Abstract

Acid-soluble collagen (ASC) and pepsin-solubilized collagen (PSC) were prepared from the waste freshwater carp fish scales. The results of SDS-PAGE showed that purified collagens were composed of at least two different chains which were in accordance with the type I collagen with α chain composition of (α1)2α2. Compared with the carp fish ordinary muscle type I collagen , porcine dermis type I collagen and other seawater fish collagens, freshwater carp fish scales collagen contained relative high half-cystine (Cys-s), but lower denaturation temperature(Td) than the porcine dermis type I collagen. These collagens had evident absorption at 230 nm by UV-Vis spectra. The spectrum X-ray diffraction showed that the collagen remained single-helix and tri-helix configuration with the minimum values of the repeat spacings (d) of about 4.48 A and 11.87 A. Therefore, to make more effective use of limited-resources, carp fish scales can be a potential resource for the extraction of type I collagen or gelatin.

Highlights

  • Collagen is an important protein in the organisms, and the use of collagen in industry for health foods, cosmetics, and biomaterials is expanding

  • The results of SDS-PAGE showed that purified collagens were composed of at least two different chains which were in accordance with the type I collagen with α chain composition of (α1)2α2

  • The scales of teleost fish were composed of calciumdeficient hydroxyapatite Ca10(OH)2(PO4)6 and extracellular matrix, mainly type I collagen fibers, which together formed a highly ordered three-dimensional structure

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Summary

Introduction

Collagen is an important protein in the organisms, and the use of collagen in industry for health foods, cosmetics, and biomaterials is expanding. Collagens extracted from fish scales of black drum, sheep’s head sea bream, Red seabream, Red Tilapia, sardine, Japanese sea-bass, skipjack tuna, ayu, yellow sea bream and horse mackerel have been reported [4,5,6]. These collagens are mainly type I collagen with a lower denaturation temperatures than the collagen of porcine dermis. These fish are mostly seawater fish and there have been fewer reports about the freshwater fish scales. In this paper, we extracted and partially characterized the collagens of carp fish scale for potential utilization

Demineralization Process
Morphological Analysis
Amino Acid Analysis
Determination of Denaturation Temperature
X-Ray Diffraction Analysis
Morphological Analysis of Carp Fish Scale
Subunit Composition
Amino Acid Composition
Denaturation Temperature
Conclusions

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