Nippon Suisan Gakkaishi 68 (2), 137-143 (2002)

Denaturation of muscular proteins from marine animals and its control


Scientific Adviser on National Surimi Manufacturers Association, Abashiri, Hokkaido 093-0057, Japan

It is well-known that there is a striking relationship between the thermostability of myofibrillar Ca-ATPase activity and the environmental temperature at which the fish live. The difference in thermostability among fish species is attributable to physiological adaptation of this enzymes to the environment at the molecular level.

Recently, the thermostability of the rod portion of myosin molecule relative to that of its subfragment-1 portion was found to be different among several fish species. This finding may suggest that there exists another species-specific character of fish myosin.

Consequently, preventive measures have been taken against the denaturation of myofibrillar protein caused by long-term storage of fish muscle as foodstuff. An actual fruit in the food industry can be realized in the procedure for the production of frozen surimi.

The most popular processed seafood in Japan is a surimi-based product (kamaboko). Studies indicate that the heat-induced gelation of salt-ground mince is closely related to the regular reaction between myofibrillar protein and NaCl through the thermal denaturation of myosin in it. Accordingly, it is necessary to conduct kinetic studies on the gel forming reaction, which is a useful approach to understanding the mechanism, and to predict the quality of final gel product.

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