The effect of NaOH addition on the characteristics of tilapia skin collagen

Abstract

Research on fish collagen is now growing rapidly as the use of collagen in industry increases. Collagen extraction begins with the removal of non-collagen proteins using bases to maximize the extraction process. This research aims to determine the effect of differences in NaOH concentrations on the characteristics of tilapia skin collagen. NaOH in collagen extraction serves to remove alkaline soluble proteins to optimize the collagen extraction process. The bases used were NaOH with the concentration of 0.5, 1.0, and 1.5%. The extraction was carried out using the acid method. Using SEM, observation parameters for crude collagen from the tilapia skin include collagen yield, functional group analysis, lightness, and surface morphology. The results of functional groups analysis showed that the collagen obtained in all treatments had typical collagen characteristics, i.e., amide A, amide B, amide I, amide II, and amide III. The non-collagen deproteination treatment with 0.5% NaOH could produce better collagen than the 1.0 and 1.5% concentrations, as indicated by the highest yield (20.42%) and lightness (93.22). Morphological analysis showed that the collagen extracted has an irregular branched fiber structure.