An attractive way of egg white protein by-product use for producing of novel anti-hypertensive peptides
| Autor: | Ewelina Eckert, Tadeusz Trziszka, Marek Szołtysik, Bartosz Setner, Marta Pokora, Józefa Chrzanowska, Zbigniew Szewczuk, Aleksandra Zambrowicz, Agnieszka Zabłocka, Anna Dąbrowska, Antoni Polanowski |
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| Rok vydání: | 2014 |
| Předmět: |
chemistry.chemical_classification
Chromatography Chemistry Hydrolysis Egg Proteins Size-exclusion chromatography Angiotensin-Converting Enzyme Inhibitors Peptide General Medicine Tripeptide Hydrolysate Analytical Chemistry chemistry.chemical_compound Biochemistry Enzymatic hydrolysis Cystatin Lysozyme Peptides Antihypertensive Agents Food Science Egg white |
| Zdroj: | Food Chemistry. 151:500-505 |
| ISSN: | 0308-8146 |
| DOI: | 10.1016/j.foodchem.2013.11.111 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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