Safitri, Nur Maulida (2017) Screening of Bioactive Peptides with Angiotensin-I Converting Enzyme Inhibition and Antioxidative Activities from Enzymatic Hydrolysates of Spirulina platensis and Chlorella sorokiniana. Magister thesis, Universitas Brawijaya.
Abstract
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English Abstract
Angiotensin-I Converting Enzyme (ACE, EC 3.4.15.1) plays an important role in Renin Angiotensin Aldosterone System (RAAS) and Kallikrein Kinin System (KKS) system of blood pressure regulation. ACE inhibitors (ACEi) are widely used to treat hypertension. Chlorella sorokiniana and Spirulina platensis are edible microalgae with high protein content (40-70% of its dry weight) and have been used as nutraceuticals and functional foods due to its biological activities. Different enzymes have been used for the digestion of S. platensis protein (SPP) containing v antihypertensive peptides such as alcalase (Lu et al., 2010) and pepsin (Suetsuna et al., 2001) can be found in the literature, whereas there has no antihypertensive peptide from C. sorokiniana protein (CSP) been reported yet. It has been suggested that thermolysin is the most preferrable due to its broad specificity to generate hydrophobic residues at peptide N-termini. Nevertheless, the use of this enzyme for digesting CSP and SPP peptide has not been elucidated. In this study, thermolysin hydrolysate inhibited 82.60±0.16% and 80.54±0.75% ACE activity at 83.3 μg/mL, which demonstrated potent ACEi activity compared with other enzymes. Subsequently, the thermolysin hydrolysate then was fractionated using two orthogonal bioasssay-guided fractionations using reversed-phase high performance liquid chromatography (RP-HPLC) and strong-cation exchange chromatography (SCX) separation. Peptides YR5 & IK15 from CSP and IR5 & FY11 were characterized and IR5 peptide was further examine its ACE inhibitory activity due to its lowest IC50 (10.54±1.38 μM). This peptide was regarded as non-competitive ACE inhibitor according to inhibition kinetics study. Molecular docking simulation was further conducted to predict the interaction between IR5 and ACE. The result indicates that the preferable interaction is out of ACE active site, which is consistent with the result obtained from inhibition kinetics. Preliminary studies was also conducted to find potential peptide as antioxidant. Our result demonstrate that CSP and SPP are promising material to obtain potential bioactive peptide as ACE inhibitor and antioxidant in the prevention and treatment of hypertension.
| Item Type: | Thesis (Magister) |
|---|---|
| Identification Number: | TES/612.015 756/SAF/s/2017/041706907 |
| Uncontrolled Keywords: | PEPTIDES, ANGIOTENSINS, ENZYANE INHIBITORS, ANTIOXIDANTS, PROTEIN HYDROLYSATES, SPIRULINA, CHLORELLA |
| Subjects: | 600 Technology (Applied sciences) > 612 Human Physiology > 612.01 Biophysics and biochemistry > 612.015 28 Pigments > 612.015 75 Proteins |
| Divisions: | S2/S3 > Magister Bioteknologi Perikanan dan Kelautan, Fakultas Perikanan dan Ilmu Kelautan |
| Depositing User: | Nur Cholis |
| Date Deposited: | 21 Aug 2017 02:00 |
| Last Modified: | 18 Nov 2022 07:45 |
| URI: | http://repository.ub.ac.id/id/eprint/1443 |
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