The HMG-CoA Reductase Inhibitor Activities of Soy Protein Hydrolysates from Papain Hydrolysis

The search for an HMG-CoA reductase inhibitor agent as a safe and inexpensive alternative treatment for hypercholesterolemia has been carried out using soy protein hydrolysates as one of the bioactive peptide sources. This study was conducted to explore the potency of soy protein hydrolysates as an...

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Main Authors: Sandra Hermanto, Aldi Octavio, Azrifitria Azrifitria, Susi Kusumaningrum
Format: Article
Language:English
Published: Jenderal Soedirman University 2021-07-01
Series:Molekul
Online Access:https://ojs.jmolekul.com/ojs/index.php/jm/article/view/724
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spelling doaj-058101d9f18a40f984a8a1b2818765552021-07-27T03:27:29ZengJenderal Soedirman UniversityMolekul1907-97612503-03102021-07-0116214515510.20884/1.jm.2021.16.2.724336The HMG-CoA Reductase Inhibitor Activities of Soy Protein Hydrolysates from Papain HydrolysisSandra Hermanto0Aldi Octavio1Azrifitria Azrifitria2Susi Kusumaningrum3Syarif Hidaytullah Jakarta State Islamic UniversitySyarif Hidaytullah Jakarta State Islamic UniversityPharmacy Study Program, Faculty of Health Sciences UIN Syarif Hidayatulah JakartaCenter for Pharmaceutical and Medical Technology BPPT Serpong, Tangerang SelatanThe search for an HMG-CoA reductase inhibitor agent as a safe and inexpensive alternative treatment for hypercholesterolemia has been carried out using soy protein hydrolysates as one of the bioactive peptide sources. This study was conducted to explore the potency of soy protein hydrolysates as an anti hypercholesterolemia agent by an in vitro assay, through the inhibition capacity of the HMG-CoA (3-hydroxy-3-methyl glutaryl-coenzyme A) reductase enzyme as a key component of cholesterol biosynthesis. Sample preparation started with soy protein isolation through acid precipitation and separated by centrifugation. The samples were analyzed the proximate content and hydrolyzed by papain enzyme at concentration 0.2% (w/v), for 0-6 hours and at 37, 50, and 55 oC. The protein hydrolysates were subsequently evaluated for hydrolysis degree (% DH), hydrolysates profile with SDS-PAGE (Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis), and anti-cholesterol assay through HMG-CoA reductase inhibition tests. The sample with the highest inhibition activity was fractionated using gel filtration chromatography (Sephadex G-10) and the molecular weight of fractions was characterized by LCMS QTOF (Liquid Chromatography-Mass Spectrometry Quadrupole Time-of-Flight) for molecular weight determination. The results indicated the optimum hydrolysis conditions of soy protein isolates were obtained at 3 hours incubation, at 50 °C with DH 33.39% and the inhibition value was 95.65% (protein concentration 39.21 μg / mL). LCMS data showed the molecular weight of fractionated peptides were 1514 and 2029 Da. We assumed that both peptides have the same affinity as previous peptides in inhibiting HMG-CoA reductase.https://ojs.jmolekul.com/ojs/index.php/jm/article/view/724
collection DOAJ
language English
format Article
sources DOAJ
author Sandra Hermanto
Aldi Octavio
Azrifitria Azrifitria
Susi Kusumaningrum
spellingShingle Sandra Hermanto
Aldi Octavio
Azrifitria Azrifitria
Susi Kusumaningrum
The HMG-CoA Reductase Inhibitor Activities of Soy Protein Hydrolysates from Papain Hydrolysis
Molekul
author_facet Sandra Hermanto
Aldi Octavio
Azrifitria Azrifitria
Susi Kusumaningrum
author_sort Sandra Hermanto
title The HMG-CoA Reductase Inhibitor Activities of Soy Protein Hydrolysates from Papain Hydrolysis
title_short The HMG-CoA Reductase Inhibitor Activities of Soy Protein Hydrolysates from Papain Hydrolysis
title_full The HMG-CoA Reductase Inhibitor Activities of Soy Protein Hydrolysates from Papain Hydrolysis
title_fullStr The HMG-CoA Reductase Inhibitor Activities of Soy Protein Hydrolysates from Papain Hydrolysis
title_full_unstemmed The HMG-CoA Reductase Inhibitor Activities of Soy Protein Hydrolysates from Papain Hydrolysis
title_sort hmg-coa reductase inhibitor activities of soy protein hydrolysates from papain hydrolysis
publisher Jenderal Soedirman University
series Molekul
issn 1907-9761
2503-0310
publishDate 2021-07-01
description The search for an HMG-CoA reductase inhibitor agent as a safe and inexpensive alternative treatment for hypercholesterolemia has been carried out using soy protein hydrolysates as one of the bioactive peptide sources. This study was conducted to explore the potency of soy protein hydrolysates as an anti hypercholesterolemia agent by an in vitro assay, through the inhibition capacity of the HMG-CoA (3-hydroxy-3-methyl glutaryl-coenzyme A) reductase enzyme as a key component of cholesterol biosynthesis. Sample preparation started with soy protein isolation through acid precipitation and separated by centrifugation. The samples were analyzed the proximate content and hydrolyzed by papain enzyme at concentration 0.2% (w/v), for 0-6 hours and at 37, 50, and 55 oC. The protein hydrolysates were subsequently evaluated for hydrolysis degree (% DH), hydrolysates profile with SDS-PAGE (Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis), and anti-cholesterol assay through HMG-CoA reductase inhibition tests. The sample with the highest inhibition activity was fractionated using gel filtration chromatography (Sephadex G-10) and the molecular weight of fractions was characterized by LCMS QTOF (Liquid Chromatography-Mass Spectrometry Quadrupole Time-of-Flight) for molecular weight determination. The results indicated the optimum hydrolysis conditions of soy protein isolates were obtained at 3 hours incubation, at 50 °C with DH 33.39% and the inhibition value was 95.65% (protein concentration 39.21 μg / mL). LCMS data showed the molecular weight of fractionated peptides were 1514 and 2029 Da. We assumed that both peptides have the same affinity as previous peptides in inhibiting HMG-CoA reductase.
url https://ojs.jmolekul.com/ojs/index.php/jm/article/view/724
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