Insights into milk-clotting activity of latex peptidases from <i>Calotropis procera</i> and <i>Cryptostegia grandiflora</i>

Autores
Freitas, Cleverson D. T.; Leite, Hugo B.; Oliveira, João B. P.; Amaral, Jackson L.; Egito, Antônio S.; Vairo Cavalli, Sandra Elizabeth; Lobo, Marina D. P.; Monteiro Moreira, Ana C. O.; Ramos, Márcio V.
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Latex fractions from Calotropis procera, Cryptostegia grandiflora, Plumeria rubra, and Himatanthus drasticus were assayed in order to prospect for new plant peptidases with milk-clotting activities, for use as rennet alternatives. Only C. procera and C. grandiflora latex fractions exhibited proteolytic and milk-clotting activities, which were not affected by high concentrations of NaCl and CaCl2. However, pre-incubation of both samples at 75 °C for 10 min eliminated completely their activities. Both proteolytic fractions were able to hydrolyze k-casein and to produce peptides of 16 kDa, a similar SDS-PAGE profile to commercial chymosin. RP-HPLC and mass spectrometry analyses of the k-casein peptides showed that the peptidases from C. procera or C. grandiflora hydrolyzed k-casein similar to commercial chymosin. The cheeses made with both latex peptidases exhibited yields, dry masses, and soluble proteins similar to cheeses prepared with commercial chymosin. In conclusion, C. procera and C. grandiflora latex peptidases with the ability to coagulate milk can be used as alternatives to commercial animal chymosin in the cheese manufacturing process.
Centro de Investigación de Proteínas Vegetales
Materia
Biología
Casein
Chymosin
Himatanthus drasticus
Plumeria rubra
Papain-like peptidase
Rennet
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/92378
Acceder
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repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Insights into milk-clotting activity of latex peptidases from <i>Calotropis procera</i> and <i>Cryptostegia grandiflora</i>Freitas, Cleverson D. T.Leite, Hugo B.Oliveira, João B. P.Amaral, Jackson L.Egito, Antônio S.Vairo Cavalli, Sandra ElizabethLobo, Marina D. P.Monteiro Moreira, Ana C. O.Ramos, Márcio V.BiologíaCaseinChymosinHimatanthus drasticusPlumeria rubraPapain-like peptidaseRennetLatex fractions from Calotropis procera, Cryptostegia grandiflora, Plumeria rubra, and Himatanthus drasticus were assayed in order to prospect for new plant peptidases with milk-clotting activities, for use as rennet alternatives. Only C. procera and C. grandiflora latex fractions exhibited proteolytic and milk-clotting activities, which were not affected by high concentrations of NaCl and CaCl2. However, pre-incubation of both samples at 75 °C for 10 min eliminated completely their activities. Both proteolytic fractions were able to hydrolyze k-casein and to produce peptides of 16 kDa, a similar SDS-PAGE profile to commercial chymosin. RP-HPLC and mass spectrometry analyses of the k-casein peptides showed that the peptidases from C. procera or C. grandiflora hydrolyzed k-casein similar to commercial chymosin. The cheeses made with both latex peptidases exhibited yields, dry masses, and soluble proteins similar to cheeses prepared with commercial chymosin. In conclusion, C. procera and C. grandiflora latex peptidases with the ability to coagulate milk can be used as alternatives to commercial animal chymosin in the cheese manufacturing process.Centro de Investigación de Proteínas Vegetales2016info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf50-59http://sedici.unlp.edu.ar/handle/10915/92378enginfo:eu-repo/semantics/altIdentifier/issn/0963-9969info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodres.2016.06.020info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-10-15T11:11:05Zoai:sedici.unlp.edu.ar:10915/92378Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-15 11:11:06.137SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Insights into milk-clotting activity of latex peptidases from <i>Calotropis procera</i> and <i>Cryptostegia grandiflora</i>
title Insights into milk-clotting activity of latex peptidases from <i>Calotropis procera</i> and <i>Cryptostegia grandiflora</i>
spellingShingle Insights into milk-clotting activity of latex peptidases from <i>Calotropis procera</i> and <i>Cryptostegia grandiflora</i>
Freitas, Cleverson D. T.
Biología
Casein
Chymosin
Himatanthus drasticus
Plumeria rubra
Papain-like peptidase
Rennet
title_short Insights into milk-clotting activity of latex peptidases from <i>Calotropis procera</i> and <i>Cryptostegia grandiflora</i>
title_full Insights into milk-clotting activity of latex peptidases from <i>Calotropis procera</i> and <i>Cryptostegia grandiflora</i>
title_fullStr Insights into milk-clotting activity of latex peptidases from <i>Calotropis procera</i> and <i>Cryptostegia grandiflora</i>
title_full_unstemmed Insights into milk-clotting activity of latex peptidases from <i>Calotropis procera</i> and <i>Cryptostegia grandiflora</i>
title_sort Insights into milk-clotting activity of latex peptidases from <i>Calotropis procera</i> and <i>Cryptostegia grandiflora</i>
dc.creator.none.fl_str_mv Freitas, Cleverson D. T.
Leite, Hugo B.
Oliveira, João B. P.
Amaral, Jackson L.
Egito, Antônio S.
Vairo Cavalli, Sandra Elizabeth
Lobo, Marina D. P.
Monteiro Moreira, Ana C. O.
Ramos, Márcio V.
author Freitas, Cleverson D. T.
author_facet Freitas, Cleverson D. T.
Leite, Hugo B.
Oliveira, João B. P.
Amaral, Jackson L.
Egito, Antônio S.
Vairo Cavalli, Sandra Elizabeth
Lobo, Marina D. P.
Monteiro Moreira, Ana C. O.
Ramos, Márcio V.
author_role author
author2 Leite, Hugo B.
Oliveira, João B. P.
Amaral, Jackson L.
Egito, Antônio S.
Vairo Cavalli, Sandra Elizabeth
Lobo, Marina D. P.
Monteiro Moreira, Ana C. O.
Ramos, Márcio V.
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Biología
Casein
Chymosin
Himatanthus drasticus
Plumeria rubra
Papain-like peptidase
Rennet
topic Biología
Casein
Chymosin
Himatanthus drasticus
Plumeria rubra
Papain-like peptidase
Rennet
dc.description.none.fl_txt_mv Latex fractions from Calotropis procera, Cryptostegia grandiflora, Plumeria rubra, and Himatanthus drasticus were assayed in order to prospect for new plant peptidases with milk-clotting activities, for use as rennet alternatives. Only C. procera and C. grandiflora latex fractions exhibited proteolytic and milk-clotting activities, which were not affected by high concentrations of NaCl and CaCl2. However, pre-incubation of both samples at 75 °C for 10 min eliminated completely their activities. Both proteolytic fractions were able to hydrolyze k-casein and to produce peptides of 16 kDa, a similar SDS-PAGE profile to commercial chymosin. RP-HPLC and mass spectrometry analyses of the k-casein peptides showed that the peptidases from C. procera or C. grandiflora hydrolyzed k-casein similar to commercial chymosin. The cheeses made with both latex peptidases exhibited yields, dry masses, and soluble proteins similar to cheeses prepared with commercial chymosin. In conclusion, C. procera and C. grandiflora latex peptidases with the ability to coagulate milk can be used as alternatives to commercial animal chymosin in the cheese manufacturing process.
Centro de Investigación de Proteínas Vegetales
description Latex fractions from Calotropis procera, Cryptostegia grandiflora, Plumeria rubra, and Himatanthus drasticus were assayed in order to prospect for new plant peptidases with milk-clotting activities, for use as rennet alternatives. Only C. procera and C. grandiflora latex fractions exhibited proteolytic and milk-clotting activities, which were not affected by high concentrations of NaCl and CaCl2. However, pre-incubation of both samples at 75 °C for 10 min eliminated completely their activities. Both proteolytic fractions were able to hydrolyze k-casein and to produce peptides of 16 kDa, a similar SDS-PAGE profile to commercial chymosin. RP-HPLC and mass spectrometry analyses of the k-casein peptides showed that the peptidases from C. procera or C. grandiflora hydrolyzed k-casein similar to commercial chymosin. The cheeses made with both latex peptidases exhibited yields, dry masses, and soluble proteins similar to cheeses prepared with commercial chymosin. In conclusion, C. procera and C. grandiflora latex peptidases with the ability to coagulate milk can be used as alternatives to commercial animal chymosin in the cheese manufacturing process.
publishDate 2016
dc.date.none.fl_str_mv 2016
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/92378
url http://sedici.unlp.edu.ar/handle/10915/92378
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0963-9969
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodres.2016.06.020
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
50-59
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repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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