In vitro Angiotesin-1-converting enzyme, α-amylase and α-glucosidase inhibitory and antioxidant activities of Luffa cylindrical (L.) M. Roem seed protein hydrolysate

Rotimi Olusanya Arise; Jalil James Idi; Iseoluwa Maureen Mic-Braimoh; Emmanuel Korode; Risikat Nike Ahmed; Omorefosa Osemwegie

doi:10.1016/j.heliyon.2019.e01634

In vitro Angiotesin-1-converting enzyme, α-amylase and α-glucosidase inhibitory and antioxidant activities of Luffa cylindrical (L.) M. Roem seed protein hydrolysate

Heliyon. 2019 May 7;5(5):e01634. doi: 10.1016/j.heliyon.2019.e01634. eCollection 2019 May.

Authors

Rotimi Olusanya Arise^{1

2}, Jalil James Idi^{1

3}, Iseoluwa Maureen Mic-Braimoh¹, Emmanuel Korode¹, Risikat Nike Ahmed⁴, Omorefosa Osemwegie²

Affiliations

¹ Department of Biochemistry, Faculty of Life Sciences, University of Ilorin, Ilorin, Nigeria.
² Department of Biological Sciences, College of Science and Engineering, Landmark University, Omu-Aran, Nigeria.
³ Department of Biochemistry, Faculty of Sciences, Gombe State University, Gombe, Nigeria.
⁴ Department of Microbiology, Faculty of Life Sciences, University of Ilorin, Ilorin, Nigeria.

Abstract

In recent times, researchers have explored food derived peptides to circumvent the side effects of synthetic drugs. This study therefore examined the amino acid constituents, in vitro antioxidant activities, angiotensin-1-converting enzyme (ACE), α-glucosidase and α-amylase inhibition kinetics of protein hydrolysate obtained from the seed of Luffa cylindrica. The peptide yield by pepsin (16.93 ± 0.28%) and trypsin (13.20 ± 1.02%) were significantly lower than that of Alcalase (34.04 ± 1.96%). Alcalase hydrolysate however displayed the highest ferric reducing antioxidant capacity (FRAC), 1,1-diphenyl-2-picrylhydrazyl (DPPH) and H₂O₂ scavenging activities (0.63%, 85.88% and 41.69% respectively), while the highest superoxide scavenging activity was shown by peptic hydrolysate (57.89%). The ACE inhibition by the hydrolysates with IC₅₀ of 0.32-0.93 mg/mL, increased as the concentration of the peptic hydrolysate increased with the highest ACE-inhibitory activity (74.99 ± 0.43%) at 1.2 mg/mL of peptic hydrolysate. Tryptic and Alcalase hydrloysates exhibited a strong α-amylase inhibition having 27.96 ± 0.06% and 36.36 ± 0.71% inhibitory capacity respectively with IC₅₀ of 1.02-3.31 mg/mL. Alcalase hydrolysates demonstrated the strongest inhibition (65.81 ± 1.95%), followed by tryptic hydrolysates (54.53 ± 0.52%) in a concentration-dependent inhibition of α-glucosidase (IC₅₀ _, 0.48-0.80 mg/mL). Kinetic analysis showed that ACE-inhibition by different concentrations of Alcalase, pepsin and trypsin hydrolysates is uncompetitive, mixed-type and non-competitive respectively. α-Amylase was non-competitively inhibited while α-glucosidase was un-competitively inhibited by all the hydrolysates. The total amino acid concentration for Alcalase, trypsin and pepsin hydrolysates was 53.51g/100g, 75.40g/100g and 85.42g/100g of Luffa cylindrica seed protein hydrolysate respectively, with glutamate being the most concentrated essential amino acid in all the three hydrolysates. From these results, it can be deduced that Luffa cylindrica seed Alcalase and tryptic protein hydrolysates may play critical and indispensible role as bio-tools in diabetes and hypertension treatment.

Keywords: Biochemistry.