Open AccessI dentification and molecular docking of novel ACE inhibitory peptides from protein hydrolysates of shrimp waste
Author(s) -
Krichen Fatma,
Sila Assaâd,
Caron Juliette,
Kobbi Sabrine,
Nedjar Naima,
Miled Nabil,
Blecker Christophe,
Besbes Souhail,
Bougatef Ali
Publication year - 2018
Publication title -
engineering in life sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.547
H-Index - 57
eISSN - 1618-2863
pISSN - 1618-0240
DOI - 10.1002/elsc.201800045
Subject(s) - hydrolysate , shrimp , chemistry , chromatography , sephadex , hydrolysis , isoelectric point , isoelectric focusing , enzyme , peptide , amino acid , biochemistry , biology , fishery
The effect of enzymatic hydrolysis by Savinase on the interfacial properties and antihypertensive activity of shrimp waste proteins was evaluated. The physicochemical characterization, interfacial tension, and surface characteristics of shrimp waste protein hydrolysates (SWPH) using different enzyme/substrate (E/S) (SWPH 5 (SWPH using E/S = 5), SWPH 15 (SWPH using E/S = 15), and SWPH 40 (SWPH using E/S = 40)) were also studied. SWPH 5 , SWPH 15 , and SWPH 40 had an isoelectric pH around 2.07, 2.17, and 2.54 respectively. SWPH 5 exhibited the lowest interfacial tension (68.96 mN/m) followed by SWPH 15 (69.36 mN/m) and SWPH 40 (70.29 mN/m). The in vitro ACE inhibitory activity of shrimp waste protein hydrolysates showed that the most active hydrolysate was obtained using an enzyme/substrate of 15 U/mg (SWPH 15 ). SWPH 15 had a lower IC 50 value (2.17 mg/mL) than that of SWPH 5 and SWPH 40 (3.65 and 5.7 mg/mL, respectively). This hydrolysate was then purified and characterized. Fraction F1 separated by Sephadex G25 column which presents the best ACE inhibition activity was then separated by reversed‐phase high performance liquid chromatography. Four ACE inhibitory peptides were identified and their molecular masses and amino acid sequences were determined using ESI–MS and ESI–MS/MS, respectively. The structures of the most potent peptides were SSSKAKKMP, HGEGGRSTHE, WLGHGGRPDHE, and WRMDIDGDIMISEQEAHQR. The structural modeling of anti‐ACE peptides from shrimp waste through docking simulations results showed that these peptides bound to ACE with high affinity.