The thermal gel-formation properties of oval filefish muscle proteins
in the presence of n-butanol were examined by means of thermal gelatio
n curves, SDS-electrophoretograms, solubility tests, and changes in th
e fluorescence intensity caused by ANS (8-anilino-1-naphthalene sulfon
ate). The addition of 0.3 M or 0.6 M n-butanol markedly accelerated th
e thermal gelation of oval filefish myofibrillar paste, and perfectly
depressed the gel disintegration (himodori) at 60-degrees-C. In the pr
esence of n-butanol, the actomyosin solubility dependent upon the KCl
concentration decreased and there was a marked increase in actomyosin-
ANS fluorescence intensity due to heating.