Temperature and pH conditions for maximum activity of bromelain extracted from pineapple (Ananas Comosus L. Merril) - doi: 10.4025/actascitechnol.v33i2.7928
Autor(a) principal: | |
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Data de Publicação: | 2011 |
Outros Autores: | , |
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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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 |
_version_ |
1799315333761204224 |