An attractive way of egg white protein by-product use for producing of novel anti-hypertensive peptides

M Pokora; A Zambrowicz; A Dąbrowska; E Eckert; B Setner; M Szołtysik; Z Szewczuk; A Zabłocka; A Polanowski; T Trziszka; J Chrzanowska

doi:10.1016/j.foodchem.2013.11.111

An attractive way of egg white protein by-product use for producing of novel anti-hypertensive peptides

Food Chem. 2014 May 15:151:500-5. doi: 10.1016/j.foodchem.2013.11.111. Epub 2013 Nov 27.

Authors

M Pokora¹, A Zambrowicz², A Dąbrowska¹, E Eckert¹, B Setner³, M Szołtysik¹, Z Szewczuk³, A Zabłocka⁴, A Polanowski¹, T Trziszka¹, J Chrzanowska¹

Affiliations

¹ Department of Animal Products Technology and Quality Management, Wroclaw University of Environmental and Life Sciences, Chełmońskiego 37/41, 51-630 Wroclaw, Poland.
² Department of Animal Products Technology and Quality Management, Wroclaw University of Environmental and Life Sciences, Chełmońskiego 37/41, 51-630 Wroclaw, Poland. Electronic address: aleksandra.zambrowicz@up.wroc.pl.
³ Faculty of Chemistry, University of Wroclaw, Poland.
⁴ Department of Immunochemistry, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Weigla 12, 53-114 Wrocław, Poland.

PMID: 24423562
DOI: 10.1016/j.foodchem.2013.11.111

Abstract

The aim of this study was to (i) examine how enzymatic hydrolysis with a non-commercially available proteinase of fig-leaf gourd fruit (Cucurbita ficifolia) increased the use value of egg white protein preparations, generated as byproducts in the industrial process of lysozyme and cystatin isolation from egg white, and (ii) evaluate the inhibition of angiotensin I-converting enzyme (ACE) by the obtained hydrolysates. Purification procedures including membrane filtration, gel filtration chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC) led to the production of several peptide fractions. Two novel ovalbumin-derived tetrapeptides: SWVE (f 148-151) and DILN (f 86-89) with ACE inhibitory activity were obtained. Study of their inhibitory kinetics revealed a non-competitive binding mode, with an IC50 value against ACE of 33.88 and 73.44 μg for SWVE and DILN, respectively. Synthetic peptides which were designed on the basis of peptide SWVE were examined. A tripeptide sequence of SWV revealed the strongest ACE-inhibitory activity.

Keywords: Angiotensin I-converting enzyme inhibitory activity; Bioactive peptides; Hydrolysis; Protein by-product; Proteinase of Cucurbita ficifolia.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Angiotensin-Converting Enzyme Inhibitors / chemistry
Antihypertensive Agents / therapeutic use*
Egg Proteins / chemistry*
Hydrolysis
Peptides / chemistry*

Substances

Angiotensin-Converting Enzyme Inhibitors
Antihypertensive Agents
Egg Proteins
Peptides