Potential of quixaba (Sideroxylon obtusifolium) latex as a milk-clotting agent
Autor(a) principal: | |
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Data de Publicação: | 2013 |
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=S0101-20612013000300017 |
Resumo: | There are several obstacles to the use of chymosin in cheese production. Consequently, plant proteases have been studied as possible rennet substitutes, but most of these enzymes are unsuitable for the manufacture of cheese. The aim of this study was to evaluate the potential of latex from Sideroxylon obtusifolium as a source of milk-clotting proteases and to partially characterize the enzyme. The enzyme extract showed high protease and coagulant activities, with an optimal pH of 8.0 and temperature of 55 °C. The enzyme was stable in wide ranges of temperature and pH. Its activity was not affected by any metal ions tested; but was inhibited by phenylmethanesulfonyl fluoride and pepstatin. For the coagulant activity, the optimal concentration of CaCl2 was 10 µmol L- 1. Polyacrylamide gel electrophoresis showed four bands, with molecular weights between 17 and 64 kDa. These results indicate that the enzyme can be applied to the cheese industry. |
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Food Science and Technology (Campinas) |
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Potential of quixaba (Sideroxylon obtusifolium) latex as a milk-clotting agentproteolytic activityplant proteasesrennetThere are several obstacles to the use of chymosin in cheese production. Consequently, plant proteases have been studied as possible rennet substitutes, but most of these enzymes are unsuitable for the manufacture of cheese. The aim of this study was to evaluate the potential of latex from Sideroxylon obtusifolium as a source of milk-clotting proteases and to partially characterize the enzyme. The enzyme extract showed high protease and coagulant activities, with an optimal pH of 8.0 and temperature of 55 °C. The enzyme was stable in wide ranges of temperature and pH. Its activity was not affected by any metal ions tested; but was inhibited by phenylmethanesulfonyl fluoride and pepstatin. For the coagulant activity, the optimal concentration of CaCl2 was 10 µmol L- 1. Polyacrylamide gel electrophoresis showed four bands, with molecular weights between 17 and 64 kDa. These results indicate that the enzyme can be applied to the cheese industry.Sociedade Brasileira de Ciência e Tecnologia de Alimentos2013-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612013000300017Food Science and Technology v.33 n.3 2013reponame:Food Science and Technology (Campinas)instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)instacron:SBCTA10.1590/S0101-20612013005000075info:eu-repo/semantics/openAccessSilva,Anna Carolina daNascimento,Talita Camila Evaristo da SilvaSilva,Sheylla Araújo daHerculano,Polyanna NunesMoreira,Keila Aparecidaeng2013-10-08T00:00:00Zoai:scielo:S0101-20612013000300017Revistahttp://www.scielo.br/ctaONGhttps://old.scielo.br/oai/scielo-oai.php||revista@sbcta.org.br1678-457X0101-2061opendoar:2013-10-08T00:00Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)false |
dc.title.none.fl_str_mv |
Potential of quixaba (Sideroxylon obtusifolium) latex as a milk-clotting agent |
title |
Potential of quixaba (Sideroxylon obtusifolium) latex as a milk-clotting agent |
spellingShingle |
Potential of quixaba (Sideroxylon obtusifolium) latex as a milk-clotting agent Silva,Anna Carolina da proteolytic activity plant proteases rennet |
title_short |
Potential of quixaba (Sideroxylon obtusifolium) latex as a milk-clotting agent |
title_full |
Potential of quixaba (Sideroxylon obtusifolium) latex as a milk-clotting agent |
title_fullStr |
Potential of quixaba (Sideroxylon obtusifolium) latex as a milk-clotting agent |
title_full_unstemmed |
Potential of quixaba (Sideroxylon obtusifolium) latex as a milk-clotting agent |
title_sort |
Potential of quixaba (Sideroxylon obtusifolium) latex as a milk-clotting agent |
author |
Silva,Anna Carolina da |
author_facet |
Silva,Anna Carolina da Nascimento,Talita Camila Evaristo da Silva Silva,Sheylla Araújo da Herculano,Polyanna Nunes Moreira,Keila Aparecida |
author_role |
author |
author2 |
Nascimento,Talita Camila Evaristo da Silva Silva,Sheylla Araújo da Herculano,Polyanna Nunes Moreira,Keila Aparecida |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
Silva,Anna Carolina da Nascimento,Talita Camila Evaristo da Silva Silva,Sheylla Araújo da Herculano,Polyanna Nunes Moreira,Keila Aparecida |
dc.subject.por.fl_str_mv |
proteolytic activity plant proteases rennet |
topic |
proteolytic activity plant proteases rennet |
description |
There are several obstacles to the use of chymosin in cheese production. Consequently, plant proteases have been studied as possible rennet substitutes, but most of these enzymes are unsuitable for the manufacture of cheese. The aim of this study was to evaluate the potential of latex from Sideroxylon obtusifolium as a source of milk-clotting proteases and to partially characterize the enzyme. The enzyme extract showed high protease and coagulant activities, with an optimal pH of 8.0 and temperature of 55 °C. The enzyme was stable in wide ranges of temperature and pH. Its activity was not affected by any metal ions tested; but was inhibited by phenylmethanesulfonyl fluoride and pepstatin. For the coagulant activity, the optimal concentration of CaCl2 was 10 µmol L- 1. Polyacrylamide gel electrophoresis showed four bands, with molecular weights between 17 and 64 kDa. These results indicate that the enzyme can be applied to the cheese industry. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013-09-01 |
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=S0101-20612013000300017 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612013000300017 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0101-20612013005000075 |
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.33 n.3 2013 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_ |
1752126318629093376 |