Effect of salt treatment on beef protein thermal behaviour.

PIGHIN, D.; PAZOS, A.; GONZALEZ, C.

Dublin, Irlanda

Congreso; 52 th International Congress of Meat Science and Technology (ICoMST).; 2006

ICoMST

In the last few years, differential scanning calorimetry (DSC) has become a useful technique to study the thermal behaviour of proteins (Stabursvik & Martens, 1980). Analysis performed in different muscles established the presence of three distinctive peaks: 54-58°C, 67°C and 71-83°C (Parson & Paterson, 1986, Mietsch et al., 1994), mainly related to the thermal denaturation of myosin heads; myosin tails, sarcoplasmic proteins and collagen; and actin respectively. Studies of thermal transitions has involved protein conformation changes induced by environmental factors, such as pH and ionic strengh (Findlay & Barbut, 1990) or by the addition of different additives (Farkas & Mohácsi-Farkas, 1996).  Being these changes responsible for the variation of meat proteins stability (Ensor et al., 1991). Previous research of the group was focused on the increase of water holding capacity (WHC) of beef products added of sodium chloride (SC) and sodium tripolyphosphate (STPP) and cooked by the sous vide system (Vaudagna et al., 2005). The purpose of the present study is to investigate the thermal behaviour of muscle proteins, including isolated myofibrillar proteins, when SC and/or STPP were injected to beef Semitendinosus muscle.