Water dispersions of myofibrillar proteins from capelin (Mallotus villosus)

Mechanically deboned whole capelin was subjected to washing with water, 0.5% sodium chloride, and 0.5% sodium bicarbonate. The washing process yielded myofibrillar proteins which, upon homogenization in cold water and heat treatment at 70 °C for 15 min followed by centrifugation, produced a low-viscosity dispersion. The proteins in the dispersion were stable to heating at 100 °C and remained soluble in solution over a wide range of pH and in the presence of some salts. The amino acid composition of the dispersion was similar to that of the original mince. The product was nearly bland in taste as most of its flavour-active free amino acids were removed by the washing process.