Spearation of Myofibrils from Antarcitc Krill Muscle and Properties of Heated Gel from It

Abstract

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.