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     Advance Journal of Food Science and Technology


Production of Angiotensin I Converting Enzyme Inhibitory Peptides from Peanut Meal Fermented with Lactic Acid Bacteria and Facilitated with Protease

Yuan Zeng, Naifu Wang and Wei Qian
School of Tea and Food Science, Anhui Agricultural University, No. 130 West Changjiang Road, Hefei, Anhui, 230036, China
Advance Journal of Food Science and Technology  2013  9:1198-1203
http://dx.doi.org/10.19026/ajfst.5.3082  |  © The Author(s) 2013
Received: May 21, 2013  |  Accepted: June 11, 2013  |  Published: September 05, 2013

Abstract

The aim of this study was to develop a simpler and cheaper technique using a combination of Lactic Acid Bacteria (LAB) fermentation and protease hydrolysis to accelerate the production of bioactive peptides in peanut meal. Firstly, peanut meal was fermented with a total of 14 LAB strains to assay in vitro Angiotensin I Converting Enzyme (ACE) inhibitory activity and Degree of Hydrolysis (DH). Among the strains used, Lactobacillus plantarum Lp6 was selected for further studies because of its highest ACE inhibitory activity (47.83±4.92%) and DH of protein (2.29±0.51%). The addition of protease during the fermentation could highly improve the soluble protein, DH and ACE inhibitory activity of peanut meal. Molecular weight distribution analysis revealed the Extracts from Fermented Peanut Meal (EFPM) was mainly composed of oligopeptides. The ACE inhibitory activity of EFPM remained stable after pepsin and pancreatin treatments simulating an in vitro gastrointestinal digestion. Furthermore, the EFPM exerted potent antihypertensive effect in Spontaneously Hypertensive Rats (SHR) after oral administrations at a dose of 200 or 500 mg/kg body weight. In conclusion, the peanut meal fermented with L. plantarum Lp6 and facilitated with protease could serve as a useful antihypertensive product in the prevention and treatment of hypertension.

Keywords:

ACE inhibitory activity, antihypertensive, fermentation, lactic acid bacteria, peanut meal, protease addition,


References


Competing interests

The authors have no competing interests.

Open Access Policy

This article is 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.

Copyright

The authors have no competing interests.

ISSN (Online):  2042-4876
ISSN (Print):   2042-4868
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