Suaeda physophora Pall.is a kind of desert plant mostly growing in saline habitats in Xinjiang Uygur Autonomous Region.In order to have a better utilization of halophytes,a screening for ACE inhibitors from halophytes...Suaeda physophora Pall.is a kind of desert plant mostly growing in saline habitats in Xinjiang Uygur Autonomous Region.In order to have a better utilization of halophytes,a screening for ACE inhibitors from halophytes growing in Xinjiang was carried out.The result showed that the 70%EtOH extract and n-BuOH extract of S.physophora Pall.possessed significant ACE inhibitory activities.So we focused on its biochemical constituents firstly.One new quinazoline alkaloid,namely Suaedine(1),along with six known compounds(2–7)was isolated from the aerial parts of S.physophora Pall.The structure of the new quinazoline alkaloid was established by one-and two-dimensional nuclear magnetic resonance,optical rotation and mass spectrometry analysis.The flavonoid compounds(2–4)and phenolic compound(5)exhibited significant ACE activities.It was the first time to focus on the chemical constituents and bioactivities of this plant.展开更多
Over 400 yeast strains from seawater and sediments were obtained, but only five strains named HN2 -3, N13d, N13C, Mb5 and HN3 - 2 among them could form clear zones around their colonies on the double plates with 2.0% ...Over 400 yeast strains from seawater and sediments were obtained, but only five strains named HN2 -3, N13d, N13C, Mb5 and HN3 - 2 among them could form clear zones around their colonies on the double plates with 2.0% casein. Peptides in the hydrolysate produced by the proteases from strains HN2 -3 and N13d had higher angiotensin I-converting-enzyme （ACE）-inhibitory activity. The two marine yeast strains were identified to be Aureobasidium pullulans according to the results of routine yeast identification and molecular methods. After purification of the proteases from the two marine yeast strains, it was found that the optimal pH for them was both 9.0, both of them were serine alkaline protease. However, the optimal temperature for the protease from the strain HN2 -3 was 52℃ while that from strain N13d was 48℃. ACE-inhibitory activity of the peptides in the hydrolysate of shrimp protein produced by the purified protease from the strain HN2 -3 was the highest while antioxidant activity in the hydrolysate of spirulina protein produced by the purified protease from the strain N13d was the highest.展开更多
The ACE inhibitory peptides have been characterized from the enzymatic digestion product of bighead carp protein and bioconjugated with graphene oxide(GO)to enhance its activity.The results showed that aspartic acid a...The ACE inhibitory peptides have been characterized from the enzymatic digestion product of bighead carp protein and bioconjugated with graphene oxide(GO)to enhance its activity.The results showed that aspartic acid and glutamic acid had the highest levels in ultrafiltration fractions(<5 kDa),where eight potential ACE inhibitory peptides were also identified(ADSNHKAF,KLWHHTF,LLRLHF,PPSEPTKL,VEKFPLF,YLRLHF,YYKLKPLL,YYKLKPML).Among the eight peptides,YLRLHF showed the best ACE inhibitory activity(IC50=121.90μM)and was a competitive inhibitor.Molecular docking experiments showed that YLRLHF formed four hydrogen bond interactions in the ACE protein pocket,coordination bonding with Zn^(2+),and π-πconjugation interactions to His421.GO elevated the ACE inhibitory activity of YLRLHF(at 0.1 mg/mL)from 43.36%to 51.72%.The structural characterization results obtained from FI-IR,XPS,SEM,and TEM demonstrated the successful combination of GO and YLRLHF.Additionally,biocouples of ACE inhibitory peptides from bighead carp proteins with GO might be potential candidates for future functional foods and antihypertensive drugs.展开更多
基金supported by the National Natural Science Foundation of China(81001371)the Science and Technology Foundation of Dalian city(2011J21DW012).
文摘Suaeda physophora Pall.is a kind of desert plant mostly growing in saline habitats in Xinjiang Uygur Autonomous Region.In order to have a better utilization of halophytes,a screening for ACE inhibitors from halophytes growing in Xinjiang was carried out.The result showed that the 70%EtOH extract and n-BuOH extract of S.physophora Pall.possessed significant ACE inhibitory activities.So we focused on its biochemical constituents firstly.One new quinazoline alkaloid,namely Suaedine(1),along with six known compounds(2–7)was isolated from the aerial parts of S.physophora Pall.The structure of the new quinazoline alkaloid was established by one-and two-dimensional nuclear magnetic resonance,optical rotation and mass spectrometry analysis.The flavonoid compounds(2–4)and phenolic compound(5)exhibited significant ACE activities.It was the first time to focus on the chemical constituents and bioactivities of this plant.
基金The Hi-Tech Research and Development Program ("863") of China,under contract No 2006AA09Z403
文摘Over 400 yeast strains from seawater and sediments were obtained, but only five strains named HN2 -3, N13d, N13C, Mb5 and HN3 - 2 among them could form clear zones around their colonies on the double plates with 2.0% casein. Peptides in the hydrolysate produced by the proteases from strains HN2 -3 and N13d had higher angiotensin I-converting-enzyme （ACE）-inhibitory activity. The two marine yeast strains were identified to be Aureobasidium pullulans according to the results of routine yeast identification and molecular methods. After purification of the proteases from the two marine yeast strains, it was found that the optimal pH for them was both 9.0, both of them were serine alkaline protease. However, the optimal temperature for the protease from the strain HN2 -3 was 52℃ while that from strain N13d was 48℃. ACE-inhibitory activity of the peptides in the hydrolysate of shrimp protein produced by the purified protease from the strain HN2 -3 was the highest while antioxidant activity in the hydrolysate of spirulina protein produced by the purified protease from the strain N13d was the highest.
基金The research was funded by the National Key R&D Program of China(2019YFD0901805).
文摘The ACE inhibitory peptides have been characterized from the enzymatic digestion product of bighead carp protein and bioconjugated with graphene oxide(GO)to enhance its activity.The results showed that aspartic acid and glutamic acid had the highest levels in ultrafiltration fractions(<5 kDa),where eight potential ACE inhibitory peptides were also identified(ADSNHKAF,KLWHHTF,LLRLHF,PPSEPTKL,VEKFPLF,YLRLHF,YYKLKPLL,YYKLKPML).Among the eight peptides,YLRLHF showed the best ACE inhibitory activity(IC50=121.90μM)and was a competitive inhibitor.Molecular docking experiments showed that YLRLHF formed four hydrogen bond interactions in the ACE protein pocket,coordination bonding with Zn^(2+),and π-πconjugation interactions to His421.GO elevated the ACE inhibitory activity of YLRLHF(at 0.1 mg/mL)from 43.36%to 51.72%.The structural characterization results obtained from FI-IR,XPS,SEM,and TEM demonstrated the successful combination of GO and YLRLHF.Additionally,biocouples of ACE inhibitory peptides from bighead carp proteins with GO might be potential candidates for future functional foods and antihypertensive drugs.
