Optimization of Hydrolysis Conditions for the Isolation of Angiotensin-I Converting Enzyme(ACE) Inhibitory Peptides from Rhopilema hispidum

查看全文 作　　者：SUN [1,2]Zhenliang;QIN [1]Huanlong;CAO [3]Duo;YAN [1]Xuebing;LI [1]Hao;HUANG [1]Linsheng;QU [1]Xiao;KONG [1]Cheng;WANG [2]Man

机构地区：[1]Department of General Surgery, Shanghai Tenth People's Hospital, Tongji University School of Medicine;[2]Shanghai Jiaotong University Affiliated Sixth People's Hospital,South Campus;[3]The College of Life Science, Northwest University

出　　处：《Journal of Ocean University of China》索引2018年第17卷第6期,共7页

基　　金：supported by the National Natural Science Foundation of China (Nos. 81230057, 81372615, 81472262, 41306133 and 81200264);the Emerging Cutting-Edge Technology Joint Research projects of Shanghai (No. SHDC12012106);the Tongji University Subject Pilot Program (No. 162385);partly funded by the Shanghai Municipal Health and Family Planning Commission Project (Nos. 201540027 and 20174Y0236);the seed fund program of Shanghai University of Medicine & Health Sciences (No. HSMF-17-22-031);Excellent Young Medical Expert of Shanghai (No. 2017YQ048);Shangha Natural Science Foundation (No. 18ZR1431700);China Postdoctoral Science Foundation (No. 2017M610278);the Key Research and Developing Plan of Shandong Province (No. 2015GSF115015) 摘　　要：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. 关键词：Rhopilema hispidum ACE INHIBITORY PEPTIDE response surface methodology protein HYDROLYSATE

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Optimization of Hydrolysis Conditions for the Isolation of Angiotensin-I Converting Enzyme(ACE) Inhibitory Peptides from Rhopilema hispidum

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