Stabilization of low denaturation temperature collagen from fish by physical cross-linking methods

Shunji Yunoki; Takeshi Suzuki; Mitsuo Takai

doi:10.1016/S1389-1723(04)70152-8

Stabilization of low denaturation temperature collagen from fish by physical cross-linking methods

J Biosci Bioeng. 2003;96(6):575-7. doi: 10.1016/S1389-1723(04)70152-8.

Authors

Shunji Yunoki¹, Takeshi Suzuki, Mitsuo Takai

Affiliation

¹ Division of Molecular Chemistry, Graduate School of Engineering, Hokkaido University, Kita-13, Nishi-8, Kita-ku, Sapporo, Hokkaido 060-8628, Japan. [email protected]

PMID: 16233576
DOI: 10.1016/S1389-1723(04)70152-8

Abstract

Collagen matrices were prepared from atelo salmon collagen (SC). SC has a lower denaturation temperature (19 degrees C) than mammalian collagen. SC matrices were successfully stabilized by ultraviolet irradiation and dehydrothermal treatment, and their optimum conditions were determined. By sponging at 37 degrees C, partial denaturation of the collagen molecules resulted in shrinkage of the matrices.