Conformational Changes in Black Marlin Myosin at Interface as Affected by Air-Blowing in Relation to Gel-Formation

Abstract

The conformational changes in black marlin myosin and its fragments at interfaces as affected by air-blowing in relation to gel-formation were examined by means of solubility test, CD measurement, and reactivity with fluorescent probe (8-anilino-1-naphthalene sulfonate: ANS). Air-blowing treatment, accompanied by dehydration from the surface of myosin sol, noticeably facilitated its thermal gelation on the surface of myosin gel. It was revealed that the solubility of myosin and the helix content of myosin, S-1, and rod decreased during air-blowing. The fluorescence intensity of myosin-ANS increased with air-blowing time. The intensity of air-blown S-1-ANS showed a marked increase, whereas that of the rod-ANS was almost unchanged.