Study of the angiotensin I converting enzyme inhibitory peptides from royal jelly and bee larva
| Autor: | Huei-Yuan Chen, 陳惠媛 |
|---|---|
| Rok vydání: | 2015 |
| Druh dokumentu: | 學位論文 ; thesis |
| Popis: | 103 In this research, water soluble protein of RJ and bee larva will be extracted and then hydrolyzed in vitro by gastrointestinal enzymes, pepsin and trypsin. After enzymatic treatment for 36 h, the angiotensin converting enzyme (ACE) inhibitory activities of the protein hydrolysates were evaluated. The results revealed that: in RJ group, that the degree of hydrolysis (DH) of the hydrolysate by pepsin for 36 h was 60.63% and the ACE inhibitory activity was 84.88%. While the DH of the hydrolysate by trypsin for 36 hours was 89.66 % and the ACE inhibitory activity was 94.02%. As for the bee larva group, the DH of the hydrolysate by pepsin for 36 h was 50.88% and the ACE inhibitory activity was 95.12%. While the DH of the hydrolysate by trypsin for 36 hours was 50.75% and the ACE inhibitory activity was 97.35%. Furthermore, the bioactive peptides in RJ and bee larva protein hydrolysate were purification by microfiltration (MWCO 5,000 and 2,000) and anion ion-exchange column (DEAE column). Two active fractions (IC50 value are 0.32 and 0.17 mg/mL) derived from royal jelly and bee larva which hydrolyzed by trypsin were purification and desalted by high performance liquid chromatography. These results indicated that, after hydrolyzed with protease, royal jelly and bee larva both have potential to develop antihypertensive functional foods. |
| Databáze: | Networked Digital Library of Theses & Dissertations |
| Externí odkaz: |
|