Application of peptidases from Maclura pomifera fruit for the production of active biopeptides from whey protein
A crude extract containing serine peptidases, was prepared from latex of Maclura pomifera fruits. Peptidases were isolated by precipitation with one volume of ethanol with a yield of 5.4 ± 0.4 Ucas per milligram of protein. This extract was used for hydrolysis of bovine whey proteins at 45 °C and pH...
| Autores: | , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2015 |
| País: | Argentina |
| Institución: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositorio: | CONICET Digital (CONICET) |
| Idioma: | inglés |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/53698 |
| Acceso en línea: | http://hdl.handle.net/11336/53698 |
| Access Level: | acceso abierto |
| Palabra clave: | Bioactive Peptide Maclura Pomifera Plant Peptidase Whey Hydrolysate |
| Sumario: | A crude extract containing serine peptidases, was prepared from latex of Maclura pomifera fruits. Peptidases were isolated by precipitation with one volume of ethanol with a yield of 5.4 ± 0.4 Ucas per milligram of protein. This extract was used for hydrolysis of bovine whey proteins at 45 °C and pH 6.5. Proteolytic activity was 99% inactivated after 5 min of heat treatment (100 °C). Major whey proteins degradation profile was analysed by tricine SDS-PAGE. After 180 min of hydrolysis alpha-lactalbumin (α-LA) and beta-lactoglobulin (β-LG) were almost completely degraded. Hydrolysis degree was 31.3 ± 1.7% at 180 min of reaction and the peptides produced that were smaller than 3 kDa were analysed by reversed-phase high-performance liquid chromatography (RP-HPLC). Angiotensin-converting enzyme (ACE) inhibitory activity and antioxidant capacity were detected in the hydrolysates and IC50 values for 180 min of hydrolysis were 0.53 ± 0.02 and 4.44 ± 0.44 mg/ml, respectively. One peptide sequence deduced from peptide masses in the 180 min filtered hydrolysate, coincided with an ACE-inhibitory peptide reported by other author. The results support the conclusion that, by the presence of ACE-inhibitory and antioxidant peptides, it would be possible to use these whey protein hydrolysates for functional food manufacturing. |
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