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Background: Oratosquilla woodmasoni is one of the marine squilla species, which is found in the entire Asia-Pacific region. This current study assesses the species as the main basis of both ACEi and antioxidant peptide. Objective: To isolate the ACEi peptide derived from O. woodmasoni and examine its ACE inhibition along with antioxidant potential. Materials and Methods: The squilla muscle protein was hydrolysed using alcalase and trypsin enzymes for 12 hours and tested for DH. The hydrolysates were examined for their ACEi activity and then the best hydrolysate was sequentially purified in various chromatographical methods. The purified peptide was studied for anti-oxidant and functional properties, followed by amino acid sequencing. The purified peptide was also evaluated for its toxicity by in vitro cell viability assay. Results: The DH% was found to be 47.13 ± 0.72% and 89.43 ± 2.06% for alcalase and trypsin, respectively. The alcalase 5th-hour hydrolysate was detected with potent activity (65.97 ± 0.56%) using ACEi assay and was primarily fractionated using ultrafiltration; the maximum inhibitory activity was found with 77.04 ± 0.52% in 3-10 kDa fraction. Subsequently, the fraction was purified using IEC and GFC, in which the AC1-A2 fraction had higher antihypertensive activity (70.85 ± 0.78%). The non-toxic fraction showed hexapeptide HVGGCG with molecular weight 529 Da with great potential of antioxidant activity along with functional property. Conclusion: This peptide could be developed as a potential ACE-inhibitory and antioxidant agent.

Background: Green mussel Perna viridis is a bivalve mollusc which is native to the Indian coast and can be found in the Indo-Pacific as well as Asia-Pacific regions. This study evaluates the P. viridis foot (PVF) as a source of an anti-inflammatory peptide. Objective: To characterize and evaluate the possibility of pro-inflammatory cytokines, nitric oxide (NO) as well as cyclooxygenase (COX)-2 reduction in RAW264.7 cells and to analyze functional aspects of the derived peptide from PVF. Materials and Methods: The PVF was hydrolysed with different enzymes and the antiinflammatory activity of hour hydrolysates were evaluated using HRBC Membrane Stabilization (HMS) against hypotonicity induced haemolysis and Albumin Denaturation (AD) inhibition from induced heat assays. Later, the active hour hydrolysate was separated by ultrafiltration and purified using Size-Exclusion Chromatography (SEC). Further, the purified peptide’s sequence was identified using LC-MS/MS and functional properties were determined. Also, the peptide was observed for its anti-inflammatory effects in lipopolysaccharide (LPS)-stimulated RAW264.7 cells for pro-inflammatory cytokines, NO production and COX-2 activation. Results: Among the four enzymes 6th hour alcalase hydrolysate exhibited potent anti-inflammatory activity and was sequentially fractioned with molecular weight cut-offs; further active fraction (30- 10 kDa) was purified. The active peak-II was identified as EGLLGDVF (849.435 Da) and exhibited decent functional aspects. The peptide successfully reduced the production of pro-inflammatory cytokines, NO and COX-2 activation; and down-regulated the iNOS and COX-2 protein expression in LPS-stimulated RAW264.7 cells. Conclusion: Our study indicates that EGLLGDVF derived from PVF has potential antiinflammatory applications applicable in food and pharmaceutical industries.