LENTIL TANNIN-GLOBULIN INTERACTIONAND AND IN VITRO HYDROLYSIS
Autor(a) principal: | |
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Data de Publicação: | 1998 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Food Science and Technology (Campinas) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20611998000300017 |
Resumo: | Protein fractions were isolated from lentil cotyledons and tannins were isolated and purified from lentil seed coats. The globulin fraction corresponded to 42.7% of the total lentil flour nitrogen, representing the major protein fraction. Acetone:water (7:3) was the best extractant for seed coat tannins compared to methanol or methanol-HCl 1%. Native and heated (99oC/15 min.) isolated lentil globulin and casein were hydrolyzed with trypsin and pepsin in the absence of tannins and at 1:40, 1:20, 1:10, 1:5 and 1:2.5 tannin-to-protein ratios. The tryptic and peptic hydrolysis of the unheated proteins were reduced with increasing tannin-to-protein ratios. Unheated casein showed to be more susceptible to trypsin than globulin and the opposite effect was observed with pepsin. Heating followed by tannin interaction and hydrolysis had a more pronounced effect on tryptic than peptic digestion for both proteins. |
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Food Science and Technology (Campinas) |
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LENTIL TANNIN-GLOBULIN INTERACTIONAND AND IN VITRO HYDROLYSISLens culinarislentiltanninglobulinin vitro hydrolysisProtein fractions were isolated from lentil cotyledons and tannins were isolated and purified from lentil seed coats. The globulin fraction corresponded to 42.7% of the total lentil flour nitrogen, representing the major protein fraction. Acetone:water (7:3) was the best extractant for seed coat tannins compared to methanol or methanol-HCl 1%. Native and heated (99oC/15 min.) isolated lentil globulin and casein were hydrolyzed with trypsin and pepsin in the absence of tannins and at 1:40, 1:20, 1:10, 1:5 and 1:2.5 tannin-to-protein ratios. The tryptic and peptic hydrolysis of the unheated proteins were reduced with increasing tannin-to-protein ratios. Unheated casein showed to be more susceptible to trypsin than globulin and the opposite effect was observed with pepsin. Heating followed by tannin interaction and hydrolysis had a more pronounced effect on tryptic than peptic digestion for both proteins.Sociedade Brasileira de Ciência e Tecnologia de Alimentos1998-08-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20611998000300017Food Science and Technology v.18 n.3 1998reponame:Food Science and Technology (Campinas)instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)instacron:SBCTA10.1590/S0101-20611998000300017info:eu-repo/semantics/openAccessNEVES,Valdir A.LOURENÇO,Euclides J.eng1999-05-20T00:00:00Zoai:scielo:S0101-20611998000300017Revistahttp://www.scielo.br/ctaONGhttps://old.scielo.br/oai/scielo-oai.php||revista@sbcta.org.br1678-457X0101-2061opendoar:1999-05-20T00:00Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)false |
dc.title.none.fl_str_mv |
LENTIL TANNIN-GLOBULIN INTERACTIONAND AND IN VITRO HYDROLYSIS |
title |
LENTIL TANNIN-GLOBULIN INTERACTIONAND AND IN VITRO HYDROLYSIS |
spellingShingle |
LENTIL TANNIN-GLOBULIN INTERACTIONAND AND IN VITRO HYDROLYSIS NEVES,Valdir A. Lens culinaris lentil tannin globulin in vitro hydrolysis |
title_short |
LENTIL TANNIN-GLOBULIN INTERACTIONAND AND IN VITRO HYDROLYSIS |
title_full |
LENTIL TANNIN-GLOBULIN INTERACTIONAND AND IN VITRO HYDROLYSIS |
title_fullStr |
LENTIL TANNIN-GLOBULIN INTERACTIONAND AND IN VITRO HYDROLYSIS |
title_full_unstemmed |
LENTIL TANNIN-GLOBULIN INTERACTIONAND AND IN VITRO HYDROLYSIS |
title_sort |
LENTIL TANNIN-GLOBULIN INTERACTIONAND AND IN VITRO HYDROLYSIS |
author |
NEVES,Valdir A. |
author_facet |
NEVES,Valdir A. LOURENÇO,Euclides J. |
author_role |
author |
author2 |
LOURENÇO,Euclides J. |
author2_role |
author |
dc.contributor.author.fl_str_mv |
NEVES,Valdir A. LOURENÇO,Euclides J. |
dc.subject.por.fl_str_mv |
Lens culinaris lentil tannin globulin in vitro hydrolysis |
topic |
Lens culinaris lentil tannin globulin in vitro hydrolysis |
description |
Protein fractions were isolated from lentil cotyledons and tannins were isolated and purified from lentil seed coats. The globulin fraction corresponded to 42.7% of the total lentil flour nitrogen, representing the major protein fraction. Acetone:water (7:3) was the best extractant for seed coat tannins compared to methanol or methanol-HCl 1%. Native and heated (99oC/15 min.) isolated lentil globulin and casein were hydrolyzed with trypsin and pepsin in the absence of tannins and at 1:40, 1:20, 1:10, 1:5 and 1:2.5 tannin-to-protein ratios. The tryptic and peptic hydrolysis of the unheated proteins were reduced with increasing tannin-to-protein ratios. Unheated casein showed to be more susceptible to trypsin than globulin and the opposite effect was observed with pepsin. Heating followed by tannin interaction and hydrolysis had a more pronounced effect on tryptic than peptic digestion for both proteins. |
publishDate |
1998 |
dc.date.none.fl_str_mv |
1998-08-01 |
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=S0101-20611998000300017 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20611998000300017 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0101-20611998000300017 |
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 |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos |
publisher.none.fl_str_mv |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos |
dc.source.none.fl_str_mv |
Food Science and Technology v.18 n.3 1998 reponame:Food Science and Technology (Campinas) instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) instacron:SBCTA |
instname_str |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) |
instacron_str |
SBCTA |
institution |
SBCTA |
reponame_str |
Food Science and Technology (Campinas) |
collection |
Food Science and Technology (Campinas) |
repository.name.fl_str_mv |
Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) |
repository.mail.fl_str_mv |
||revista@sbcta.org.br |
_version_ |
1752126309645942784 |