EKSTRAKSI DAN KARAKTERISTIK KIMIA KOLAGEN AKTIF DARI BERBAGAI JENIS KULIT TERNAK

Abstract

Collagen is a structural protein widely utilized in the food, pharmaceutical, and
cosmetic industries. This study aimed to evaluate the chemical characteristics of active
collagen extracted from cattle, goat, and broiler chicken skins using bromelain enzyme.
The research process included raw material preparation, pretreatment using NaOH
and acetic acid, collagen extraction at 40°C, and enzymatic hydrolysis using
bromelain. The observed characteristics included yield, moisture content, protein
content, ash content, pH value, and degree of hydrolysis. The results showed that cattle
skin had the best chemical composition as a raw material, with the highest protein
content (35.35%) and the lowest fat content (1.87%). Active collagen produced from
cattle skin also exhibited the best characteristics, with a yield of 21.11%, protein
content of 70.27%, pH value of 6.06, and degree of hydrolysis of 75.65%. In contrast,
active collagen derived from goat and broiler chicken skins showed lower
characteristics. Differences in livestock skin types affected the yield, protein content,
and degree of hydrolysis of the resulting active collagen. Based on these findings, cattle
skin has the greatest potential as a raw material for active collagen production through
bromelain-assisted hydrolysis due to its superior chemical characteristics compared
to goat and broiler chicken skins.