Observance of polymorphic behaviour during dissolution of insulin and lysozyme
Autor(a) principal: | |
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Data de Publicação: | 2005 |
Outros Autores: | , |
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=S0104-66322005000300002 |
Resumo: | Although protein crystallization is a unit operation with potentially high separation factors, it has not been widely used in industry. Protein crystallization studies and practices have hitherto been largely limited to crystallography protocols. Knowledge of the behaviour of protein in solution would help to overcome empiric limitations in protein crystallisation. Thus, dissolution of porcine insulin and hen egg white lysozyme was studied and an unusual variation in solute concentration, with a concentration peak for short dissolution times, was verified. Polymorphic behaviour of protein in solution was observed, which altered physical properties such as solubility. |
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Brazilian Journal of Chemical Engineering |
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Observance of polymorphic behaviour during dissolution of insulin and lysozymeInsulinLysozymeDissolutionPseudopolymorphismSolvatomorphismSolubilityAlthough protein crystallization is a unit operation with potentially high separation factors, it has not been widely used in industry. Protein crystallization studies and practices have hitherto been largely limited to crystallography protocols. Knowledge of the behaviour of protein in solution would help to overcome empiric limitations in protein crystallisation. Thus, dissolution of porcine insulin and hen egg white lysozyme was studied and an unusual variation in solute concentration, with a concentration peak for short dissolution times, was verified. Polymorphic behaviour of protein in solution was observed, which altered physical properties such as solubility.Brazilian Society of Chemical Engineering2005-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322005000300002Brazilian Journal of Chemical Engineering v.22 n.3 2005reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/S0104-66322005000300002info:eu-repo/semantics/openAccessBernardo,A.Calmanovici,C. E.Miranda,E. A.eng2005-09-26T00:00:00Zoai:scielo:S0104-66322005000300002Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:2005-09-26T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false |
dc.title.none.fl_str_mv |
Observance of polymorphic behaviour during dissolution of insulin and lysozyme |
title |
Observance of polymorphic behaviour during dissolution of insulin and lysozyme |
spellingShingle |
Observance of polymorphic behaviour during dissolution of insulin and lysozyme Bernardo,A. Insulin Lysozyme Dissolution Pseudopolymorphism Solvatomorphism Solubility |
title_short |
Observance of polymorphic behaviour during dissolution of insulin and lysozyme |
title_full |
Observance of polymorphic behaviour during dissolution of insulin and lysozyme |
title_fullStr |
Observance of polymorphic behaviour during dissolution of insulin and lysozyme |
title_full_unstemmed |
Observance of polymorphic behaviour during dissolution of insulin and lysozyme |
title_sort |
Observance of polymorphic behaviour during dissolution of insulin and lysozyme |
author |
Bernardo,A. |
author_facet |
Bernardo,A. Calmanovici,C. E. Miranda,E. A. |
author_role |
author |
author2 |
Calmanovici,C. E. Miranda,E. A. |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Bernardo,A. Calmanovici,C. E. Miranda,E. A. |
dc.subject.por.fl_str_mv |
Insulin Lysozyme Dissolution Pseudopolymorphism Solvatomorphism Solubility |
topic |
Insulin Lysozyme Dissolution Pseudopolymorphism Solvatomorphism Solubility |
description |
Although protein crystallization is a unit operation with potentially high separation factors, it has not been widely used in industry. Protein crystallization studies and practices have hitherto been largely limited to crystallography protocols. Knowledge of the behaviour of protein in solution would help to overcome empiric limitations in protein crystallisation. Thus, dissolution of porcine insulin and hen egg white lysozyme was studied and an unusual variation in solute concentration, with a concentration peak for short dissolution times, was verified. Polymorphic behaviour of protein in solution was observed, which altered physical properties such as solubility. |
publishDate |
2005 |
dc.date.none.fl_str_mv |
2005-09-01 |
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=S0104-66322005000300002 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322005000300002 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0104-66322005000300002 |
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.22 n.3 2005 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_ |
1754213171897303040 |