کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
7622914 | 1494540 | 2016 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Isolation and characterization of angiotensin I-converting enzyme (ACE) inhibitory peptides from Ulva rigida C. Agardh protein hydrolysate
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
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چکیده انگلیسی
Ulva rigida protein was hydrolysed with pepsin plus bromelain after a screening of nine enzymes for optimal proteolysis. This hydrolysate, presenting ACE-inhibitory activity with an IC50 value of 0.483âmg/mL, was fractionated by ultrafiltration membranes into three molecular weight ranges (<1âkDa, 1-3âkDa and >3âkDa). The <1âkDa fraction that exhibited the highest activity (IC50: 0.095âmg/mL) was purified using size-exclusion chromatography and reversed-phase high-performance liquid chromatography, yielding two active ACE-inhibitory purified peptides. Edman degradation revealed its amino acid sequences to be IP and AFL with IC50 values of 0.020 and 0.023âmg/mL, respectively. Both peptides were synthesized to confirm the structure and to validate their ACE-inhibitory activities. Lineweaver-Burk plots suggest that IP acts as a non-competitive and AFL as a competitive ACE-inhibitors. Stability assays showed that both peptides are heat-stable and AFL is hydrolysed by intestinal mucosa peptidases to FL with IC50 value of 0.004âmg/mL that acts as a non-competitive ACE-inhibitor. The results suggest that these peptides might have a potential use in the preparation of antihypertensive drugs or functional foods.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Functional Foods - Volume 26, October 2016, Pages 65-76
Journal: Journal of Functional Foods - Volume 26, October 2016, Pages 65-76
نویسندگان
Lisete Paiva, Elisabete Lima, Ana Isabel Neto, José Baptista,