It was observed that the amount of salt soluble protein from myofibrils of Antarctic krill Euphausia superba muscle and its physicochemical and biochemical properties, such as viscosity, ATP-sensitivity, flow birefringence, Mg-ATPase activity and gel-forming ability were increased with the lapse of aging time of washed muscle at 2°C, reaching to the maximum values within a few days.
On the basis of these findings, the authors developed a new method to collect myofibrillar protein in high yeild as the debris of myofibrils (nmaed Myofibrils Fragmemt, MfF) from the muscle after aging by the following procedure: the muscle was homogenized wiht 10 volumes of 0.3% NaCl solution and sedimented by high speed centrifugation at 10, 000×g for 10minutes.
The myofibrils preparation, thus obtained, was found to form a Kamaboko-like gel having a characteristic nature (elasticity) upon grinding with 5% NaCl at 2°C for 2 minutes, setting (suwari) at 5°C for 3 hours and heating at 90°C for 20 minutes.
The addition of sorbitol (ca. 10%) to the myofibrils preparation remarkably strengthened the gel strength of the gel formed by heating.