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: | , , , , , , , , |
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| Formato: | Articulo |
| Lenguaje: | Inglés |
| Publicado: |
2016
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| Materias: | |
| Acceso en línea: | http://sedici.unlp.edu.ar/handle/10915/92378 |
| Aporte de: |
| id |
I19-R120-10915-92378 |
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| 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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