Effectiveness inactivation of trypsin inhibitor fron brazilian cultivarof beans (Phaseolus vulgaris L.)

Detalhes bibliográficos
Autor(a) principal: Paiva, Kelli Cristina [UNESP]
Data de Publicação: 2011
Outros Autores: Carvalho, Maria Regina Barbieri de [UNESP], Pizauro Júnior, Joao Martins [UNESP]
Tipo de documento: Artigo
Idioma: por
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://serv-bib.fcfar.unesp.br/seer/index.php/alimentos/article/view/1487
http://hdl.handle.net/11449/123617
Resumo: The trypsin inhibitor, an antinutritional factor, which is abundant in dycotiledoneous and monocotyledoneous, is usually inactivated by heating treatment. The infl uence of pressure-cooking (121°C and 141kPa) for 30 min on, trypsin inhibitors concentration and inhibitors reactivation from ten Brazilian beans varieties of Phaseolus vulgaris L. namely: IAPAR-14, IAC-Carioca, Rudá, Corrente, IAC-Aruã, IAPAR-16, IAPAR-57, IAC-Carioca Pyatã, Carioca, Aporé, were investigated. The inhibitors reactivation was evaluated in comparison with the activity of raw and pressure-cooking. For raw the in vitro protein digestibility mean values ranged from 40% (in Carioca cultivar) to 60% (in IAC-Aruã cultivar), showing an increase from 11% to 37% using the autoclaving at 121°C and 141kPa. Among ten cultivars studied the trypsin inhibitor activity varied from 36.18UTI.mg-1 for IAC-Aruã to 63.33UTI.mg-1 for IAPAR-16. Trypsin inhibitor activity was totally inactivated by pressure-cooking. The study of the trypsin inhibitors reactivation using double-digestive pepsin-pancreatin enzymes in vitro showed a recovering activity from 34% up to 100%. Native inhibitor is resistant to double- digestive pepsin-pancreatin proteolysis, whereas autoclaving to 121oC.30 min-1 results in a non-native conformation that is susceptible to proteolysis, improving the digestibility and inactivate differentially the activity of trypsin inhibitors. The results of the thermal treatment of the beans show inactivation of the inhibitors, which may be due to formation of high molecular weight aggregates with other substances of the grain. The pepsin-pancreatin digestion of the inactivated inhibitor restores the activity, probably due to its retention by the digested fragments.
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spelling Effectiveness inactivation of trypsin inhibitor fron brazilian cultivarof beans (Phaseolus vulgaris L.)Eficácia da inativação do inibidor de tripsina em cultivares brasileiras de feijão (Phaseolus vulgaris L.)Antinutritional factorHeat treatmentIn vitro protein digestibilityInhibitor reactivationThe trypsin inhibitor, an antinutritional factor, which is abundant in dycotiledoneous and monocotyledoneous, is usually inactivated by heating treatment. The infl uence of pressure-cooking (121°C and 141kPa) for 30 min on, trypsin inhibitors concentration and inhibitors reactivation from ten Brazilian beans varieties of Phaseolus vulgaris L. namely: IAPAR-14, IAC-Carioca, Rudá, Corrente, IAC-Aruã, IAPAR-16, IAPAR-57, IAC-Carioca Pyatã, Carioca, Aporé, were investigated. The inhibitors reactivation was evaluated in comparison with the activity of raw and pressure-cooking. For raw the in vitro protein digestibility mean values ranged from 40% (in Carioca cultivar) to 60% (in IAC-Aruã cultivar), showing an increase from 11% to 37% using the autoclaving at 121°C and 141kPa. Among ten cultivars studied the trypsin inhibitor activity varied from 36.18UTI.mg-1 for IAC-Aruã to 63.33UTI.mg-1 for IAPAR-16. Trypsin inhibitor activity was totally inactivated by pressure-cooking. The study of the trypsin inhibitors reactivation using double-digestive pepsin-pancreatin enzymes in vitro showed a recovering activity from 34% up to 100%. Native inhibitor is resistant to double- digestive pepsin-pancreatin proteolysis, whereas autoclaving to 121oC.30 min-1 results in a non-native conformation that is susceptible to proteolysis, improving the digestibility and inactivate differentially the activity of trypsin inhibitors. The results of the thermal treatment of the beans show inactivation of the inhibitors, which may be due to formation of high molecular weight aggregates with other substances of the grain. The pepsin-pancreatin digestion of the inactivated inhibitor restores the activity, probably due to its retention by the digested fragments.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Universidade Estadual Paulista Júlio de Mesquita Filho, Departamento de Tecnologia, Faculadade de Ciências Agrárias e Veterinárias Jaboticabal, Jaboticabal, Via deAcesso Prof Paulo Donato Castellani s/n, Rural, CEP 14884-900, SP, BrasilUniversidade Estadual Paulista Júlio de Mesquita Filho, Departamento de Tecnologia, Faculadade de Ciências Agrárias e Veterinárias Jaboticabal, Jaboticabal, Via deAcesso Prof Paulo Donato Castellani s/n, Rural, CEP 14884-900, SP, BrasilDepartment of Technology – College of Agricultural and Veterinarian Science – São Paulo State University – UNESPUniversidade Estadual Paulista (Unesp)Paiva, Kelli Cristina [UNESP]Carvalho, Maria Regina Barbieri de [UNESP]Pizauro Júnior, Joao Martins [UNESP]2015-05-15T13:30:30Z2015-05-15T13:30:30Z2011info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article331-337application/pdfhttp://serv-bib.fcfar.unesp.br/seer/index.php/alimentos/article/view/1487Alimentos e Nutrição, v. 22, n. 3, p. 331-337, 2011.2179-4448http://hdl.handle.net/11449/123617ISSN2179-4448-2011-22-03-331-337.pdf3958124498479090Currículo Lattesreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPporAlimentos e Nutriçãoinfo:eu-repo/semantics/openAccess2024-06-07T15:31:59Zoai:repositorio.unesp.br:11449/123617Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T18:16:05.712865Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Effectiveness inactivation of trypsin inhibitor fron brazilian cultivarof beans (Phaseolus vulgaris L.)
Eficácia da inativação do inibidor de tripsina em cultivares brasileiras de feijão (Phaseolus vulgaris L.)
title Effectiveness inactivation of trypsin inhibitor fron brazilian cultivarof beans (Phaseolus vulgaris L.)
spellingShingle Effectiveness inactivation of trypsin inhibitor fron brazilian cultivarof beans (Phaseolus vulgaris L.)
Paiva, Kelli Cristina [UNESP]
Antinutritional factor
Heat treatment
In vitro protein digestibility
Inhibitor reactivation
title_short Effectiveness inactivation of trypsin inhibitor fron brazilian cultivarof beans (Phaseolus vulgaris L.)
title_full Effectiveness inactivation of trypsin inhibitor fron brazilian cultivarof beans (Phaseolus vulgaris L.)
title_fullStr Effectiveness inactivation of trypsin inhibitor fron brazilian cultivarof beans (Phaseolus vulgaris L.)
title_full_unstemmed Effectiveness inactivation of trypsin inhibitor fron brazilian cultivarof beans (Phaseolus vulgaris L.)
title_sort Effectiveness inactivation of trypsin inhibitor fron brazilian cultivarof beans (Phaseolus vulgaris L.)
author Paiva, Kelli Cristina [UNESP]
author_facet Paiva, Kelli Cristina [UNESP]
Carvalho, Maria Regina Barbieri de [UNESP]
Pizauro Júnior, Joao Martins [UNESP]
author_role author
author2 Carvalho, Maria Regina Barbieri de [UNESP]
Pizauro Júnior, Joao Martins [UNESP]
author2_role author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv Paiva, Kelli Cristina [UNESP]
Carvalho, Maria Regina Barbieri de [UNESP]
Pizauro Júnior, Joao Martins [UNESP]
dc.subject.por.fl_str_mv Antinutritional factor
Heat treatment
In vitro protein digestibility
Inhibitor reactivation
topic Antinutritional factor
Heat treatment
In vitro protein digestibility
Inhibitor reactivation
description The trypsin inhibitor, an antinutritional factor, which is abundant in dycotiledoneous and monocotyledoneous, is usually inactivated by heating treatment. The infl uence of pressure-cooking (121°C and 141kPa) for 30 min on, trypsin inhibitors concentration and inhibitors reactivation from ten Brazilian beans varieties of Phaseolus vulgaris L. namely: IAPAR-14, IAC-Carioca, Rudá, Corrente, IAC-Aruã, IAPAR-16, IAPAR-57, IAC-Carioca Pyatã, Carioca, Aporé, were investigated. The inhibitors reactivation was evaluated in comparison with the activity of raw and pressure-cooking. For raw the in vitro protein digestibility mean values ranged from 40% (in Carioca cultivar) to 60% (in IAC-Aruã cultivar), showing an increase from 11% to 37% using the autoclaving at 121°C and 141kPa. Among ten cultivars studied the trypsin inhibitor activity varied from 36.18UTI.mg-1 for IAC-Aruã to 63.33UTI.mg-1 for IAPAR-16. Trypsin inhibitor activity was totally inactivated by pressure-cooking. The study of the trypsin inhibitors reactivation using double-digestive pepsin-pancreatin enzymes in vitro showed a recovering activity from 34% up to 100%. Native inhibitor is resistant to double- digestive pepsin-pancreatin proteolysis, whereas autoclaving to 121oC.30 min-1 results in a non-native conformation that is susceptible to proteolysis, improving the digestibility and inactivate differentially the activity of trypsin inhibitors. The results of the thermal treatment of the beans show inactivation of the inhibitors, which may be due to formation of high molecular weight aggregates with other substances of the grain. The pepsin-pancreatin digestion of the inactivated inhibitor restores the activity, probably due to its retention by the digested fragments.
publishDate 2011
dc.date.none.fl_str_mv 2011
2015-05-15T13:30:30Z
2015-05-15T13:30:30Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://serv-bib.fcfar.unesp.br/seer/index.php/alimentos/article/view/1487
Alimentos e Nutrição, v. 22, n. 3, p. 331-337, 2011.
2179-4448
http://hdl.handle.net/11449/123617
ISSN2179-4448-2011-22-03-331-337.pdf
3958124498479090
url http://serv-bib.fcfar.unesp.br/seer/index.php/alimentos/article/view/1487
http://hdl.handle.net/11449/123617
identifier_str_mv Alimentos e Nutrição, v. 22, n. 3, p. 331-337, 2011.
2179-4448
ISSN2179-4448-2011-22-03-331-337.pdf
3958124498479090
dc.language.iso.fl_str_mv por
language por
dc.relation.none.fl_str_mv Alimentos e Nutrição
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 331-337
application/pdf
dc.source.none.fl_str_mv Currículo Lattes
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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