Insights into milk-clotting activity of latex peptidases from Calotropis procera and Cryptostegia grandiflora |
| |
| Affiliation: | 1. Department of Biochemistry and Molecular Biology, Federal University of Ceara, Campus do Pici, Cx. Postal 6033, Fortaleza, CEP 60451-970, Ceara, Brazil;2. Brazilian Agricultural Research Corporation, Embrapa Goats and Sheep, Estrada Sobral Groaíras km 4, Sobral, Ceara, Brazil;3. Department of Biological Sciences, Faculty of Exact Sciences, Plant Proteins Research Centre (CIProVe), National University of La Plata, La Plata, Argentina;4. NUBEX - Núcleo de Biologia Experimental, Centro de Ciências da Saúde, Universidade de Fortaleza-UNIFOR, Fortaleza, CE, Brazil;1. Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Centro de Ciências, Campus do Pici. Fortaleza, Ceará, CEP 60440-900, Brazil;2. Fundação Oswaldo Cruz, Fiocruz-Ceará, Brazil;3. Departamento de Engenharia de Pesca, Universidade Federal do Ceará, Fortaleza, CE, Brazil |
| |
| Abstract: | 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. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
