The michanism of the transition of actomyosin (abbreviated as AM) to β-structure upon dehydration was studied. AM extracted from flatfish showed two rounded peaks at near 16° (2θ) and 29° in the X-ray diffraction pattern. Upon hot air dehydration at 60°C, the peak at 16° disappeared after 60min and two new peaks appeared at near 9° and at 28°; the former was rounded, while the latter was very sharp. After 120min, another rounded peak appeared at near 20°. In the presence of 3%, (w/w) glycerol, the round peak at 2° appeared after 60min and that at near 9°, after 180min, the two original peaks at near 16° and near 29° never being formed.
Both IR-spectra of AM dehydrated in the presence and absence of glycerol for 180min showed amide I and II bands at near 1620cm-1 and near 1520cm-1, respectively. The results obtained in dolphin-fish resembled the spectral data described above very closely.
- Nippon Suisan Gakkaishi is an official journal of the Japanese Society of Fisheries Science written in Japanese only.
The society publishes an English journal, Fisheries Science, as well, which accepts submissions from non-members of the society over the world. Detailed information is available in http://jsfs.jp/en/journals/fisheries-science.