ACE-Inhibitory Peptides

from Aquatic Resources

Deny Tri Prastyo (C351180071)
Aquatic Product Technology
Graduate School of IPB
Journal Review

• Antioxidant and angiotensin-I converting enzyme inhibitory

peptides from Hippocampus abdominalis (Kim et al., 2018)

• Angiotensin-Converting Enzyme Inhibition In Vitro by Protein

Hydrolysates and Peptide Fractions from Mojarra of Nile Tilapia
(Oreochromis niloticus) Skeleton (Borges et al., 2019)
Introduction

(Borges et al., 2019)

Bioactive Peptide

ACE-Inhibitor
(Kim et al., 2018)
ACE Inhibitory Mechanism

(Sciencedirect, 2018)
 Materials & Methods

(Kim et al., 2018) (Borges et al., 2019)

• Seahorse (Hippocampus abdominalis) • Nile tilapia (Oreochromis niloticus)

• Alcalase Enzyme • Alcalase & Flavourzyme Enzyme
• Sephadex G-10 • HHL ACE synthetic substrat
• ACE inhibition potential evaluation kit • ACE Enzyme from rabbit lung
 H. abdominalis Research Procedure
(Kim et al., 2018)
Preparation of alcalase hydrolysate

Protein hydrolisate ACE inhibitory activity

Ultrafiltration (5 kDa & 10 kDa membranes)

Peptide

Gel Filtration (Sephadex G-10)

Amino Acid Sequence (LC-MS/MS)
Bioactive Peptide ACE inhibitory Activity
Molecular Docking

Tilapia skeleton flour
Hydrolysis using alcalase & flavourzyme
(0, 20,40, 60, 80 & 100 minutes
Protein hydrolisate
Ultrafiltration
(using 1, 3, 5 & 10 kDa membranes)
Bioactive Peptide
Chemical Composition
Determination of Color
Energy Value
Degree of Hydrolysis
Molecular Mass (SDS PAGE)
ACE Inhibitory Activity
Research Procedure
(Borges et al., 2019)
ACE inhibitory Activity
Results & Discussion
(Kim et al., 2018)
Amino Acid Sequences & Bioactivity
Results & Discussion
(Borges et al., 2019)
Degree of Hydrolysis
Molecular Weight
Flavourzyme Alcalase
ACE-Inhibitory Activity
ACE-Inhibitory Activity
Conclusion (Borges et al., 2019)
• The use of the enzymes Flavourzyme and Alcalase individually
achieved extensive hydrolysates from the protein-rich flour of the
mojarra of Nile tilapia (O. niloticus) skeleton.
• The electrophoretic patterns obtained by SDS-PAGE of these
hydrolysates showed low MW protein bands, thus suggesting the
presence of bioactive peptides on hydrolysates.
• The hydrolysates showed ACE inhibitory activity in all their reaction
times, the hydrolyzate having greater activity with Flavourzyme at
60min and with Alcalase at 80min of reaction.
• Peptide fractions obtained by UF that showed greater activity were
peptide fraction C (5–3kDa) with both enzymes.
• So they could have applications as a functional ingredient in the
design and development of specialized foods.
Conclusion (Kim et al., 2018)

• The current study demonstrates the potential ACE inhibition

activities of novel nine peptides isolated from the alcalase
hydrolysate of H. abdominalis.
• The sequences of the active peptides were evaluated to be
(GIIGPSGSP, HA-III-b-4), (IGTGIPGIW, HA-IIIb-5) and (QIGFIW,
HA-III-b-6).
• These three active peptides showed a signifiantly ACE inhibition
activity. Hydrolysates or oligopeptides derived from H. abdominalis
containing three active peptides could be applied to industry as a
functional food or as a healthy dietary supplement for the prevention
of healthy disorders.
Thank you for your attention