Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>Silybum marianum</i> flowers

The flowers of cardoon (Asteraceae) are a rich source of aspartic peptidases which possess milk clotting activity – and are thus used in traditional cheesemaking in the Iberian Peninsula. This study was aimed at characterizing the enzymatic action of the aspartic peptidases present in flowers of Sil...

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Autores principales: Vairo Cavalli, Sandra Elizabeth, Silva, Sofía V., Cimino, Cecilia Verónica, Malcata, F. Xavier, Priolo de Lufrano, Nora Silvia
Formato: Articulo
Lenguaje:Inglés
Publicado: 2008
Materias:
Biología
Rennet substitute
Proteolysis
Electrophoresis
Aspartic peptidase
Milk clotting
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/128229
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-128229
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Biología
Rennet substitute
Proteolysis
Electrophoresis
Aspartic peptidase
Milk clotting
spellingShingle Biología
Rennet substitute
Proteolysis
Electrophoresis
Aspartic peptidase
Milk clotting
Vairo Cavalli, Sandra Elizabeth
Silva, Sofía V.
Cimino, Cecilia Verónica
Malcata, F. Xavier
Priolo de Lufrano, Nora Silvia
Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>Silybum marianum</i> flowers
topic_facet Biología
Rennet substitute
Proteolysis
Electrophoresis
Aspartic peptidase
Milk clotting
description The flowers of cardoon (Asteraceae) are a rich source of aspartic peptidases which possess milk clotting activity – and are thus used in traditional cheesemaking in the Iberian Peninsula. This study was aimed at characterizing the enzymatic action of the aspartic peptidases present in flowers of Silybum marianum (L.) Gaertn. (Asteraceae), specifically upon degradation of caseins. The proteolytic activities toward Na-caseinates previously prepared from caprine and ovine milks were studied, in a comparative fashion, using urea-PAGE, tricine-SDS-PAGE, densitometry, electroblotting and sequencing. Caprine αs1- and β-caseins were degraded up to 68% and 40%, respectively, during 24 h of incubation. Only one important and well-defined band corresponding to a molecular weight of 14.4 kDa – i.e. a fragment of β-casein, was observed by 12 h of hydrolysis. By 24 h of incubation, ovine αs- and β-caseins were degraded up to 76% and 19%, respectively. In what concerns specificity, the major cleavage site in ovine caseinate was Leu99-Arg100 in αs1-casein.
format Articulo
Articulo
author Vairo Cavalli, Sandra Elizabeth
Silva, Sofía V.
Cimino, Cecilia Verónica
Malcata, F. Xavier
Priolo de Lufrano, Nora Silvia
author_facet Vairo Cavalli, Sandra Elizabeth
Silva, Sofía V.
Cimino, Cecilia Verónica
Malcata, F. Xavier
Priolo de Lufrano, Nora Silvia
author_sort Vairo Cavalli, Sandra Elizabeth
title Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>Silybum marianum</i> flowers
title_short Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>Silybum marianum</i> flowers
title_full Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>Silybum marianum</i> flowers
title_fullStr Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>Silybum marianum</i> flowers
title_full_unstemmed Hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>Silybum marianum</i> flowers
title_sort hydrolysis of caprine and ovine milk proteins, brought about by aspartic peptidases from <i>silybum marianum</i> flowers
publishDate 2008
url http://sedici.unlp.edu.ar/handle/10915/128229
work_keys_str_mv AT vairocavallisandraelizabeth hydrolysisofcaprineandovinemilkproteinsbroughtaboutbyasparticpeptidasesfromisilybummarianumiflowers
AT silvasofiav hydrolysisofcaprineandovinemilkproteinsbroughtaboutbyasparticpeptidasesfromisilybummarianumiflowers
AT ciminoceciliaveronica hydrolysisofcaprineandovinemilkproteinsbroughtaboutbyasparticpeptidasesfromisilybummarianumiflowers
AT malcatafxavier hydrolysisofcaprineandovinemilkproteinsbroughtaboutbyasparticpeptidasesfromisilybummarianumiflowers
AT priolodelufranonorasilvia hydrolysisofcaprineandovinemilkproteinsbroughtaboutbyasparticpeptidasesfromisilybummarianumiflowers
bdutipo_str Repositorios
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