کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1185156 963385 2010 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Isolation and identification of angiotensin-converting enzyme inhibitory peptides from egg white protein hydrolysates
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
Isolation and identification of angiotensin-converting enzyme inhibitory peptides from egg white protein hydrolysates
چکیده انگلیسی

The aim of this study was to identify potential angiotensin I-converting enzyme (ACE) inhibitory peptide from egg white protein. The protein was hydrolysed by Alcalase and the hydrolysates were isolated with Gel filtration to get the high activity fraction. The fraction was identified by LC tandem mass spectrometric 4000 Q Trap MS. In the current work, 19 peptides were discovered in the fractions, five of which sourced from ovotransferrin and were synthesised by Fmoc solid phase method. ACE-inhibitory activity was measured by HPLC assay. The 50% inhibitory concentrations of Arg–Val–Pro–Ser–Leu (RVPSL) was 20 μM. Based on this remarkable ACE-inhibitory activity, it is suggested that RVPSL may have potential applications as a functional food, which could be used as nutraceutical compounds.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 122, Issue 4, 15 October 2010, Pages 1159–1163
نویسندگان
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