Handbook of Meat Processing

Curing 131

As already described, some of the proteins
even dissolve and attract each other by the
hydrophobic side chains. These swollen and
dissolved proteins form a three - dimensional
heat - stable network, as they do in emulsion -
type sausages (scheme in Fig. 6.8 ). The
hydrophobic bonds on the surface are able to
interact with each other (Fig. 6.7 ) or interact
with small “ emulsifi ed ” fat particles of meat
batters (Fig. 6.9 ) surrounding them, thus pre-
venting their cohesion to larger fat droplets
(Fig. 6.10 ) and the cookout of fat in a batter
(Table 6.2 )
When meat is heated without salt, the
denatured shrunken protein (Fig. 6.7 , left
side) is no longer able to be dissolved or
swollen by the addition of salt. This is why
products like liver pat é and blood sausages,
which are cooked before salt is added, do not
form a heat - stable batter. Pat é , with liver as
the only protein source, as well as blood sau-
sages, do not form heat - stable batters because
liver and blood proteins do not swell and
dissolve like myofi brillar proteins. These
products may be sliceable below ambient
temperatures, but above 20 to 25 ° C they are
usually spreadable.

Conclusion for the Meat Processors

Salt causes swelling of myofi bers, and with
the simultaneous addition of water, a partial
dissolving of myofi brillar proteins takes

comminuted

lean meat

plus salt and

water

fat particles

comminuted

heating

fat droplet surrounded

by protein structures

fat addition

Figure 6.8. Formation of the three - dimensional

meat batter network by comminution, salt, water,

and heating. The myofi bers are indicated by the

honeycomb - like structures, solubilized proteins are

shown by wave - like structure, fat particles are the

black rectangular or circular structures.

native protein

water

fat

by salt dissolved or swollen protein

Figure 6.9. Covering of fat particles ’ surfaces by protein. For explanation of structures, see Figure 6.7.