Characterization of Acid Soluble Collagen from Redbelly Yellowtail Fusilier Fish Skin (Caesio cuning)

  • Ika Astiana Departemen Teknologi Hasil Perairan, Fakultas Perikanan dan Ilmu Kelautan, Institut Pertanian Bogor, kampus IPB Darmaga, Jalan Agatis, Bogor, Jawa Barat 16680 Telepon (0251) 8622909 –8622907, Faks. (0251) 8622907
  • Nurjanah Nurjanah Departemen Teknologi Hasil Perairan, Fakultas Perikanan dan Ilmu Kelautan, Institut Pertanian Bogor, kampus IPB Darmaga, Jalan Agatis, Bogor, Jawa Barat 16680 Telepon (0251) 8622909 –8622907, Faks. (0251) 8622907
  • Tati Nurhayati Departemen Teknologi Hasil Perairan, Fakultas Perikanan dan Ilmu Kelautan, Institut Pertanian Bogor, kampus IPB Darmaga, Jalan Agatis, Bogor, Jawa Barat 16680 Telepon (0251) 8622909 –8622907, Faks. (0251) 8622907

Abstract

Fish skin can be used as raw material for producing collagen. The collagen can be extracted by chemical
or combination of chemical and enzymatic processes. Extraction of collagen chemically can do with the
acid process that produces acid soluble collagen (ASC). This study aimed to determine the optimum
concentration and time of pretreatment and extraction, also to determine the characteristics of the acid
soluble collagen from the skin of yellow tail fish. Extraction of collagen done by pretreatment using NaOH at
the concentration of 0.05; 0.1; and 0.15 M and extraction using acetic acid at the concentration of 0.3; 0.5; and
0.7 M. Pretreatment NaOH with concentration 0.05 M and soaking time of 8 hours is the best combination
for eliminating non collagen protein. Combination treatment of acetic acid at the concentration of 0.3 M
for 3 days obtained the best solubility. The yield of collagen ASC was 18.4±1.49% (db) and 5.79±0.47%
(wb). Amino acid composition that is dominant in the ASC collagen was glycine (25.09±0.003%), alanine
(13.71±0.075%), and proline (12.15±0.132%). Collagen from yellow tail fish skin has α1, α2, β and γ
protein structure with the molecular weight of 125, 113, 170-181, and 208 KDa. The transition and melting
temperatures of collagen were 67.69oC and 144.4oC. The surface structure of collagen by analysis of SEM has
fibers on the surface.
Keywords: cholesterol, fatty acids, meat tissue, proximate, red snapper (L. argentimaculatus)

Published
2016-04-26