Transepithelial transport of milk-derived angiotensin I-converting enzyme inhibitory peptide with the RLSFNP sequence

2017 ◽  
Vol 98 (3) ◽  
pp. 976-983 ◽  
Author(s):  
Yuxing Guo ◽  
Junai Gan ◽  
Qian Zhu ◽  
Xiaoqun Zeng ◽  
Yangying Sun ◽  
...  
Keyword(s):  
Transepithelial Transport ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme

Transepithelial Transport and Stability in Blood Serum of Angiotensin-I-Converting Enzyme Inhibitory Dipeptides

2008 ◽  
Vol 63 (5-6) ◽  
pp. 451-459 ◽  
Author(s):  
Anne-Kathrin Pentzien ◽  
Hans Meisel
Keyword(s):  
Blood Serum ◽  
Milk Proteins ◽  
Transepithelial Transport ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme ◽  
Brush Border Enzyme ◽  
Dipeptidyl Aminopeptidase ◽  
Human Intestinal Epithelium

The dipeptides Ala-Trp, Val-Phe, and Val-Tyr inhibit the angiotensin-I-converting enzyme. They are encrypted within the primary sequences of different food proteins, e. g. milk proteins. The angiotensin-I-converting enzyme inhibitory potency of these synthetic dipeptides was quantified using a spectrophotometric assay. The dipeptides showed no adverse effects on differentiated Caco-2 cells (model for human intestinal epithelium), as confirmed by transepithelial electrical resistance, microscopy and the activity of the brush-border enzyme dipeptidyl aminopeptidase IV. Furthermore, the transport of these bioactive dipeptides through intact Caco-2 monolayers and their stability to incubation in human blood serum has been demonstrated for the first time. Low molecular mass peptides represent the minimal structures required for angiotensin-I-converting enzyme inhibition which have a high potential bioavailability. Therefore, they may act as target peptides in enriched hydrolysates for the preparation of an angiotensin-I-converting enzyme inhibitory peptide and for the use in special formulations as functional foods/foods of specified health use.

scholarly journals Separation and Purification of Angiotensin I Converting Enzyme Inhibitory Peptide in Peptic Hydrolyzate of Oyster.

1994 ◽  
Vol 41 (9) ◽  
pp. 589-594 ◽  
Author(s):  
Kiyoshi MATSUMOTO ◽  
Atsuko OGIKUBO ◽  
Takatada YOSHINO ◽  
Toshiro MATSUI ◽  
Yutaka OSAJIMA
Keyword(s):  
Converting Enzyme ◽  
Separation And Purification ◽  
Angiotensin I ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme

Evaluation and Identification of Potent Angiotensin-I Converting Enzyme Inhibitory Peptide Derived from Dwarf Gulper Shark (C entrophorus atromarginatus )

2014 ◽  
Vol 39 (2) ◽  
pp. 107-115 ◽  
Author(s):  
Asami Ikeda ◽  
Hayato Ichino ◽  
Saori Kiguchiya ◽  
Petros Chigwechokha ◽  
Masaharu Komatsu ◽  
...  
Keyword(s):  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme

Inhibitory mechanism of a substrate-type angiotensin I-converting enzyme inhibitory peptide

2019 ◽  
Vol 79 ◽  
pp. 97-104 ◽  
Author(s):  
Junjie Wu ◽  
Dewei Xie ◽  
Xujun Chen ◽  
Ya-Jie Tang ◽  
Lixin Wang ◽  
...  
Keyword(s):  
Converting Enzyme ◽  
Inhibitory Mechanism ◽  
Substrate Type ◽  
Angiotensin I ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme
Sign in / Sign up

Export Citation Format

Share Document