Characteristics of papain soluble collagen from redbelly yellowtail fusilier (Caesio cuning)

Abstract

Redbelly yellowtail fusilier skin is one of the side products that can be used as raw material for collagen production. Collagen can be extracted by several methods, one of which is through a combination of chemical and enzymatic processes. Useable enzymes was such as papain enzymes. Collagen extracted with this enzyme is known as papain soluble enzyme (PaSC). This study aims to determine the concentration and optimum time of extraction and character of soluble collagen papain (PaSC) from the skin of redbelly yellowtail fusilier. The extraction method of yellow tail skin collagen was divided into three stages: raw material preparation, deproteination using NaOH, and extraction of acid mixture with papain enzyme (PaSC). The results showed that the use of NaOH with a concentration of 0.05 M with an immersion time of 8 hours was able to dissolve the non-collagen protein in an optimal amount. The combination of acetic acid treatment with a concentration of 0.3 M for 3 days and the use of papain enzyme with a concentration of 5,000 U / mg / g of skin was able to produce the highest collagen solubility. The yield of PaSC collagen was 33.28 ± 2.74% (db). The dominant amino acid composition of PaSC collagen was glycine (26.17 ± 0.029%), alanine (13.56 ± 0.025%), and proline (12.34 ± 0.048%). Glycine, proline, and alanine have been the three major amino acids.