Abstract
Studies on the freeze denaturation of fish muscle proteins were reviewed with emphasis given to changes in their physicochemical and biochemical properties during frozen storage. Denaturation of actomyosin commonly occurs during frozen storage and side-to-side aggregation of myosin molecules apppears to major role in this reaction. The author's group performed freezing studies with isolated preparations of proteins from carp muscle, namely actomyosin, myosin, H-meromyosin, L-meromyosin, and actin. Freeze denaturation occurred with indvidual proteins as well as with their subunits. Not only aggregation but also some conformational changes were observed. Denaturation was inhibited in the presence of added glutamate.
