Physicochemical Characteristics Of Chicken Feet Collagen Extract In Variations Of Papain Enzyme Concentration And Extraction Duration

Abstract

Collagen is a polypeptide dominated by the amino acids glycine, proline, and hydroxyproline. The polypeptide is in the form of a triple helix structure which is the main characteristic of collagen. Chicken feet which are rich in collagen can be an alternative as a source of collagen that is widely accepted by the community. This study aims to determine the effect of papain enzyme concentration and extraction time on the physicochemical characteristics of the collagen produced and to determine the combination of treatments that produce the highest physicochemical characteristics of collagen. This study is an experimental study designed using a Randomized Block Design (RBD) with a factorial experiment consisting of two factors, namely the concentration of papain enzyme (0%, 2%, 4%, and 6%) and extraction time (6, 12, and 18 hours). Collagen in this study was tested qualitatively (Ninhydrin and FTIR) and quantitatively using a UV-Vis spectrophotometer. FTIR results showed success in extracting collagen while maintaining its structure and components. The physicochemical variables observed included yield, pH, water content, ash content, and protein content. The results showed that the interaction between the two treatments had a very significant effect on the observed variables, except for ash content. The combination of treatments to produce the highest physicochemical characteristics of collagen is a papain enzyme concentration of 4% and an extraction time of 18 hours with a value of 60.19%. The characteristics of the collagen produced are a yield of 0.61%, pH 6.56, water content of 3.82%, ash content of 0.85%, and protein content of 85.29%.