DICP OpenIR
Subject Area物理化学
Obtation of hydrolysate from oyster proteins exhibiting angiotensin I-converting enzyme inhibitory activity and antihypertensive effect in spontaneously hypertensive rats
Wang JP(王佳培); Hu JE(胡建恩); Cui JZ(崔金哲); Bai XF(白雪芳); Du YG(杜昱光); Lin BC(林炳承)
Conference NameThe 13th International Biotechnology Symposium
Conference Date2008-10-12
2008-10-12
Conference Place中国
PagesS81/2
Department十八室
Funding Organization中国科学院 中国工程院 中华人民共和国教育部 中华人民共和国科学技术部 中华人民共和国国家发展改革委员会
AbstractHypertension is the most common serious chronic health problem. ACE is a Zn-containing enzyme and plays an important role in regulating blood pressure.ACE catalyzes the conversion froman inactive angiotensin I to a potent vasoconstrictor angiotensin II and also inactivates the antihypertensive vasodilator bradykinin (Ondetti et al., 1997). Since the discovery ofACE inhibitor in snake venom,many studies have been attempted in the synthesis of ACE inhibitors, such as captopril, enalapril, alacepril and lisinopril (Patchett et al.,1979). However, the aforementioned synthetic inhibitors of ACE were believed to have certain many side effects (Atkinson and Robertson, 1979). So, in recent years, some ACE inhibitors derived from food had been studied (Ma et al., 2006). The hydrolysate from oyster proteins by pepsin treatment was separated on Sephadex LH-20 gel filtration chromatography and three fractions (fraction I, fraction II and fraction III) were obtained. The IC50 values of the three fractionswere 1.2, 0.49 and 0.53mg/mL and these yieldswere 4.7%, 55.8% and 13.5% from 6 g of oyster proteins, respectively. The fraction II retained ACE inhibitory activity after treatment in different temperatures and pH conditions. The stability of the fraction II against gastrointestinal proteases was assessed in vitro. The ACE inhibitory activity of the fraction II (0.5 mg/mL) shown hardly any change after treatment by gastrointestinal proteases, which suggested fraction II had stodgy properties. The kinetic experiments demonstrated that the mechanism of ACE inhibitory activity was noncompetitive inhibition. The calculated Ki value for the fraction II was 1.2mmol/L. Furthermore, the fraction II demonstrated antihypertensive activity when they were orally administered to SHR. These results demonstrated that the hydrolysate from oyster proteins by pepsin could serve as a good source of peptides with antihypertensive activity.
Language中文
WOS IDWOS:000208979400188
Citation statistics
Document Type会议论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/113216
Collection中国科学院大连化学物理研究所
Corresponding AuthorDu YG(杜昱光)
Recommended Citation
GB/T 7714
Wang JP,Hu JE,Cui JZ,et al. Obtation of hydrolysate from oyster proteins exhibiting angiotensin I-converting enzyme inhibitory activity and antihypertensive effect in spontaneously hypertensive rats[C],2008:S81/2.
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