%0 Journal Article
%T Optimization of Hydrolysis Conditions for the Isolation of Angiotensin-I Converting Enzyme(ACE) Inhibitory Peptides from Rhopilema hispidum Optimization of Hydrolysis Conditions for the Isolation of Angiotensin-I Converting Enzyme(ACE) Inhibitory Peptides from Rhopilema hispidum
%A SUN Zhenliang
%A QIN Huanlong
%A CAO Duo
%A YAN Xuebing
%A LI Hao
%A HUANG Linsheng
%A QU Xiao
%A KONG Cheng
%A WANG Man
%J 中国海洋大学学报（英文版）
%D 2018
%X To obtain the maximum angiotensin-I converting enzyme(ACE) inhibitory activity, the protein hydrolysis conditions of the jellyfish Rhopilema hispidum were optimized using response surface methodology(RSM). Trypsin was selected to produce R. hispidum protein hydrolysates(RPH) with ACE inhibitory activity. The optimal parameters for producing protein hydrolysates with the highest ACE inhibitory activity were as follows: hydrolysis time 5 h, hydrolysis temperature 50℃, and the enzyme-to-substrate ratio 6%. Under these conditions, the ACE inhibitory rate of RPH could reach 64.28% ± 5.72%. In addition, RPH contained high levels of Gly, Glu, Pro, Ala, Asp and Arg, with a molecular weight distribution range of 0.32–6.84 kDa. The following three novel ACE inhibitory peptides were isolated and identified: Ile-Gly-Glu-Thr-Gly-Pro, Gly-Ala-Thr-Gly-Pro-Ala-Gly-Tyr-Val and Gly-AlaPhe-Gly-Pro-Gly-Gly-Leu-Val-Gly-Arg-Pro. The IC_(50) values of the ACE inhibitory activity of these three purified peptides were 19.07, 27.42 and 31.26 μmol L~(-1), respectively. These results suggested that proteins and peptides isolated from R. hispidum could be utilized as antihypertensive functional food sources
%U http://qdhb.cbpt.cnki.net/WKD/WebPublication/paperDigest.aspx?paperID=1246cd91-3626-4b27-b5ca-36399fdb9dd7