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Food Engineering Technology
Exploration Of The Molecular Interaction Between Angiontensin-I-Converting Enzyme (ACE) And The Inhibitory Peptides Derived From Red Tilapia (Oreochromis sp.) By- Product In Lowering Blood Pressure
- Supervisor : Khairul Faizal Pa’ee
- Keywords : Red Tilapa By-Product, ACE Inhibition, ACE inhibitory Peptides
Red tilapia (Oreochromis sp.) has been a significant source of protein in a Malaysian diet. It is estimated that 725,119 metric tonnes of freshwater fish including tilapia is expected by 2020 (Marzuki, 2015). However, subsequent processing of the tilapia generates more than 60% tilapia by-product (head, skin, trimmings, fins, frames, viscera, and roe) with potential environmental issues (Ishak and Sarbon, 2017). Conversion of the by-product to protein hydrolysate has been initiated with ACE-inhibitory activity being the bioactivity of interest (Choonpicharn et al., 2015; Chuesiang and Sanguandeekul, 2015; Lin et al., 2017; Roslan et al., 2014). However, the chemical characteristics of ACE-inhibitory hydrolysate require thorough investigation. To date, detail information regarding peptides sequence and its molecular mechanism of peptide inhibitor-ACE interaction remain unknown. Thus, it is imperative to determine specific ACE-inhibitory peptides sequence derived from red tilapia by-product to elucidate the mechanism of ACE inhibition as an alternative antihypertensive ingredient yet natural.
UNIVERSITI KUALA LUMPUR
Branch Campus Malaysian Institute of Chemical & Bioengineering Technology (UniKL MICET)
Lot 1988, Kawasan Perindustrian Bandar Vendor, Taboh Naning,
78000 Alor Gajah, Melaka.
+606 – 551 2011
+606 – 551 2001
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