Premium
Fish Myosin Fragments Solubility and ANS‐Fluorescence Intensity Affected by n‐Butanol
Author(s) -
ISHIZAKI SHOICHIRO,
LIN WILOON,
TANAKA MUNEHIKO,
TAGUCHI TAKESHI,
AMANO KEISHI
Publication year - 1994
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1994.tb06906.x
Subject(s) - solubility , myosin , chemistry , fluorescence , butanol , chromatography , solubilization , intensity (physics) , ethanol , biochemistry , organic chemistry , optics , physics
Changes in the solubility and 8‐anilino‐1‐napthalene sulfonate (ANS)‐fluorescence intensity of oval filefish, tilapia, and black marlin myo‐sins and their fragments by n‐butanol were examined in connection with myosin gel‐forming abilities. The thermal gel‐forming abilities of myosins were greatly enhanced by the addition of 0.3–0.8M n‐butanol. KC1 concentration‐solubility curves revealed that after n‐butanol addition a marked decrease in the solubility was observed for myosins and S‐1s, whereas there was a slight decrease for rods. The fluorescence intensity of myosins‐ANS in the presence of n‐butanol increased markedly by heating at 30° and 35°C. A similar increase in the fluorescence intensity occurred in all S‐ls‐ANS, but not in rods.