Extraction and characterization of acid-soluble collagen and pepsin-soluble collagen from the dry scales of the striped snakehead (Channa striatus)
DOI:
https://doi.org/10.17844/jphpi.v21i3.24734Keywords:
Extraction methods, haruan scale, protein pattern, type I collagenAbstract
Characteristics of collagen are influenced by the source of raw materials and extraction methods used. The aim of this research was to characterize the acid- and pepsin-soluble collagens from the dry scales of the striped snakehead (Channa striatus). Collagen was extracted using to methods including 0.5 M acetic acid and 0.1% pepsin. The yield of acid soluble collagen (KLA-SH) and pepsin soluble collagen (KLP-SH) were 0.98% and 1.94%, respectively. KLA-SH and KLP-SH contained glycine as the major amino acid and had high imino acid group content i.e 226 and 230 residues/1.000 residues, respectively. FTIR spectra of KLA-SH and KLP-SH showed that of the structure of collagen could be maintained in the form of triple helix structure. KLA-SH and KLP-SH consisted of α1- and α2-chain, β-chain, and γ-chain and is suggested as type I collagen.Downloads
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2018-12-28
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How to Cite
Pamungkas, B. F., Supriyadi, S., Murdiati, A., & Indrati, R. (2018). Extraction and characterization of acid-soluble collagen and pepsin-soluble collagen from the dry scales of the striped snakehead (Channa striatus). Jurnal Pengolahan Hasil Perikanan Indonesia, 21(3), 513-521. https://doi.org/10.17844/jphpi.v21i3.24734






