ACE inhibitory peptides and antioxidant peptides derived from in vitro digestion hydrolysate of hen egg white lysozyme.

Abstract:

:Lysozyme from hen egg white is a well-known antimicrobial protein with high ratio of hydrophobic and positively charged amino acid residues. In order to explore functional bioactivities of enzymatic hydrolysates of lysozyme, the protein was subjected to a simulated gastrointestinal digestion and the resulting hydrolysate (LPH2) showed a strong competitive angiotensin I-converting enzyme (ACE) inhibitory activity (IC(50)=12.6μg/ml) and a remarkable antioxidant activity. The LPH2 was fractionated using a 3kDa cut-off membrane and the obtained permeate LPH2-3kDa was analysed by MALDI-TOF-TOF MS. Using this technology, 38 different peptides were identified and some of these peptides were well fit with structure requirements of ACE inhibitory peptides and/or antioxidant peptides. The findings from this study suggest that the protein containing high proportion of hydrophobic and positively charged residues have the potential to generate multifunctional peptides, and these peptides would be beneficial ingredient to be used in functional foods.

journal_name

Food Chem

journal_title

Food chemistry

authors

Rao S,Sun J,Liu Y,Zeng H,Su Y,Yang Y

doi

10.1016/j.foodchem.2012.05.059

subject

Has Abstract

pub_date

2012-12-01 00:00:00

pages

1245-52

issue

3

eissn

0308-8146

issn

1873-7072

pii

S0308-8146(12)00887-4

journal_volume

135

pub_type

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