T. Shoji et al., INFLUENCE OF AMMONIUM SALT ON THE FORMATI ON OF PRESSURE-INDUCED GEL FROM WALLEYE POLLACK SURIMI, Nippon Suisan Gakkaishi, 60(1), 1994, pp. 101-109
To investigate the effect of ammonium ion on the quality of pressure-i
nduced gel, walleye pollack surimi was ground with NaCl, or NaCl conta
ining a small amount of (NH4)2SO4 or NH4Cl. The salt-ground meat was t
hen treated under 300 MPa at 0-degrees-C for 10 min followed by storag
e at 5-degrees-C for 120 hours, and breaking strength and breaking str
ain together with subunit composition of myofibrillar protein were eva
luated. Transglutaminase activities and epsilon-(gamma-glutamyl) lysin
e contents were also measured. The results obtained were as follows: (
1) Transglutaminase activity of the salt-ground meat was mostly inacti
vated by the pressure-treatment, (2) The rates of formation of cross-l
inked myosin heavy chain (60% of total protein) and of epsilon-(gamma-
glutamyl) lysine (2.7 mg/g) in the pressure-induced gel were virtually
identical with those in the setting gel from the same surimi, (3) The
breaking strength of the pressure-induced gel reached more than twice
that of the setting gel, (4) Addition of ammonium salts to the salt-g
round meat largely suppressed the formation of cross-linked myosin hea
vy chain and of epsilon-(gamma-glutamyl) lysine, while the breaking st
rength of the pressure-induced gel remained at half the level of that
of the gel formed without ammonium salts. These results suggested that
intermolecular hydrophobic interaction between myofibrillar proteins,
which was formed through the pressure-treatment, might contribute to
the production of an elastic gel.