Microstructure of fermented sausage.

A protein matrix is necessary for the desired texture of fermented sausages suitable for slicing. The formation of this network is predominantly induced by myosin and actin proteins. A change in the structure of native muscle proteins results from different technological processes such as chopping, salting, and fermentation. During chopping with simultaneous release of meat proteins, the salt brings about a change in the original structure of proteins by swelling and partial solution of myofibrils. The dissolved proteins are transformed into a thin fluid colloidal transition state, the so-called 'sol-state' with unstable coagulation bonds. During sausage ripening, as a result of denaturation by lactic-acid and due to gradual loss of water (drying), the unstable bonds are replaced by condensation bonds, and thus the sol-state is converted into the 'gel-state'. Both gel formation (condensation structure) and water evaporation (syneresis) result in the development of a matrix in fermented sausage and, consequently, in the texture of the sliceable product.