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

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 proteoly...

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Autores principales: 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.
Formato: Articulo
Lenguaje:Inglés
Publicado: 2016
Materias:
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/92378
Aporte de:
id I19-R120-10915-92378
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Biología
Casein
Chymosin
Himatanthus drasticus
Plumeria rubra
Papain-like peptidase
Rennet
spellingShingle Biología
Casein
Chymosin
Himatanthus drasticus
Plumeria rubra
Papain-like peptidase
Rennet
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.
Insights into milk-clotting activity of latex peptidases from <i>Calotropis procera</i> and <i>Cryptostegia grandiflora</i>
topic_facet Biología
Casein
Chymosin
Himatanthus drasticus
Plumeria rubra
Papain-like peptidase
Rennet
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.
format Articulo
Articulo
author 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_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_sort Freitas, Cleverson D. T.
title Insights into milk-clotting activity of latex peptidases from <i>Calotropis procera</i> and <i>Cryptostegia grandiflora</i>
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>
publishDate 2016
url http://sedici.unlp.edu.ar/handle/10915/92378
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