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

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 pr...

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Main Authors: Rotimi Olusanya Arise, Jalil James Idi, Iseoluwa Maureen Mic-Braimoh, Emmanuel Korode, Risikat Nike Ahmed, Omorefosa Osemwegie
Format: Article
Language:English
Published: Elsevier 2019-05-01
Series:Heliyon
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S2405844018381179
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spelling doaj-c6627db4a79644e58959b4ab6f0f87772020-11-25T03:16:26ZengElsevierHeliyon2405-84402019-05-0155e01634In vitro Angiotesin-1-converting enzyme, α-amylase and α-glucosidase inhibitory and antioxidant activities of Luffa cylindrical (L.) M. Roem seed protein hydrolysateRotimi Olusanya Arise0Jalil James Idi1Iseoluwa Maureen Mic-Braimoh2Emmanuel Korode3Risikat Nike Ahmed4Omorefosa Osemwegie5Department of Biochemistry, Faculty of Life Sciences, University of Ilorin, Ilorin, Nigeria; Department of Biological Sciences, College of Science and Engineering, Landmark University, Omu-Aran, Nigeria; Corresponding author.Department of Biochemistry, Faculty of Life Sciences, University of Ilorin, Ilorin, Nigeria; Department of Biochemistry, Faculty of Sciences, Gombe State University, Gombe, NigeriaDepartment of Biochemistry, Faculty of Life Sciences, University of Ilorin, Ilorin, NigeriaDepartment of Biochemistry, Faculty of Life Sciences, University of Ilorin, Ilorin, NigeriaDepartment of Microbiology, Faculty of Life Sciences, University of Ilorin, Ilorin, NigeriaDepartment of Biological Sciences, College of Science and Engineering, Landmark University, Omu-Aran, NigeriaIn 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.http://www.sciencedirect.com/science/article/pii/S2405844018381179Biochemistry
collection DOAJ
language English
format Article
sources DOAJ
author Rotimi Olusanya Arise
Jalil James Idi
Iseoluwa Maureen Mic-Braimoh
Emmanuel Korode
Risikat Nike Ahmed
Omorefosa Osemwegie
spellingShingle Rotimi Olusanya Arise
Jalil James Idi
Iseoluwa Maureen Mic-Braimoh
Emmanuel Korode
Risikat Nike Ahmed
Omorefosa Osemwegie
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
Biochemistry
author_facet Rotimi Olusanya Arise
Jalil James Idi
Iseoluwa Maureen Mic-Braimoh
Emmanuel Korode
Risikat Nike Ahmed
Omorefosa Osemwegie
author_sort Rotimi Olusanya Arise
title In vitro Angiotesin-1-converting enzyme, α-amylase and α-glucosidase inhibitory and antioxidant activities of Luffa cylindrical (L.) M. Roem seed protein hydrolysate
title_short In vitro Angiotesin-1-converting enzyme, α-amylase and α-glucosidase inhibitory and antioxidant activities of Luffa cylindrical (L.) M. Roem seed protein hydrolysate
title_full In vitro Angiotesin-1-converting enzyme, α-amylase and α-glucosidase inhibitory and antioxidant activities of Luffa cylindrical (L.) M. Roem seed protein hydrolysate
title_fullStr In vitro Angiotesin-1-converting enzyme, α-amylase and α-glucosidase inhibitory and antioxidant activities of Luffa cylindrical (L.) M. Roem seed protein hydrolysate
title_full_unstemmed In vitro Angiotesin-1-converting enzyme, α-amylase and α-glucosidase inhibitory and antioxidant activities of Luffa cylindrical (L.) M. Roem seed protein hydrolysate
title_sort in vitro angiotesin-1-converting enzyme, α-amylase and α-glucosidase inhibitory and antioxidant activities of luffa cylindrical (l.) m. roem seed protein hydrolysate
publisher Elsevier
series Heliyon
issn 2405-8440
publishDate 2019-05-01
description 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.
topic Biochemistry
url http://www.sciencedirect.com/science/article/pii/S2405844018381179
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