@article{oai:ir.kagoshima-u.ac.jp:00004848,
 author = {御木, 英昌 and 上西, 由翁 and 西元, 諄一},
 journal = {鹿児島大学水産学部紀要=Memoirs of Faculty of Fisheries Kagoshima University},
 month = {2016-10-28},
 note = {The gel forming ability of heating myosin B (MB) prepared from shark muscle was
investigated by a slightly modified apparatus of Saunders and Ward's method for measuring
rigidity (R).
The MB-gels, so-called heat-induced gels of MB, were obtained by heating MB-sol
(protein concentration ： 20-60mg/g) of pH 5.0-7.5 at 80°C for 20 min in a water-bath and then
cooled at 0-3°C for 20 min in an ice-bath. The maximal R of MB-gel was equivalent to the R of
that after heating MB-sol of pH 6.0. For the MB-sol of pH 5.0-5.5, MB-gels were unformed
by heating. It seemed that this property was derived from the effect of the isoelectric point of
this protein. An increase of protein concentration enhanced the gel-R. A plot of double
logarithms of protein concentration and gel-R gave straight lines at pH 6.0 and 6.8. The
heating temperature required to obtain the maximal R of MB-gel was 70°C among degrees from
40°C to 90°C at pH 6.0 and 6.8 in MB-sol.
Further, the R of MB-gel was compared with the jelly strength of Kamaboko. As a result,
the R of MB-gel mostly corresponded to jelly strength of Kamaboko.
We may conclude that the gel forming ability of shark muscle is estimated from R of pure MB
for a molecular model instead of making Kamaboko practically.},
 pages = {35--43},
 title = {サメ筋肉ミオシンBの加熱ゲル形成性の測定法について},
 volume = {37},
 year = {}
}