Studies on fish scale collagen of Pacific saury (Cololabis saira)

Hideki Mori; Yurie Tone; Kouske Shimizu; Kazunori Zikihara; Satoru Tokutomi; Tomoaki Ida; Hideshi Ihara; Masayuki Hara

doi:10.1016/j.msec.2012.08.025

Studies on fish scale collagen of Pacific saury (Cololabis saira)

Hideki Mori, Yurie Tone, Kouske Shimizu, Kazunori Zikihara, Satoru Tokutomi, Tomoaki Ida, Hideshi Ihara, Masayuki Hara

Research output: Contribution to journal › Article › peer-review

41 Citations (Scopus)

Abstract

We purified and characterized Type I collagen from the scales of the Pacific saury (Cololabis saira) and compared it with collagen from other organisms. Subunit composition of C. saira collagen (2α1 + α2) was similar to that of red sea bream (Pagrus major) and porcine collagen. C. saira collagen did not form a firm gel after neutralization of pH in solution. The temperature of denaturation (24-25 °C) of C. saira collagen was slightly lower than that of P. major collagen (26-27 °C). The contents of proline and hydroxyproline were lower in red sea bream and Pacific saury collagen than in porcine collagen. Circular dichroism spectra and Fourier-transformed infrared spectra showed that heat denaturation caused unfolding of the triple helices in all three collagens.

Original language	English
Pages (from-to)	174-181
Number of pages	8
Journal	Materials Science and Engineering C
Volume	33
Issue number	1
DOIs	https://doi.org/10.1016/j.msec.2012.08.025
Publication status	Published - 2013 Jan 1
Externally published	Yes

Keywords

Collagen
Denaturation temperature
Fibril
Fish scale
Gel
Pacific saury

ASJC Scopus subject areas

Materials Science(all)
Condensed Matter Physics
Mechanics of Materials
Mechanical Engineering

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abstract = "We purified and characterized Type I collagen from the scales of the Pacific saury (Cololabis saira) and compared it with collagen from other organisms. Subunit composition of C. saira collagen (2α1 + α2) was similar to that of red sea bream (Pagrus major) and porcine collagen. C. saira collagen did not form a firm gel after neutralization of pH in solution. The temperature of denaturation (24-25 °C) of C. saira collagen was slightly lower than that of P. major collagen (26-27 °C). The contents of proline and hydroxyproline were lower in red sea bream and Pacific saury collagen than in porcine collagen. Circular dichroism spectra and Fourier-transformed infrared spectra showed that heat denaturation caused unfolding of the triple helices in all three collagens.",

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AU - Mori, Hideki

AU - Tone, Yurie

AU - Shimizu, Kouske

AU - Zikihara, Kazunori

AU - Tokutomi, Satoru

AU - Ida, Tomoaki

AU - Ihara, Hideshi

AU - Hara, Masayuki

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N2 - We purified and characterized Type I collagen from the scales of the Pacific saury (Cololabis saira) and compared it with collagen from other organisms. Subunit composition of C. saira collagen (2α1 + α2) was similar to that of red sea bream (Pagrus major) and porcine collagen. C. saira collagen did not form a firm gel after neutralization of pH in solution. The temperature of denaturation (24-25 °C) of C. saira collagen was slightly lower than that of P. major collagen (26-27 °C). The contents of proline and hydroxyproline were lower in red sea bream and Pacific saury collagen than in porcine collagen. Circular dichroism spectra and Fourier-transformed infrared spectra showed that heat denaturation caused unfolding of the triple helices in all three collagens.

AB - We purified and characterized Type I collagen from the scales of the Pacific saury (Cololabis saira) and compared it with collagen from other organisms. Subunit composition of C. saira collagen (2α1 + α2) was similar to that of red sea bream (Pagrus major) and porcine collagen. C. saira collagen did not form a firm gel after neutralization of pH in solution. The temperature of denaturation (24-25 °C) of C. saira collagen was slightly lower than that of P. major collagen (26-27 °C). The contents of proline and hydroxyproline were lower in red sea bream and Pacific saury collagen than in porcine collagen. Circular dichroism spectra and Fourier-transformed infrared spectra showed that heat denaturation caused unfolding of the triple helices in all three collagens.

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KW - Denaturation temperature

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KW - Fish scale

KW - Gel

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