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

研究成果: Article › 査読

48 被引用数 (Scopus)

抄録

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.

本文言語	English
ページ（範囲）	174-181
ページ数	8
ジャーナル	Materials Science and Engineering C
巻	33
号	1
DOI	https://doi.org/10.1016/j.msec.2012.08.025
出版ステータス	Published - 2013 1月 1
外部発表	はい

ASJC Scopus subject areas

材料科学（全般）
凝縮系物理学
材料力学
機械工学

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10.1016/j.msec.2012.08.025

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title = "Studies on fish scale collagen of Pacific saury (Cololabis saira)",

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.",

keywords = "Collagen, Denaturation temperature, Fibril, Fish scale, Gel, Pacific saury",

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

note = "Funding Information: This research was partially supported by the Asahi Beer Science Promotion Foundation and the Sentan Kagaku Kyoudou Kenkyu Project of Osaka Prefecture University (OPU) . The authors would like to thank the members of the Eishin Kasei Company and Prof. Emer. Yoshihisa Nakano of OPU for their support of the project.",

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AU - Tokutomi, Satoru

AU - Ida, Tomoaki

AU - Ihara, Hideshi

AU - Hara, Masayuki

N1 - Funding Information: This research was partially supported by the Asahi Beer Science Promotion Foundation and the Sentan Kagaku Kyoudou Kenkyu Project of Osaka Prefecture University (OPU) . The authors would like to thank the members of the Eishin Kasei Company and Prof. Emer. Yoshihisa Nakano of OPU for their support of the project.

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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 - Fibril

KW - Fish scale

KW - Gel

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

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