Angiotensin-converting enzyme inhibitor activity of peptides derived from Kacang goat skin collagen through thermolysin hydrolysis

Vet World Vol.14 January-2021 Article-21

Research Article

Veterinary World, 14(1): 161-167

https://doi.org/10.14202/vetworld.2021.161-167

Arby'in Pratiwi¹, Thoyib R. Hakim¹, Mohammad Z. Abidin¹, Nanung A. Fitriyanto¹, Jamhari Jamhari¹, Rusman Rusman¹, and Yuny Erwanto^1,2

1. Department of Animal Products Technology, Faculty of Animal Sciences, Universitas Gadjah Mada, Jl. Fauna No. 3, Bulaksumur, Yogyakarta 55281, Indonesia.
2. Division of Halal Materials Development, Institute for Halal Industry and System, Universitas Gadjah Mada, Jl. Kaliurang km. 4.5, Bulaksumur, Yogyakarta 55281, Indonesia.

Background and Aim: Angiotensin-converting enzyme (ACE) is one of the inhibitory enzymes isolated from animals for the treatment of hypertension. ACE inhibitor (ACE-I) peptides can be obtained by hydrolyzing proteins from various animal tissues, including muscle and connective tissues. However, the study on ACE-I activity from collagen of Kacang goat skin has not been conducted. This study explores the potency of collagen from Kacang goat skin as a source of an antihypertensive agent through ACE inhibition. Thermolysin will hydrolyze collagen and produce the peptide classified antihypertensive bioactive peptides. This study aimed to determine the potential of thermolysin to hydrolyze collagen of Kacang goat skin for ACE-I peptide production and to identify the production of ACE-I peptides.

Materials and Methods: Collagen from Kacang goat skin was hydrolyzed with thermolysin and incubated at 37°C for 1 h. Molecular weight (MW) evaluation was performed by SDS PAGE; fractionation peptides at <5 kDa, 3-5 kDa, and <3 kDa were performed by ultrafiltration and ACE-I activity determined by IC50 measurement.

Results: Collagen was hydrolyzed by thermolysin, resulting in protein with MW of 117.50-14.60 kDa. The protein content of fractionation at >5 kDa was 3.93±0.72 mg/mL, content of 3-5 kDa was 3.81±0.68 mg/mL, and that of <3 kDa was 2.33±0.38 mg/mL. Fractionation was performed 3 times and one of the results was selected for the ACE-I test. The selected fraction was tested by IC50 measurement with three repetitions and it showed an average enzyme activity at 0.83 μg/mL or 82.94 mg/mL.

Conclusion: Thermolysin hydrolysis of collagen from Kacang goat skin showed the potential to produce bioactive peptides, such as ACE-I. Keywords: angiotensin-I-converting enzyme inhibitor, bioactive peptides, collagen, hydrolysis, thermolysin.

Keywords: angiotensin-I-converting enzyme inhibitor, bioactive peptides, collagen, hydrolysis, thermolysin.

How to cite this article: Pratiwi A, Hakim TR, Abidin MZ, Fitriyanto NA, Jamhari J, Rusman R, Erwanto Y (2021) Angiotensin-converting enzyme inhibitor activity of peptides derived from Kacang goat skin collagen through thermolysin hydrolysis, Veterinary World, 14(1): 161-167.

Received: 11-08-2020 Accepted: 01-12-2020 Published online: 21-01-2021

Corresponding author: Yuny Erwanto E-mail: yunyer@ugm.ac.id

DOI: 10.14202/vetworld.2021.161-167

Copyright: Pratiwi, et al. This article is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http:// creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.