Low Molecular Weight (LMW) of collagen or hydrolyzed collagen is widely used in cosmetic industries due to high efficient penetration into skin and easily distributed in the human body. In this study, collagen from Tilapia (Oreochromis niloticus) fish scales was extracted and hydrolyzed using enzymatic hydrolysis technique. Gel Permeation Chromatography (GPC) analysis revealed that the molecular weight of extracted collagen, 12.5 kDa significantly decreased to 1.3 kDa with narrow distribution when hydrolyzed with 0.5 wt.% of alcalase enzyme. The effect of enzyme treatment on the pH, degree of hydrolysis, functional group, viscosity and amino acid content of collagen were studied using pH measurement, Kjeldahl method, Fourier Transform Infrared (FTIR), viscosity measurement and amino acid profile analysis, respectively. FTIR and amino acid analysis revealed that the functional groups were found unchanged and the profile content of amino acids in hydrolyzed collagen were similar to untreated collagen. The LMW of collagen prepared from Tilapia fish scales will be suitable for cosmetic ingredient.