Angiotensin Converting Enzyme Inhibitory, Antioxidant Activities, and Antihyperlipidaemic Activities of Protein Hydrolysates From Scallop Mantle (<i>Chlamys Farreri</i>)

Zhang, Li; Liu, Yezhou; Lu, Di; Han, Jing; Liu, Xuemin; Tian, Zhenghua; Wang, Zhe

doi:10.1080/10942912.2013.800986

Cited by 9 publications

(5 citation statements)

References 34 publications

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“…Among all of the enzymatic hydrolysates, the peptic hydrolysate exhibited the highest level of activity relative to the other enzymatic hydrolysates, with an IC 50 value of 0.266 mg/mL (Table 3). Compared to previous studies, the ACE inhibitory activity of enzymatic hydrolysates from G. vrijenhoeki was more effective than those of seahorse (0.81 mg/mL) [8], Yellowbelly (3.98 mg/mL) [9], scallop (10.28 mg/mL) [32], and blue mussel (1.13 mg/mL) [19] hydrolysates. Interestingly, oysters (0.40 mg/mL) [33] exhibit a similar ACE inhibitory activity.…”

Section: Amino Acid Profile Of G Vrijenhoekicontrasting

confidence: 78%

Purification and Molecular Docking Study on the Angiotensin I-Converting Enzyme (ACE)-Inhibitory Peptide Isolated from Hydrolysates of the Deep-Sea Mussel Gigantidas vrijenhoeki

Heo,

Kang,

Kim

et al. 2023

Marine Drugs

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The objective of this study was to prepare an angiotensin I-converting enzyme (ACE)-inhibitory peptide from the hydrothermal vent mussel, Gigantidas vrijenhoeki. The G. vrijenhoeki protein was hydrolyzed by various hydrolytic enzymes. The peptic hydrolysate exhibited the highest ACE-inhibitory activity and was fractionated into four molecular weight ranges by ultrafiltration. The <1 kDa fraction exhibited the highest ACE inhibitory activity and was found to have 11 peptide sequences. Among the analyzed peptides, KLLWNGKM exhibited stronger ACE inhibitory activity and an IC50 value of 0.007 μM. To investigate the ACE-inhibitory activity of the analyzed peptides, a molecular docking study was performed. KLLWNGKM exhibited the highest binding energy (−1317.01 kcal/mol), which was mainly attributed to the formation of hydrogen bonds with the ACE active pockets, zinc-binding motif, and zinc ion. These results indicate that G. vrijenhoeki-derived peptides can serve as nutritional and pharmacological candidates for controlling blood pressure.

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Section: Amino Acid Profile Of G Vrijenhoekicontrasting

confidence: 78%

Purification and Molecular Docking Study on the Angiotensin I-Converting Enzyme (ACE)-Inhibitory Peptide Isolated from Hydrolysates of the Deep-Sea Mussel Gigantidas vrijenhoeki

Heo,

Kang,

Kim

et al. 2023

Marine Drugs

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“…Similar to the polyphenolics extracted from many plants, peptides hydrolyzed from animal proteins usually exhibited antioxidant activities. [43][44][45] In this study, the antioxidant peptide was prepared step-bystep using different purification methods, and its antioxidant ability was tested during each step at the same time. It could be seen that antioxidant ability was enhanced by a large margin from 37 to 89.82 U/mL.…”

Section: Resultsmentioning

confidence: 99%

Purification and antioxidant ability of peptide from egg in sea cucumberApostichopus japonicus

Zhang

Liu

Zhang

et al. 2016

International Journal of Food Properties

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The antioxidant peptide was prepared from hydrolyzed egg of Apostichopus japonicus. Ultra-filtration, high-speed counter-current chromatography and gel filtration were used in peptide purification. In each step of purification, meanwhile, peptide was tested with its antioxidant ability. The purity and molecular weight was tested by using Tricine-sodium dodecyl sulphatepolyacrylamide gel electrophoresis. Results showed that the purified peptide obtained a sharply enhancing ability to scavenge hydroxyl radical from 37 to 89.82 U/mL. The purity of peptide was conformed and molecular weight was estimated about 30 KDa. It would be promising for purified peptide to be a good functional food resource.

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“…The ultrafiltrates from these mollusks exhibited ACE inhibitory activity, although, significantly lower than the control (Captopril). In another study, enzymatic digestion with a combination of neutral protease and trypsin of the mantle tissue of Chlamys farreri (Jones and Preston, 1904) yielded a hydrolysate with ACE inhibitory activity [34].…”

Section: Biochemical Studiesmentioning

confidence: 99%

Marine-Derived Peptides with Anti-Hypertensive Properties: Prospects for Pharmaceuticals, Supplements, and Functional Food

Walquist,

Eilertsen,

Elvevoll

et al. 2024

Marine Drugs

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Hypertension, a major health concern linked to heart disease and premature mortality, has prompted a search for alternative treatments due to side effects of existing medications. Sustainable harvesting of low-trophic marine organisms not only enhances food security but also provides a variety of bioactive molecules, including peptides. Despite comprising only a fraction of active natural compounds, peptides are ideal for drug development due to their size, stability, and resistance to degradation. Our review evaluates the anti-hypertensive properties of peptides and proteins derived from selected marine invertebrate phyla, examining the various methodologies used and their application in pharmaceuticals, supplements, and functional food. A considerable body of research exists on the anti-hypertensive effects of certain marine invertebrates, yet many species remain unexamined. The array of assessments methods, particularly for ACE inhibition, complicates the comparison of results. The dominance of in vitro and animal in vivo studies indicates a need for more clinical research in order to transition peptides into pharmaceuticals. Our findings lay the groundwork for further exploration of these promising marine invertebrates, emphasizing the need to balance scientific discovery and marine conservation for sustainable resource use.

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Angiotensin Converting Enzyme Inhibitory, Antioxidant Activities, and Antihyperlipidaemic Activities of Protein Hydrolysates From Scallop Mantle (Chlamys Farreri)

Cited by 9 publications

References 34 publications

Purification and Molecular Docking Study on the Angiotensin I-Converting Enzyme (ACE)-Inhibitory Peptide Isolated from Hydrolysates of the Deep-Sea Mussel Gigantidas vrijenhoeki

Purification and Molecular Docking Study on the Angiotensin I-Converting Enzyme (ACE)-Inhibitory Peptide Isolated from Hydrolysates of the Deep-Sea Mussel Gigantidas vrijenhoeki

Purification and antioxidant ability of peptide from egg in sea cucumberApostichopus japonicus

Marine-Derived Peptides with Anti-Hypertensive Properties: Prospects for Pharmaceuticals, Supplements, and Functional Food

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