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 proce ss yielded myofibrillar proteins which, upon homogenization in cold wa ter and heat treatment at 70 degrees C for 15 min followed by centrifu gation, produced a low-viscosity dispersion. The proteins in the dispe rsion were stable to heating at 100 degrees C and remained soluble in solution over a wide range of pH and in the presence of some salts. Th e 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 f lavour-active free amino acids were removed by the washing process.