Development of a Spectrophotometric Method for Monitoring Angiotensin-Converting Enzyme in Dairy Products

The angiotensin-converting enzyme (ACE) regulates the levels of blood pressure through generation of angiotensin-II from angiotensin-I. It is of great importance to have a reliable and yet simple method for a quantitative determination ACE inhibitory peptides in whey of milk products. A rapid, simpl...

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Main Author: Julijana Tomovska*, S. Presilski, N. Gjorgievski, N. Tomovska1, M. S. Qureshi2 and N. P. Bozinovska3
Format: Article
Language:English
Published: University of Agriculture, Faisalabad 2013-01-01
Series:Pakistan Veterinary Journal
Subjects:
Online Access:http://pvj.com.pk/pdf-files/33_1/14-18.pdf
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author Julijana Tomovska*, S. Presilski, N. Gjorgievski, N. Tomovska1, M. S. Qureshi2 and N. P. Bozinovska3
author_facet Julijana Tomovska*, S. Presilski, N. Gjorgievski, N. Tomovska1, M. S. Qureshi2 and N. P. Bozinovska3
author_sort Julijana Tomovska*, S. Presilski, N. Gjorgievski, N. Tomovska1, M. S. Qureshi2 and N. P. Bozinovska3
collection DOAJ
description The angiotensin-converting enzyme (ACE) regulates the levels of blood pressure through generation of angiotensin-II from angiotensin-I. It is of great importance to have a reliable and yet simple method for a quantitative determination ACE inhibitory peptides in whey of milk products. A rapid, simple, sensitive and accurate spectrophotometric kinetic method has been developed for determination of ACE inhibitory peptides, using competitive inhibition. Samples of dairy product from the market were used for the determination of ACE inhibitory peptides in whey. Holmquist’s kinetic method was used for determining ACE inhibitory activity in blood serum and Ronca-Testoni method was used for the determination of ACE inhibitory activity in whey. Enzymatic inhibition activity was determined using 0.8 mmol/L FAPGG (N-[3-(Furyl) –Acryloyl]-L-Phenylalanyl Glycyl Glycyne) as the substrate in 50 mmol/L Tris buffer at pH 8.2 at 37°C and a standard serum containing ACE. First, a solution of whey was mixed in a 1 to 10 ratio with serum (elevation) containing high ACE activity. The enzymatic activity was determined by monitoring the decrease in absorbance at 340 nm as result of hydrolysis of the substrate. The concentration of ACE inhibitory peptides was determined from a standard curve of inhibitor concentration versus percent of ACE inhibition. The study suggests that the method possesses good reproducibility and accuracy. The linear range enabled determination of high enzymatic activity of ACE and all ACE inhibitory peptides from dairy products act as competitive inhibitors.
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spelling doaj.art-17140e69e89a4ac7ba8d3339b2d48c6d2022-12-22T01:50:10ZengUniversity of Agriculture, FaisalabadPakistan Veterinary Journal0253-83182013-01-013311418Development of a Spectrophotometric Method for Monitoring Angiotensin-Converting Enzyme in Dairy ProductsJulijana Tomovska*, S. Presilski, N. Gjorgievski, N. Tomovska1, M. S. Qureshi2 and N. P. Bozinovska3The angiotensin-converting enzyme (ACE) regulates the levels of blood pressure through generation of angiotensin-II from angiotensin-I. It is of great importance to have a reliable and yet simple method for a quantitative determination ACE inhibitory peptides in whey of milk products. A rapid, simple, sensitive and accurate spectrophotometric kinetic method has been developed for determination of ACE inhibitory peptides, using competitive inhibition. Samples of dairy product from the market were used for the determination of ACE inhibitory peptides in whey. Holmquist’s kinetic method was used for determining ACE inhibitory activity in blood serum and Ronca-Testoni method was used for the determination of ACE inhibitory activity in whey. Enzymatic inhibition activity was determined using 0.8 mmol/L FAPGG (N-[3-(Furyl) –Acryloyl]-L-Phenylalanyl Glycyl Glycyne) as the substrate in 50 mmol/L Tris buffer at pH 8.2 at 37°C and a standard serum containing ACE. First, a solution of whey was mixed in a 1 to 10 ratio with serum (elevation) containing high ACE activity. The enzymatic activity was determined by monitoring the decrease in absorbance at 340 nm as result of hydrolysis of the substrate. The concentration of ACE inhibitory peptides was determined from a standard curve of inhibitor concentration versus percent of ACE inhibition. The study suggests that the method possesses good reproducibility and accuracy. The linear range enabled determination of high enzymatic activity of ACE and all ACE inhibitory peptides from dairy products act as competitive inhibitors.http://pvj.com.pk/pdf-files/33_1/14-18.pdfAngiotensin-convertingCompetitive inhibitorsDairy productsEnzymeEnzymatic activitySpectrophotometry
spellingShingle Julijana Tomovska*, S. Presilski, N. Gjorgievski, N. Tomovska1, M. S. Qureshi2 and N. P. Bozinovska3
Development of a Spectrophotometric Method for Monitoring Angiotensin-Converting Enzyme in Dairy Products
Pakistan Veterinary Journal
Angiotensin-converting
Competitive inhibitors
Dairy products
Enzyme
Enzymatic activity
Spectrophotometry
title Development of a Spectrophotometric Method for Monitoring Angiotensin-Converting Enzyme in Dairy Products
title_full Development of a Spectrophotometric Method for Monitoring Angiotensin-Converting Enzyme in Dairy Products
title_fullStr Development of a Spectrophotometric Method for Monitoring Angiotensin-Converting Enzyme in Dairy Products
title_full_unstemmed Development of a Spectrophotometric Method for Monitoring Angiotensin-Converting Enzyme in Dairy Products
title_short Development of a Spectrophotometric Method for Monitoring Angiotensin-Converting Enzyme in Dairy Products
title_sort development of a spectrophotometric method for monitoring angiotensin converting enzyme in dairy products
topic Angiotensin-converting
Competitive inhibitors
Dairy products
Enzyme
Enzymatic activity
Spectrophotometry
url http://pvj.com.pk/pdf-files/33_1/14-18.pdf
work_keys_str_mv AT julijanatomovskaspresilskingjorgievskintomovska1msqureshi2andnpbozinovska3 developmentofaspectrophotometricmethodformonitoringangiotensinconvertingenzymeindairyproducts