کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
7623052 | 1494544 | 2016 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Extraction, identification, and structure-activity relationship of antioxidative and α-amylase inhibitory peptides from cumin seeds (Cuminum cyminum)
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Cumin seed-derived peptides were extracted, fractionated, and identified in this study. The three novel peptides produced were named as CSP1 (FFRSKLLSDGAAAAKGALLPQYW), CSP2 (RCMAFLLSDGAAAAQQLLPQYW), and CSP3 (DPAQPNYPWTAVLVFRH). These peptides exhibited different bioactivity potencies at 100âµg. CSP1 showed the highest ferric-reducing antioxidant power (FRAP) activity (36.71âmM) and α-amylase inhibition (24.54%) but relatively low radical scavenging activity (3.88%DPPHsc). CSP2 appeared to be an effective di(phenyl)-(2,4,6-trinitrophenyl)iminoazanium (DPPH) radical scavenger (58.64%) with a FRAP value of 29.16âmM but showed poor inhibition against α-amylase (7.22%). CSP3 exhibited the lowest DPPHsc activity of 3.43%, with a FRAP value of 7.6âmM and α-amylase inhibition of 12.52%. The IC50 values of CSP1, CSP2, and CSP3 were 0.04, 0.002, and 0.05âµM, respectively, in the DPPH radical scavenging assays, as well as 0.02, 0.04, and 0.03âµM, respectively, for α-amylase inhibitory activity. A structure-activity relationship study (SAR) was also conducted to evaluate the inhibition mechanism.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Functional Foods - Volume 22, April 2016, Pages 1-12
Journal: Journal of Functional Foods - Volume 22, April 2016, Pages 1-12
نویسندگان
Hwee-Leng Siow, Chee-Yuen Gan,