کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
7588101 | 1492081 | 2016 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification and characterisation of a novel angiotensin-I converting enzyme (ACE)-inhibitory peptide derived from the enzymatic hydrolysate of Enteromorpha clathrata protein
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
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چکیده انگلیسی
Hydrolysates containing angiotensin-I converting enzyme (ACE)-inhibitory peptide were prepared from Enteromorpha clathrata protein using alcalase. The hydrolysates were fractionated into two molecular-weight ranges (below and above 10 kDa) by ultrafiltration. The below-10 kDa fraction showed higher ACE-inhibitory activity and was subsequently purified by Sephadex G-15 gel filtration chromatography. The structure of active peptide was identified as Pro-Ala-Phe-Gly by HPLC-Q-TOF-MS and its IC50 value was 35.9 μM. The yield of this peptide from E. clathrata protein was 0.82%. Lineweaver-Burk plots demonstrated that the inhibitory kinetic mechanism of this peptide was non-competitive. Stability study revealed that the purified peptide showed resistance against gastrointestinal proteases. Thus, E. clathrata protein hydrolysate treated with alcalase is a beneficial ingredient of nutraceuticals and pharmaceuticals against hypertension and related diseases.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 211, 15 November 2016, Pages 423-430
Journal: Food Chemistry - Volume 211, 15 November 2016, Pages 423-430
نویسندگان
Saikun Pan, Shujun Wang, Lingling Jing, Dongrui Yao,