Separation and Characterization of Antioxidative and Angiotensin Converting Enzyme Inhibitory Peptide from Jellyfish Gonad Hydrolysate
The gonad of jellyfish (Rhopilema esculentum Kishinouye), containing high protein content with a rich amino acid composition, is suitable for the preparation of bioactive peptides. Jellyfish gonad was hydrolysed with neutral protease to obtain jellyfish gonad protein hydrolysate (JGPH), which was th...
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| Published in | Molecules (Basel, Switzerland) Vol. 23; no. 1; p. 94 |
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| Main Authors | , , , , , , , , |
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| Abstract | The gonad of jellyfish (Rhopilema esculentum Kishinouye), containing high protein content with a rich amino acid composition, is suitable for the preparation of bioactive peptides. Jellyfish gonad was hydrolysed with neutral protease to obtain jellyfish gonad protein hydrolysate (JGPH), which was then purified sequentially by ultrafiltration, gel filtration chromatography, and RP-HPLC. The peptides were characterized with HPLC-MS/MS. One peptide with amino acid sequence Ser-Tyr (SY) was identified and synthesized, which showed good ACE inhibitory and antioxidant activity. The IC50 of this peptide on DPPH, ·OH, super oxygen anion scavenging activities, and ACE inhibitory activity are 84.623 μM, 1177.632 μM, 456.663 μM, and 1164.179 μM, respectively. The anchor in the binding site of SY and ACE C-domain (ACE-C) was obtained by molecular simulations. The results showed that the dipeptide purified from jellyfish gonad protein hydrolysates can be used as functional food material and is helpful in the study of antioxidant and inhibition of ACE. |
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| AbstractList | The gonad of jellyfish (
Rhopilema
esculentum
Kishinouye
), containing high protein content with a rich amino acid composition, is suitable for the preparation of bioactive peptides. Jellyfish gonad was hydrolysed with neutral protease to obtain jellyfish gonad protein hydrolysate (JGPH), which was then purified sequentially by ultrafiltration, gel filtration chromatography, and RP-HPLC. The peptides were characterized with HPLC-MS/MS. One peptide with amino acid sequence Ser-Tyr (SY) was identified and synthesized, which showed good ACE inhibitory and antioxidant activity. The IC
50
of this peptide on DPPH, ·OH, super oxygen anion scavenging activities, and ACE inhibitory activity are 84.623 μM, 1177.632 μM, 456.663 μM, and 1164.179 μM, respectively. The anchor in the binding site of SY and ACE C-domain (ACE-C) was obtained by molecular simulations. The results showed that the dipeptide purified from jellyfish gonad protein hydrolysates can be used as functional food material and is helpful in the study of antioxidant and inhibition of ACE. The gonad of jellyfish ( ), containing high protein content with a rich amino acid composition, is suitable for the preparation of bioactive peptides. Jellyfish gonad was hydrolysed with neutral protease to obtain jellyfish gonad protein hydrolysate (JGPH), which was then purified sequentially by ultrafiltration, gel filtration chromatography, and RP-HPLC. The peptides were characterized with HPLC-MS/MS. One peptide with amino acid sequence Ser-Tyr (SY) was identified and synthesized, which showed good ACE inhibitory and antioxidant activity. The IC of this peptide on DPPH, ·OH, super oxygen anion scavenging activities, and ACE inhibitory activity are 84.623 μM, 1177.632 μM, 456.663 μM, and 1164.179 μM, respectively. The anchor in the binding site of SY and ACE C-domain (ACE-C) was obtained by molecular simulations. The results showed that the dipeptide purified from jellyfish gonad protein hydrolysates can be used as functional food material and is helpful in the study of antioxidant and inhibition of ACE. The gonad of jellyfish (Rhopilema esculentum Kishinouye), containing high protein content with a rich amino acid composition, is suitable for the preparation of bioactive peptides. Jellyfish gonad was hydrolysed with neutral protease to obtain jellyfish gonad protein hydrolysate (JGPH), which was then purified sequentially by ultrafiltration, gel filtration chromatography, and RP-HPLC. The peptides were characterized with HPLC-MS/MS. One peptide with amino acid sequence Ser-Tyr (SY) was identified and synthesized, which showed good ACE inhibitory and antioxidant activity. The IC50 of this peptide on DPPH, ·OH, super oxygen anion scavenging activities, and ACE inhibitory activity are 84.623 μM, 1177.632 μM, 456.663 μM, and 1164.179 μM, respectively. The anchor in the binding site of SY and ACE C-domain (ACE-C) was obtained by molecular simulations. The results showed that the dipeptide purified from jellyfish gonad protein hydrolysates can be used as functional food material and is helpful in the study of antioxidant and inhibition of ACE. The gonad of jellyfish (Rhopilema esculentum Kishinouye), containing high protein content with a rich amino acid composition, is suitable for the preparation of bioactive peptides. Jellyfish gonad was hydrolysed with neutral protease to obtain jellyfish gonad protein hydrolysate (JGPH), which was then purified sequentially by ultrafiltration, gel filtration chromatography, and RP-HPLC. The peptides were characterized with HPLC-MS/MS. One peptide with amino acid sequence Ser-Tyr (SY) was identified and synthesized, which showed good ACE inhibitory and antioxidant activity. The IC50 of this peptide on DPPH, •OH, super oxygen anion scavenging activities, and ACE inhibitory activity are 84.623 μM, 1177.632 μM, 456.663 μM, and 1164.179 μM, respectively. The anchor in the binding site of SY and ACE C-domain (ACE-C) was obtained by molecular simulations. The results showed that the dipeptide purified from jellyfish gonad protein hydrolysates can be used as functional food material and is helpful in the study of antioxidant and inhibition of ACE. The gonad of jellyfish (RhopilemaesculentumKishinouye), containing high protein content with a rich amino acid composition, is suitable for the preparation of bioactive peptides. Jellyfish gonad was hydrolysed with neutral protease to obtain jellyfish gonad protein hydrolysate (JGPH), which was then purified sequentially by ultrafiltration, gel filtration chromatography, and RP-HPLC. The peptides were characterized with HPLC-MS/MS. One peptide with amino acid sequence Ser-Tyr (SY) was identified and synthesized, which showed good ACE inhibitory and antioxidant activity. The IC50 of this peptide on DPPH, ·OH, super oxygen anion scavenging activities, and ACE inhibitory activity are 84.623 μM, 1177.632 μM, 456.663 μM, and 1164.179 μM, respectively. The anchor in the binding site of SY and ACE C-domain (ACE-C) was obtained by molecular simulations. The results showed that the dipeptide purified from jellyfish gonad protein hydrolysates can be used as functional food material and is helpful in the study of antioxidant and inhibition of ACE.The gonad of jellyfish (RhopilemaesculentumKishinouye), containing high protein content with a rich amino acid composition, is suitable for the preparation of bioactive peptides. Jellyfish gonad was hydrolysed with neutral protease to obtain jellyfish gonad protein hydrolysate (JGPH), which was then purified sequentially by ultrafiltration, gel filtration chromatography, and RP-HPLC. The peptides were characterized with HPLC-MS/MS. One peptide with amino acid sequence Ser-Tyr (SY) was identified and synthesized, which showed good ACE inhibitory and antioxidant activity. The IC50 of this peptide on DPPH, ·OH, super oxygen anion scavenging activities, and ACE inhibitory activity are 84.623 μM, 1177.632 μM, 456.663 μM, and 1164.179 μM, respectively. The anchor in the binding site of SY and ACE C-domain (ACE-C) was obtained by molecular simulations. The results showed that the dipeptide purified from jellyfish gonad protein hydrolysates can be used as functional food material and is helpful in the study of antioxidant and inhibition of ACE. |
| Author | Liu, Jing Jin, Wengang Song, Chengcheng Zhao, Jun Fu, Yinghuan Zhang, Qin Sun, Meiling Shi, Xiaomei Zhu, Beiwei |
| AuthorAffiliation | 1 School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China; zhangqin3595@163.com (Q.Z.); 18242054628@163.com (C.S.); shaerxiao@126.com (X.S.); Kexinxiaojia@163.com (M.S.); g815512123@163.com (J.L.) 2 National Engineering Research Center of Seafood, Dalian 116034, China; kittyufo@163.com 4 Bio-resources Key Laboratory of Shanxi Province, School of Biological Science and Engineering, Shanxi University of Science & Technology, Hanzhong 723001, China; jinwengang@nwafu.edu.cn 3 School of Light Industry and Chemical Engineering, Dalian Polytechnic University, Dalian 116034, China |
| AuthorAffiliation_xml | – name: 4 Bio-resources Key Laboratory of Shanxi Province, School of Biological Science and Engineering, Shanxi University of Science & Technology, Hanzhong 723001, China; jinwengang@nwafu.edu.cn – name: 2 National Engineering Research Center of Seafood, Dalian 116034, China; kittyufo@163.com – name: 1 School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China; zhangqin3595@163.com (Q.Z.); 18242054628@163.com (C.S.); shaerxiao@126.com (X.S.); Kexinxiaojia@163.com (M.S.); g815512123@163.com (J.L.) – name: 3 School of Light Industry and Chemical Engineering, Dalian Polytechnic University, Dalian 116034, China |
| Author_xml | – sequence: 1 givenname: Qin surname: Zhang fullname: Zhang, Qin – sequence: 2 givenname: Chengcheng surname: Song fullname: Song, Chengcheng – sequence: 3 givenname: Jun surname: Zhao fullname: Zhao, Jun – sequence: 4 givenname: Xiaomei surname: Shi fullname: Shi, Xiaomei – sequence: 5 givenname: Meiling surname: Sun fullname: Sun, Meiling – sequence: 6 givenname: Jing surname: Liu fullname: Liu, Jing – sequence: 7 givenname: Yinghuan orcidid: 0000-0001-8056-5674 surname: Fu fullname: Fu, Yinghuan – sequence: 8 givenname: Wengang orcidid: 0000-0002-9838-3905 surname: Jin fullname: Jin, Wengang – sequence: 9 givenname: Beiwei surname: Zhu fullname: Zhu, Beiwei |
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| Snippet | The gonad of jellyfish (Rhopilema esculentum Kishinouye), containing high protein content with a rich amino acid composition, is suitable for the preparation... The gonad of jellyfish ( ), containing high protein content with a rich amino acid composition, is suitable for the preparation of bioactive peptides.... The gonad of jellyfish (RhopilemaesculentumKishinouye), containing high protein content with a rich amino acid composition, is suitable for the preparation of... The gonad of jellyfish ( Rhopilema esculentum Kishinouye ), containing high protein content with a rich amino acid composition, is suitable for the preparation... |
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| SubjectTerms | ACE inhibitory activity Amino Acid Sequence Angiotensin-Converting Enzyme Inhibitors - chemistry Angiotensin-Converting Enzyme Inhibitors - isolation & purification Animals antioxidant activity Binding sites Biphenyl Compounds - chemistry Catalytic Domain Chromatography, Gel Dipeptides - chemistry Dipeptides - isolation & purification Free Radical Scavengers - chemistry Free Radical Scavengers - isolation & purification Gonads - chemistry Hydrolysis jellyfish gonad protein hydrolysate Molecular Docking Simulation Peptides Peptidyl-Dipeptidase A - chemistry Picrates - chemistry Protein Binding Proteins Scyphozoa - chemistry Superoxides - chemistry |
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| Title | Separation and Characterization of Antioxidative and Angiotensin Converting Enzyme Inhibitory Peptide from Jellyfish Gonad Hydrolysate |
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