EXTRACTABILITY AND STABILITY OF WASHED CAPELFIN (MALLOTUS-VILLOSUS) MUSCLE IN WATER

Whole capelin (Mallotus villosus) mince was sequentially washed with c old water (< 10-degrees-C) and aqueous solutions of 0.5% NaCl and 0.5% NaHCO3. The washed mince was suspended in cold water at concentration s of 5-30%. The suspensions were homogenized after an 18 h incubation at ambient temperature. heated to 70 or 100-degrees-C for 15 min and t hen centrifuged at 1160 g for 10 min. The prepared dispersion containe d up to 90% of the proteins present in the washed mince. The protein d ispersion was highly thermostable. Solubility of protein in the disper sion was not affected even after heating the dispersion at 100-degrees -C for 30 min, centrifugation for 1 h at 12 000 g. repeated freeze-tha w operations, or after increasing the pH values >7.0 in combination wi th heat. Addition of calcium and sodium chlorides caused precipitation of the protein. which was reversed by tripolyphosphate. Low levels of CaCl2 enhanced apparent viscosity as well as turbidity of the dispers ion as determined spectrophotometrically at 600 nm. Its amino acid com position was generally comparable to those of fish myosins.