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¹ Department of Fish Processing Technology, Fisheries College and Research Institute, Tamil Nadu Dr. J. Jayalalithaa Fisheries University, Tuticorin, Tamil Nadu, India
² Department of Fish Quality Assurance and Management, Fisheries College and Research Institute, Tamil Nadu Dr. J. Jayalalithaa Fisheries University, Tuticorin, Tamil Nadu, India
³ Directorate of Research, Tamil Nadu Dr. J. Jayalalithaa Fisheries University, Nagapattinam, Tamil Nadu, India DOI : 10.4194/1303-2712-v19_7_02 Viewed : 4382 - Downloaded : 4969 In this study, skin of unicorn leatherjacket (Aluterus monoceros) was hydrolyzed using collagenase at three different temperatures viz. 5°C, 25°C and 50°C, to obtain collagen hydrolysates. Collagen peptides of low molecular masses (<3kDa) viz. CP-5, CP-25 and CP-50 were obtained by sequential ultrafiltration with tangential flow filtration (TFF) system. The results indicated that CP-5 exhibited the maximum in vitro anti-cancer, anti-diabetic and wound healing activities than CP-25 and CP-50. In MTT assay, CP-5 inhibited the viability of COLO320 cancer cells upto 49.78% at 1 mg/mL concentration, while the inhibition was only 29.92% by CP-50. Anti-diabetic activity as assessed by α-amylase inhibition was 80.45% by CP-5 at 1 mg/mL concentration, as against 75.81% and 71.17% by CP-25 and CP-50, respectively. Collagen peptides, in general, exhibited very low anti-inflammatory property, which ranged between 3.27% to 4.01%. In vitro wound healing tested by scratch assay showed good migration of 3T3-L1 cells in CP-5 treated than CP-25 and CP-50 at 0.2 mg/mL concentration. The study thus proved that collagen peptides derived from fish skin at low hydrolysis temperatures (50C) exhibited more bio-active activities than those hydrolysed at high temperatures (500C); and shall be effectively utilized in various bio-medical applications. Keywords : Fish skin, Collagen peptides, MTT assay, α-amylase inhibition assay