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¹ University of Muhammadiyah Gresik, Faculty of Agriculture, Department of Aquaculture, 61121 Gresik, Indonesia
² National Pingtung University of Science and Technology, Department of Biological Science and Technology, 91201 Pingtung, Taiwan, ROC
³ UIN Sunan Ampel, Faculty of Science and Technology, Department of Marine Science, 60237 Surabaya, Indonesia DOI : 10.4194/TRJFAS20316 Viewed : 2301 - Downloaded : 2320 Chlorella sorokiniana is an edible microalga known for its high protein content with a balanced amino acid composition, nutritional value, beneficial health effect, and natural antioxidant. The enzymatic assays was used to extract the peptides of C. sorokiniana which was an uncommon method to test the antioxidant activity. In this research, protein of C. sorokiniana was extracted, purified, and hydrolyzed in several enzymes and kept at 37°C for 16h. Hence, enzymatic hydrolysate <3kDA was fractionated into 11 portions (C0%, C10%, to C100%) by using offline Strong Cation Exchange Chromatography (SCX) and their antioxidant activity was tested using DPPH (2.2-diphenyl-1-picrylhydrazyl) radical scavenging assay. The results indicated that C80%, contributed to the highest free DPPH scavenging on C. sorokiniana hydrolysate with the inhibition of 22.04%. Furthermore, to find the candidate peptides, this fraction was injected into LC-MS/MS for characterization of it's DPPH inhibitation. LSSATSAPS (m/z 1638,78) and AGLYGHPQTQEE (m/z 1328.59) are peptides that were identified and confirmed by LC-MS/MS. The molecular docking study was conducted to provide the binding simulation between these peptides and the ROS1 as the receptor. In conclusion, our results suggested that the aforementioned peptides were attached to ROS1 binding site and contributed to its potential antioxidant activity. Keywords : Bioactive peptides, Chlorella sorokiniana, DPPH assay, Molecular docking, SCX Chromatography