Dairy Debaryomyces hansenii strains produce the antihypertensive casein-derived peptides LHLPLP and HLPLP
The ability of dairy Debaryomyces hansenii, Kluyveromyces lactis and Kluyveromyces marxianus strains to release the casein-derived antihypertensive sequences RYLGY, AYFYPEL, LHLPLP, HLPLP, VPP and/or IPP was examined. Yeast strains were grown in medium with casein as sole nitrogen source and the yea...
| Autores: | , , , , |
|---|---|
| Tipo de recurso: | artículo |
| Estado: | Versión aceptada para publicación |
| Fecha de publicación: | 2014 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/148426 |
| Acceso en línea: | http://hdl.handle.net/10261/148426 |
| Access Level: | acceso abierto |
| Palabra clave: | Dairy yeasts Debaryomyces hansenii Kluyveromyces lactis Kluyveromyces marxianus Casein-derived antihypertensive peptides |
| Sumario: | The ability of dairy Debaryomyces hansenii, Kluyveromyces lactis and Kluyveromyces marxianus strains to release the casein-derived antihypertensive sequences RYLGY, AYFYPEL, LHLPLP, HLPLP, VPP and/or IPP was examined. Yeast strains were grown in medium with casein as sole nitrogen source and the yeast casein hydrolysates (CSHs) were analysed by HPLC-MS/MS to search for the six antihypertensive sequences. Only LHLPLP and HLPLP were identified in CSHs and exclusively in D. hansenii Dh1 and Dh14 hydrolysates in which both antihypertensive sequences represented approximately 6 (CSH Dh1) and 10% (CSH Dh14) of total peptide content. In addition, a complete analysis of selected CSHs by HPLC-MS/MS allowed the identification of 35 (Dh1) and 46 (Dh14) additional peptides, which could also contribute to the observed in vitro ACE inhibitory potency of both hydrolysates (Dh1, IC50 = 13.6 ± 1.8 μg/mL; Dh14, IC50 = 17.5 ± 2.1 μg/mL) and might confer them multifunctional properties. Finally casein zymography revealed the presence of at least one extracellular protease with a molecular mass of about 50 kDa. In conclusion, the present study contributes to a better insight into bioactive compounds produced by dairy yeasts and shows the feasibility of D. hansenii strains to produce antihypertensive casein-derived peptides. |
|---|