQ
reponame_str Brazilian Journal of Chemical Engineering
collection Brazilian Journal of Chemical Engineering
repository.name.fl_str_mv Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)
repository.mail.fl_str_mv rgiudici@usp.br||rgiudici@usp.br
_version_ 1754213175873503232

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