Stones from olives and Prunus genus fruits are cheap and sustainable sources of proteins and could be potential sources of bioactive peptides The main limitation to the use of these seeds is the presence of amygdalin This work proposes to determine amygdalin in olive and Prunus seeds and in protein isolates obtained from them Moreover antioxidant angiotensin I converting enzyme (ACE Sep 09 2016In the present study we investigated to the antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities of the northern shrimp (Pandalus borealis) by-products (PBB) hydrolysates prepared by enzymatic hydrolysis The antioxidant and ACE inhibitory activities of five enzymatic hydrolysates (alcalase protamex flavourzyme papain and trypsin) of PBB were evaluated

Isolation purification and characterisation of

The angiotensin I‐converting enzyme (ACE )‐inhibitory activities of catfish (C larias batrachus ) muscle protein hydrolysates were investigated Thermolytic digests of C batrachus sarcoplasmic and myofibrillar proteins exhibited inhibitory activity towards ACE and were purified with the aim of ultrafiltration gel filtration and reversed‐phase high‐performance liquid chromatography

Sep 30 2015Abalone protein was hydrolyzed by enzymatic hydrolysis and the optimal enzyme/substrate (E/S) ratios were determined Abalone protein hydrolysates (APH) produced by Protamex at E/S ratio of 1:100 showed angiotensin I converting enzyme inhibitory activity with IC 50 of 0 46 mg/mL and APH obtained by Flavourzyme at E/S ratio of 1:100 possessed the oxygen radical

Human angiotensin I-converting enzyme (ACE EC 3 4 15 1) is a zinc metallopeptidase that plays a critical role in blood pressure regulation [1–7] by catal-ysing the proteolysis of angiotensin I to the vasopres-sor angiotensin II [8–10] There are two isoforms of human ACE: in

Vicilin—A major storage protein of mungbean exhibits antioxidative potential antiproliferative effects and ACE inhibitory activity Antioxidant and angiotensin I-converting enzyme inhibitory activities of northern shrimp (Pandalus borealis) by-products hydrolysate by enzymatic hydrolysis

This study sought to investigate the in vitro antioxidant activity angiotensin-I-converting enzyme (ACE) inhibition and effects of aqueous-methanolic extract of P biglobosa leaf (PBE) on mitochondrial membrane potential and reactive oxygen species (ROS) generation Methods: Antioxidant activity was determined by extract's DPPH

Potential Antioxidant and Angiotensin I

Antioxidant activity angiotensin I-converting enzyme (ACE) inhibitory activity and protein profile of crust (the dried surface of dry-aged beef) were evaluated compared to unaged wet- and dry-aged beef Antioxidant activity was determined using 2 2-diphenyl-1-picrylhydrazyl and 2 2'-azino-di-(3-

Abstract In the present study we investigated to the antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities of the northern shrimp (Pandalus borealis) by-products (PBB) hydrolysates prepared by enzymatic hydrolysis The antioxidant and ACE inhibitory activities of five enzymatic hydrolysates (alcalase protamex flavourzyme papain and trypsin) of PBB were evaluated by

Title: Potential Deployment of Angiotensin I Converting Enzyme Inhibitors and of Angiotensin II Type 1 and Type 2 Receptor Blockers in Cancer Chemotherapy VOLUME: 6 ISSUE: 5 Author(s):Agostino Molteni Sue Heffelfinger John E Moulder Bruce Uhal and William J Castellani Affiliation:University of Missouri-Kansas City School of Medicine Kansas City Missouri USA

BACKGROUND: Enzymatic proteolysis of food proteins is used to produce peptide fractions with the potential to act as physiological modulators Fractionation of these proteins by ultrafiltration results in fractions rich in small peptides with the potential to act as functional food ingredients The present study investigated the angiotensin-I converting enzyme (ACE-I) inhibitory and antioxidant

Natural actomyosin (NAM) from the freshwater fish Catla catla was extracted and hydrolyzed using papain enzyme at different enzyme-to-substrate ratios (0 5% 1 0% 2 0% 5 0% and 10%) to obtain the cryptides with different degrees of hydrolysis (DH) Derived cryptides were evaluated for bioactive properties such as angiotensin-I-converting enzyme (ACE) inhibitory activity and antioxidant

Sep 30 2015Abalone protein was hydrolyzed by enzymatic hydrolysis and the optimal enzyme/substrate (E/S) ratios were determined Abalone protein hydrolysates (APH) produced by Protamex at E/S ratio of 1:100 showed angiotensin I converting enzyme inhibitory activity with IC 50 of 0 46 mg/mL and APH obtained by Flavourzyme at E/S ratio of 1:100 possessed the oxygen radical

However it has not been known how its bioactivity changes after cooking and gastrointestinal digestion Herein Xuanwei ham is analysed before and after cooking as well as gastrointestinal digestion being simulated so as to evaluate and compare its effect on antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities

Antioxidant and Angiotensin I Converting Enzyme (ACE) Inhibitory Properties of GL‐9 Peptide The antioxidant activity of the GL‐9 peptide was investigated based on its scavenging capacity1 1‐diphenyl‐2‐picrylhydrazyl demonstrate its potential application as an ingredient in wholesome foodstuffs Volume 41 Issue 2 April 2017

Angiotensin

Natural actomyosin (NAM) from the freshwater fish Catla catla was extracted and hydrolyzed using papain enzyme at different enzyme-to-substrate ratios (0 5% 1 0% 2 0% 5 0% and 10%) to obtain the cryptides with different degrees of hydrolysis (DH) Derived cryptides were evaluated for bioactive properties such as angiotensin-I-converting enzyme (ACE) inhibitory activity and antioxidant

Jul 18 2018Angiotensin I-converting enzyme (ACE) is an enzyme of effect in blood pressure regulation through two different reactions of the renin–angiotensin–aldosterone system ACE inhibitory activity leads to reducing the conversion of angiotensin I into the powerful vasoconstrictor angiotensin II thus decreasing blood pressure [ 18 ]

Natural actomyosin (NAM) from the freshwater fish Catla catla was extracted and hydrolyzed using papain enzyme at different enzyme-to-substrate ratios (0 5% 1 0% 2 0% 5 0% and 10%) to obtain the cryptides with different degrees of hydrolysis (DH) Derived cryptides were evaluated for bioactive properties such as angiotensin-I-converting enzyme (ACE) inhibitory activity and antioxidant

This study reports for the first time the angiotensin I-converting enzyme (ACE)-inhibition and antioxidant properties of ultrafiltrate fractions (UF) with different molecular weight ranges (lt 1 1–3 and ≥3 kDa) obtained from Fucus spiralis protein hydrolysate (FSPH) digested with cellulase–bromelain

Inhibition of angiotensin I-converting enzyme (ACE) activity is the most common mechanism underlying the lowering of blood pressure In the present study five organic extracts of a marine brown seaweed Ecklonia cava were prepared by using ethanol ethyl acetate chloroform hexane and diethyl ether as solvents which were then tested for their potential ACE inhibitory activities

Vigna Unguiculata as Source of Angiotensin-I Converting Enzyme Inhibitory and Antioxidant Peptides By Maira R Segura-Campos Luis A Chel-Guerrero and David A Betancur-Ancona Submitted: January 20th 2012 Reviewed: September 4th 2012 Published: January 30th 2013 DOI: 10 5772/53045