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Separation and identification of ACE inhibitory peptides from cashew nut ( Anacardium occidentale Linnaeus) protein.
- Source :
-
International Journal of Food Properties . 2017 Supplement, Vol. 20, pS981-S991. 11p. 3 Charts, 5 Graphs. - Publication Year :
- 2017
-
Abstract
- Cashew nut protein powder was hydrolysed by alkaline protease to prepare ACE inhibitory peptides. Results showed that the optimum conditions were: substrate concentration, 7 g/100 mL; amount of enzyme, 3%; pH, 10.5; hydrolysis time, 6 h; and temperature, 45°C. Under these conditions, ACE inhibitory rate was 57.45%. ACE inhibitory peptides were filtered using an ultrafiltration membrane of different molecular weights and Sephadex G-15 gel column. We found that the molecular weight was <3000 Da, and the ACE inhibitory rate concentration was 100 mg/mL. The M2component, which was the most active component in ACE inhibitory peptides, yielded an ACE inhibitory rate of 77.58%. The M2component contained 18 types of amino acids, including seven types of essential amino acids with the highest proline content reaching 23.56% (P< 0.01). The molecular weight of the M2constituent was observed as 389 Da, with an amino acid sequence of Glu- Ser - Arg. [ABSTRACT FROM AUTHOR]
- Subjects :
- *CASHEW nuts
*PROTEINS
*HYDROLYSIS
*ALKALINE phosphatase
*PEPTIDES
Subjects
Details
- Language :
- English
- ISSN :
- 10942912
- Volume :
- 20
- Database :
- Academic Search Index
- Journal :
- International Journal of Food Properties
- Publication Type :
- Academic Journal
- Accession number :
- 127560827
- Full Text :
- https://doi.org/10.1080/10942912.2017.1325902