Temperature and pH conditions for maximum activity of bromelain extracted from pineapple (Ananas Comosus L. Merril) - doi: 10.4025/actascitechnol.v33i2.7928

Detalhes bibliográficos
Autor(a) principal: Elias, Moacyr Jorge
Data de Publicação: 2011
Outros Autores: Arcuri, Ivan Fabian, Tambourgi, Elias Basile
Tipo de documento: Artigo
Idioma: por
Título da fonte: Acta scientiarum. Technology (Online)
Texto Completo: http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/7928
Resumo: Bromelain, the enzyme found in pineapple, hydrolyzes proteins’ peptide bonds, has several applications in the food industry and in medicine. Temperature and pH conditions for highest activity with casein as substrate were investigated from the bromelain recovered from industrialized pineapple (‘pérola’ variety) fruit residues. Extract was obtained by grinding fruit rind and its internal stem. The activity was expressed in mmol tyrosine L-1 min. -1 by absorbance at 280 nm of aromatic amino acids produced in casein hydrolysis. Assays were undertaken in duplicate for two enzyme/substrate with ratios: 1/25 and 1/125 (mass). Eight-pointed experimental design was undertaken with central value for pH at 7.0 and for temperature at 35°C. Experimental results were processed by MINITAB 15 (Minitab Inc) software which provided model’s equations and surface responses. Equations were mathematically processed by differential calculus producing graphs which exhibit the best activities according to temperatures. Loss of enzyme activity was reported with temperature increase at 1/25 ratio, due to a higher free enzyme, when compared to 1/125 ratio.
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spelling Temperature and pH conditions for maximum activity of bromelain extracted from pineapple (Ananas Comosus L. Merril) - doi: 10.4025/actascitechnol.v33i2.7928Condições de pH e temperatura para máxima atividade da bromelina do abacaxi (Ananas Comosus L. Merril) - doi: 10.4025/actascitechnol.v33i2.7928Enzymeplanningthermal decompositionproteinasesulphhydril proteaseEnzimaplanejamentodecomposição térmicaproteinasesulfidril proteaseBromelain, the enzyme found in pineapple, hydrolyzes proteins’ peptide bonds, has several applications in the food industry and in medicine. Temperature and pH conditions for highest activity with casein as substrate were investigated from the bromelain recovered from industrialized pineapple (‘pérola’ variety) fruit residues. Extract was obtained by grinding fruit rind and its internal stem. The activity was expressed in mmol tyrosine L-1 min. -1 by absorbance at 280 nm of aromatic amino acids produced in casein hydrolysis. Assays were undertaken in duplicate for two enzyme/substrate with ratios: 1/25 and 1/125 (mass). Eight-pointed experimental design was undertaken with central value for pH at 7.0 and for temperature at 35°C. Experimental results were processed by MINITAB 15 (Minitab Inc) software which provided model’s equations and surface responses. Equations were mathematically processed by differential calculus producing graphs which exhibit the best activities according to temperatures. Loss of enzyme activity was reported with temperature increase at 1/25 ratio, due to a higher free enzyme, when compared to 1/125 ratio.A bromelina, enzima presente no abacaxi, hidrolisa ligações peptídicas das proteínas; tem aplicação em diversas áreas envolvendo alimentos e medicina. Visando o aproveitamento da bromelina recuperada, a partir dos resíduos da industrialização do fruto (variedade pérola), foram pesquisadas condições de pH e temperatura para maior atividade, empregando caseína como substrato. O extrato foi obtido pela trituração da casca e do talo interno do fruto. A atividade foi expressa em mmol tirosina L-1 min. -1 pela absorbância a 280 nm dos aminoácidos aromáticos gerados na hidrólise da caseína. Os ensaios foram efetuados em duplicata para duas relações enzima/substrato: 1/25 e 1/125 (em massa). Foi estabelecido um planejamento experimental em estrela tendo como ponto central pH em 7,0 e temperatura de 35°C. Os resultados foram tratados empregando o aplicativo computacional MINITAB 15 da Minitab Inc. que forneceu as equações do modelo e as superfícies de resposta. As equações foram tratadas matematicamente (cálculo diferencial), fornecendo gráficos da melhor atividade em função da temperatura. Observou-se perda da atividade enzimática com a elevação da temperatura para relação 1/25, atribuída à maior presença de enzima livre em comparação com a relação 1/125.Universidade Estadual De Maringá2011-02-23info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/792810.4025/actascitechnol.v33i2.7928Acta Scientiarum. Technology; Vol 33 No 2 (2011); 191-196Acta Scientiarum. Technology; v. 33 n. 2 (2011); 191-1961806-25631807-8664reponame:Acta scientiarum. Technology (Online)instname:Universidade Estadual de Maringá (UEM)instacron:UEMporhttp://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/7928/7928Elias, Moacyr JorgeArcuri, Ivan FabianTambourgi, Elias Basileinfo:eu-repo/semantics/openAccess2024-05-17T13:03:11Zoai:periodicos.uem.br/ojs:article/7928Revistahttps://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/indexPUBhttps://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/oai||actatech@uem.br1807-86641806-2563opendoar:2024-05-17T13:03:11Acta scientiarum. Technology (Online) - Universidade Estadual de Maringá (UEM)false
dc.title.none.fl_str_mv Temperature and pH conditions for maximum activity of bromelain extracted from pineapple (Ananas Comosus L. Merril) - doi: 10.4025/actascitechnol.v33i2.7928
Condições de pH e temperatura para máxima atividade da bromelina do abacaxi (Ananas Comosus L. Merril) - doi: 10.4025/actascitechnol.v33i2.7928
title Temperature and pH conditions for maximum activity of bromelain extracted from pineapple (Ananas Comosus L. Merril) - doi: 10.4025/actascitechnol.v33i2.7928
spellingShingle Temperature and pH conditions for maximum activity of bromelain extracted from pineapple (Ananas Comosus L. Merril) - doi: 10.4025/actascitechnol.v33i2.7928
Elias, Moacyr Jorge
Enzyme
planning
thermal decomposition
proteinase
sulphhydril protease
Enzima
planejamento
decomposição térmica
proteinase
sulfidril protease
title_short Temperature and pH conditions for maximum activity of bromelain extracted from pineapple (Ananas Comosus L. Merril) - doi: 10.4025/actascitechnol.v33i2.7928
title_full Temperature and pH conditions for maximum activity of bromelain extracted from pineapple (Ananas Comosus L. Merril) - doi: 10.4025/actascitechnol.v33i2.7928
title_fullStr Temperature and pH conditions for maximum activity of bromelain extracted from pineapple (Ananas Comosus L. Merril) - doi: 10.4025/actascitechnol.v33i2.7928
title_full_unstemmed Temperature and pH conditions for maximum activity of bromelain extracted from pineapple (Ananas Comosus L. Merril) - doi: 10.4025/actascitechnol.v33i2.7928
title_sort Temperature and pH conditions for maximum activity of bromelain extracted from pineapple (Ananas Comosus L. Merril) - doi: 10.4025/actascitechnol.v33i2.7928
author Elias, Moacyr Jorge
author_facet Elias, Moacyr Jorge
Arcuri, Ivan Fabian
Tambourgi, Elias Basile
author_role author
author2 Arcuri, Ivan Fabian
Tambourgi, Elias Basile
author2_role author
author
dc.contributor.author.fl_str_mv Elias, Moacyr Jorge
Arcuri, Ivan Fabian
Tambourgi, Elias Basile
dc.subject.por.fl_str_mv Enzyme
planning
thermal decomposition
proteinase
sulphhydril protease
Enzima
planejamento
decomposição térmica
proteinase
sulfidril protease
topic Enzyme
planning
thermal decomposition
proteinase
sulphhydril protease
Enzima
planejamento
decomposição térmica
proteinase
sulfidril protease
description Bromelain, the enzyme found in pineapple, hydrolyzes proteins’ peptide bonds, has several applications in the food industry and in medicine. Temperature and pH conditions for highest activity with casein as substrate were investigated from the bromelain recovered from industrialized pineapple (‘pérola’ variety) fruit residues. Extract was obtained by grinding fruit rind and its internal stem. The activity was expressed in mmol tyrosine L-1 min. -1 by absorbance at 280 nm of aromatic amino acids produced in casein hydrolysis. Assays were undertaken in duplicate for two enzyme/substrate with ratios: 1/25 and 1/125 (mass). Eight-pointed experimental design was undertaken with central value for pH at 7.0 and for temperature at 35°C. Experimental results were processed by MINITAB 15 (Minitab Inc) software which provided model’s equations and surface responses. Equations were mathematically processed by differential calculus producing graphs which exhibit the best activities according to temperatures. Loss of enzyme activity was reported with temperature increase at 1/25 ratio, due to a higher free enzyme, when compared to 1/125 ratio.
publishDate 2011
dc.date.none.fl_str_mv 2011-02-23
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/7928
10.4025/actascitechnol.v33i2.7928
url http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/7928
identifier_str_mv 10.4025/actascitechnol.v33i2.7928
dc.language.iso.fl_str_mv por
language por
dc.relation.none.fl_str_mv http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/7928/7928
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Universidade Estadual De Maringá
publisher.none.fl_str_mv Universidade Estadual De Maringá
dc.source.none.fl_str_mv Acta Scientiarum. Technology; Vol 33 No 2 (2011); 191-196
Acta Scientiarum. Technology; v. 33 n. 2 (2011); 191-196
1806-2563
1807-8664
reponame:Acta scientiarum. Technology (Online)
instname:Universidade Estadual de Maringá (UEM)
instacron:UEM
instname_str Universidade Estadual de Maringá (UEM)
instacron_str UEM
institution UEM
reponame_str Acta scientiarum. Technology (Online)
collection Acta scientiarum. Technology (Online)
repository.name.fl_str_mv Acta scientiarum. Technology (Online) - Universidade Estadual de Maringá (UEM)
repository.mail.fl_str_mv ||actatech@uem.br
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