Carp natural actomyosin: thermal denaturation mechanism

A study of the effects of heat on the structure of natural actomyosin taken from a muscle of a live carp used biophysical and biochemical methods to reveal the thermal denaturation process of actomyosin. At 30 degrees centigrade, actomyosin molecules start to unfold, allowing hydrophobic amino acid residues and reactive sulfhydryls to surface, and begin to form aggregates as a result of hydrophobic interactions and disulfide bonds. Above 40 degrees centigrade, myosin dissociates from the actin filaments, which start to separate. At 60 degrees centigrade and above, the actomyosin molecules group into larger aggregates, a portion of which is insoluble.