Identification and Characterization of Gastrointestinal-Resistant Angiotensin-Converting Enzyme Inhibitory Peptides from Egg White Proteins

Hongbing Fan; Jiapei Wang; Wang Liao; Xu Jiang; Jianping Wu

doi:10.1021/acs.jafc.9b01071

Identification and Characterization of Gastrointestinal-Resistant Angiotensin-Converting Enzyme Inhibitory Peptides from Egg White Proteins

Hongbing Fan
, Jiapei Wang
, Wang Liao
, Xu Jiang
, Jianping Wu

Research output: Contribution to journal › Article › peer-review

66 Scopus citations

Abstract

Egg proteins are recognized as excellent sources of bioactive peptides, such as angiotensin-converting enzyme inhibitory (ACEi) peptides. Oral administration of a thermolysin-digested egg white hydrolysate (T-EWH) caused a significant blood pressure reduction in spontaneously hypertensive rats; a further ACEi assay implied that its ACEi activity was enhanced after in vitro gastrointestinal (GI) digestion. These results indicated that T-EWH contained ACEi peptides resisting GI digestion?and/or being further released during GI digestion. Therefore, the objective of this study was to identify these responsible?ACEi peptides from T-EWH. The conventionally activity-guided fractionation was applied, coupled with a synchronized GI digestion throughout, during which both peptide yield and ACEi activity before and after the GI digestion were measured. Finally, six ACEi peptides (LAPYK, LKISQ, LKYAT, INKVVR, LFLIKH, and LGHWVY) with good GI resistance were identified with IC₅₀ values <20 μM, especially LKYAT (0.09 μM). The structure?activity relationship of these peptides was discussed. The discovery of GI-resistant ACEi peptides could further support the application of egg white proteins as functional food ingredients.

Original language	English
Pages (from-to)	7147-7156
Number of pages	10
Journal	Journal of Agricultural and Food Chemistry
Volume	67
Issue number	25
DOIs	https://doi.org/10.1021/acs.jafc.9b01071
State	Published - Jun 26 2019

Bibliographical note

Publisher Copyright:
Copyright © 2019 American Chemical Society.

Funding

*Tel.: +1 780 492 6885. Fax: +1 780 492 4265. E-mail: jwu3@ ualberta.ca. ORCID Hongbing Fan: 0000-0003-1049-6815 Wang Liao: 0000-0001-8319-2199 Jianping Wu: 0000-0003-2574-5191 Funding This work was supported by funding from Natural Sciences and Engineering Research Council of Canada, Egg Farmers of Canada, and Burnbrae Farms Ltd. H.F. is the recipient of Doctoral Scholarships from China Scholarship Council, Alberta Innovates Technology Futures, and the Killam Trusts. Notes The authors declare no competing financial interest. This work was supported by funding from Natural Sciences and Engineering Research Council of Canada, Egg Farmers of Canada, and Burnbrae Farms Ltd. H.F. is the recipient of Doctoral Scholarships from China Scholarship Council, Alberta Innovates Technology Futures, and the Killam Trusts.

Funders
Burnbrae Farms Ltd.
Egg Farmers of Canada
Natural Sciences and Engineering Research Council of Canada
Alberta Innovates - Technology Futures
Killam Trusts
China Scholarship Council

Keywords

ACE inhibitory peptides
egg white
gastrointestinal digestion
purification and identification
structure-activity relationship

ASJC Scopus subject areas

General Chemistry
General Agricultural and Biological Sciences

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10.1021/acs.jafc.9b01071

Cite this

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title = "Identification and Characterization of Gastrointestinal-Resistant Angiotensin-Converting Enzyme Inhibitory Peptides from Egg White Proteins",

abstract = "Egg proteins are recognized as excellent sources of bioactive peptides, such as angiotensin-converting enzyme inhibitory (ACEi) peptides. Oral administration of a thermolysin-digested egg white hydrolysate (T-EWH) caused a significant blood pressure reduction in spontaneously hypertensive rats; a further ACEi assay implied that its ACEi activity was enhanced after in vitro gastrointestinal (GI) digestion. These results indicated that T-EWH contained ACEi peptides resisting GI digestion?and/or being further released during GI digestion. Therefore, the objective of this study was to identify these responsible?ACEi peptides from T-EWH. The conventionally activity-guided fractionation was applied, coupled with a synchronized GI digestion throughout, during which both peptide yield and ACEi activity before and after the GI digestion were measured. Finally, six ACEi peptides (LAPYK, LKISQ, LKYAT, INKVVR, LFLIKH, and LGHWVY) with good GI resistance were identified with IC50 values <20 μM, especially LKYAT (0.09 μM). The structure?activity relationship of these peptides was discussed. The discovery of GI-resistant ACEi peptides could further support the application of egg white proteins as functional food ingredients.",

keywords = "ACE inhibitory peptides, egg white, gastrointestinal digestion, purification and identification, structure-activity relationship",

author = "Hongbing Fan and Jiapei Wang and Wang Liao and Xu Jiang and Jianping Wu",

note = "Publisher Copyright: Copyright {\textcopyright} 2019 American Chemical Society.",

year = "2019",

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doi = "10.1021/acs.jafc.9b01071",

language = "English",

volume = "67",

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AU - Wu, Jianping

PY - 2019/6/26

Y1 - 2019/6/26

N2 - Egg proteins are recognized as excellent sources of bioactive peptides, such as angiotensin-converting enzyme inhibitory (ACEi) peptides. Oral administration of a thermolysin-digested egg white hydrolysate (T-EWH) caused a significant blood pressure reduction in spontaneously hypertensive rats; a further ACEi assay implied that its ACEi activity was enhanced after in vitro gastrointestinal (GI) digestion. These results indicated that T-EWH contained ACEi peptides resisting GI digestion?and/or being further released during GI digestion. Therefore, the objective of this study was to identify these responsible?ACEi peptides from T-EWH. The conventionally activity-guided fractionation was applied, coupled with a synchronized GI digestion throughout, during which both peptide yield and ACEi activity before and after the GI digestion were measured. Finally, six ACEi peptides (LAPYK, LKISQ, LKYAT, INKVVR, LFLIKH, and LGHWVY) with good GI resistance were identified with IC50 values <20 μM, especially LKYAT (0.09 μM). The structure?activity relationship of these peptides was discussed. The discovery of GI-resistant ACEi peptides could further support the application of egg white proteins as functional food ingredients.

AB - Egg proteins are recognized as excellent sources of bioactive peptides, such as angiotensin-converting enzyme inhibitory (ACEi) peptides. Oral administration of a thermolysin-digested egg white hydrolysate (T-EWH) caused a significant blood pressure reduction in spontaneously hypertensive rats; a further ACEi assay implied that its ACEi activity was enhanced after in vitro gastrointestinal (GI) digestion. These results indicated that T-EWH contained ACEi peptides resisting GI digestion?and/or being further released during GI digestion. Therefore, the objective of this study was to identify these responsible?ACEi peptides from T-EWH. The conventionally activity-guided fractionation was applied, coupled with a synchronized GI digestion throughout, during which both peptide yield and ACEi activity before and after the GI digestion were measured. Finally, six ACEi peptides (LAPYK, LKISQ, LKYAT, INKVVR, LFLIKH, and LGHWVY) with good GI resistance were identified with IC50 values <20 μM, especially LKYAT (0.09 μM). The structure?activity relationship of these peptides was discussed. The discovery of GI-resistant ACEi peptides could further support the application of egg white proteins as functional food ingredients.

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Identification and Characterization of Gastrointestinal-Resistant Angiotensin-Converting Enzyme Inhibitory Peptides from Egg White Proteins

Abstract

Bibliographical note

Funding

Keywords

ASJC Scopus subject areas

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