Purification and characterisation of antioxidant and nitric oxide inhibitory peptides from Tilapia (Oreochromis niloticus) protein hydrolysate

2014 ◽  
Vol 50 (3) ◽  
pp. 660-665 ◽  
Author(s):  
Sureeporn Kangsanant ◽  
Chakree Thongraung ◽  
Chaweewan Jansakul ◽  
Michael Murkovic ◽  
Vatcharee Seechamnanturakit
Keyword(s):  
Nitric Oxide ◽  
Oreochromis Niloticus ◽  
Protein Hydrolysate ◽  
Inhibitory Peptides

Nitric oxide euthanasia: a potential procedure for improving animal welfare and fillet color of tilapia (Oreochromis niloticus)

2017 ◽  
Vol 25 (5) ◽  
pp. 1845-1856 ◽  
Author(s):  
Zi-Chao Wang ◽  
Mou-Ming Zhao ◽  
Zhongxiang Fang ◽  
De-Wei Chen
Keyword(s):  
Nitric Oxide ◽  
Animal Welfare ◽  
Oreochromis Niloticus

scholarly journals Immunomodulatory Activity of Low Molecular-Weight Peptides from Nibea japonica in RAW264.7 Cells via NF-κB Pathway

Marine Drugs ◽  
2019 ◽  
Vol 17 (7) ◽  
pp. 404 ◽  
Author(s):  
Zhuangwei Zhang ◽  
Xuyang Hu ◽  
Lin Lin ◽  
Guofang Ding ◽  
Fangmiao Yu
Keyword(s):  
Nitric Oxide ◽  
Molecular Weight ◽  
Cell Cycle Progression ◽  
Protein Hydrolysate ◽  
Raw264.7 Cells ◽  
Immunomodulatory Activity ◽  
Low Molecular Weight ◽  
Phagocytic Capacity ◽  
Activated State ◽  
Factor Α

In this study, a low molecular-weight (Mw) peptide named NJP (<1 kDa), was purified from a protein hydrolysate of Nibea japonica by ultrafiltration, and its immunomodulatory effect on RAW264.7 cells was evaluated. The lactate dehydrogenase (LDH) and MTT assays were performed to explore the cytotoxicity of NJP. The results showed that NJP promoted cell proliferation and had no significant toxic effects on RAW264.7 cells. Moreover, the cells formed multiple pseudopodia indicating that they were in activated state. Further tests showed that NJP significantly promoted phagocytic capacity, and the secretion of proinflammatory cytokines tumor necrosis factor-α (TNF-α), interleukin-6 (IL-6), and interleukin-1β (IL-1β). It also increased the synthesis of nitric oxide (NO) by upregulating inducible nitric oxide synthase (iNOS) protein level. Flow cytometry revealed that NJP promoted cell cycle progression and increased the percentage of cells in G0/G1 phase. NJP promoted IκBα degradation, p65 and nuclear factor (NF)-κB activation and translocation by up-regulating IKKα/β protein expression. In conclusion, these results indicated that NJP exerts immunomodulatory effects on RAW264.7 cells through the NF-κB signaling pathway. Therefore, NJP can be incorporated in the production of functional foods or nutraceuticals.

scholarly journals Affinity Purification of Angiotensin Converting Enzyme Inhibitory Peptides from Wakame (Undaria pinnatifida) Using Immobilized ACE on Magnetic Metal Organic Frameworks

Marine Drugs ◽  
2021 ◽  
Vol 19 (3) ◽  
pp. 177
Author(s):  
Xuezhen Feng ◽  
Dankui Liao ◽  
Lixia Sun ◽  
Shanguang Wu ◽  
Ping Lan ◽  
...  
Keyword(s):  
Competitive Inhibition ◽  
Undaria Pinnatifida ◽  
Marine Organism ◽  
Protein Hydrolysate ◽  
Affinity Purification ◽  
Converting Enzyme ◽  
Food Ingredients ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

Angiotensin-I-converting enzyme (ACE) inhibitory peptides derived from marine organism have shown a blood pressure lowering effect with no side effects. A new affinity medium of Fe3O4@ZIF-90 immobilized ACE (Fe3O4@ZIF-90-ACE) was prepared and used in the purification of ACE inhibitory peptides from Wakame (Undaria pinnatifida) protein hydrolysate (<5 kDa). The Fe3O4@ZIF-90 nanoparticles were prepared by a one-pot synthesis and crude ACE extract from pig lung was immobilized onto it, which exhibited excellent stability and reusability. A novel ACE inhibitory peptide, KNFL (inhibitory concentration 50, IC50 = 225.87 μM) was identified by affinity purification using Fe3O4@ZIF-90-ACE combined with reverse phase-high performance liquid chromatography (RP-HPLC) and MALDI-TOF mass spectrometry. Lineweaver–Burk analysis confirmed the non-competitive inhibition pattern of KNFL, and molecular docking showed that it bound at a non-active site of ACE via hydrogen bonds. This demonstrates that affinity purification using Fe3O4@ZIF-90-ACE is a highly efficient method for separating ACE inhibitory peptides from complex protein mixtures and the purified peptide KNFL could be developed as a functional food ingredients against hypertension.

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