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...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.展开更多
Two new flavones, namely 5,7,2’,5’-tetrahydroxy-3,4’-dimethoxyflavone and 5’-acetoxy-5,7,2’-trihydroxy-3, 4’-dimethoxyflavone were successfuly isolated from the leaves of Acanthospermum hispidum DC and identifie...Two new flavones, namely 5,7,2’,5’-tetrahydroxy-3,4’-dimethoxyflavone and 5’-acetoxy-5,7,2’-trihydroxy-3, 4’-dimethoxyflavone were successfuly isolated from the leaves of Acanthospermum hispidum DC and identified by UV-Vis, IR, 1H-NMR and EI-MS techniques. Both compounds exhibited antibacterial activity against Salmonella typii, Staphylococcus aureus, Klebsiella pneumoniae, Proteus mirabilis, Bacillus subtilis, Pseudomonas aeruginosa and Shigella dysenteriae with minimum inhibition concentration (MIC) ranging from 0.001 - 0.20 but was inactive against Escherichia coli, Corybacterium pyogenes and Proteus vulgaris.展开更多
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)+6 种基金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)
文摘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.
文摘Two new flavones, namely 5,7,2’,5’-tetrahydroxy-3,4’-dimethoxyflavone and 5’-acetoxy-5,7,2’-trihydroxy-3, 4’-dimethoxyflavone were successfuly isolated from the leaves of Acanthospermum hispidum DC and identified by UV-Vis, IR, 1H-NMR and EI-MS techniques. Both compounds exhibited antibacterial activity against Salmonella typii, Staphylococcus aureus, Klebsiella pneumoniae, Proteus mirabilis, Bacillus subtilis, Pseudomonas aeruginosa and Shigella dysenteriae with minimum inhibition concentration (MIC) ranging from 0.001 - 0.20 but was inactive against Escherichia coli, Corybacterium pyogenes and Proteus vulgaris.
