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Journal of Zhejiang University: Agric. & Life Sci.  2011, Vol. 37 Issue (2): 219-223    DOI: 10.3785/j.issn.1008-9209.2011.02.015
Agricultural sciences     
Modified spectrophotometric method for assay of angiotensin I-converting enzyme inhibitory activity of food-derived peptides
GAO Dan-dan,CAO Yu-sheng,MAI Xi
State Key Laboratory of Food Science and Technology ,Sino-German Joint Research Institute , Nanchang University , Nanchang 330047 ,China
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Abstract  A  modified  spectrophotometric  assay  was  developed  for  determination  of  angiotensin  I-converting enzyme ( ACE) inhibitory activity of peptides derived from plant protein , which was based on the classical paper chromatography determination of hippuric acid ( HA )  content in the urine . By using the modified  method , the maximum  absorbance of  HA  was  measured at 459 nm , and  the optimum chromogenic reaction conditions were as follows : temperature of 40℃ , time for 30 min , and the DAB concentration of 0.5%. Captopril and cottonseed protein peptides showing antihypertensive activity as inhibitors of ACE were detected by this modified spectrophotometric assay . The result showed that the modified method was proved to be convenient , sensitive , accurate and reproducible , and it could be used for the screening of ACE inhibitory peptides derived from food proteins .

Published: 25 March 2011
Cite this article:

GAO Dan-dan,CAO Yu-sheng,MAI Xi. Modified spectrophotometric method for assay of angiotensin I-converting enzyme inhibitory activity of food-derived peptides. Journal of Zhejiang University: Agric. & Life Sci., 2011, 37(2): 219-223.

URL:

http://www.zjujournals.com/agr/10.3785/j.issn.1008-9209.2011.02.015     OR     http://www.zjujournals.com/agr/Y2011/V37/I2/219


改进的分光光度计法测定食源性多肽血管紧张素转化酶的抑制活性

在传统检测食源性多肽血管紧张素转化酶 ( ACE) 抑制肽体外活性方法的基础上 , 结合纸层析测定马尿酸的方法对其进行改进 , 建立了一种新的分光光度法用于测定样品中 ACE 的抑制活性 . 结果表明 : 该方法确定的显色反应吸收波长为459nm ; 最佳显色温度为40 ℃ ; 最佳显色时间为30 min ; 最佳显色剂质量分数为0.5%; 用卡托普利和有 ACE 抑制活性的棉籽蛋白肽作为样品进行检测验证 , 结果表明 , 此方法简便、灵敏、准确、重复性好 , 可用于筛选食源性 ACE 抑制肽 .
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