The effect of fibrin on rheological behavior, gelling properties and microstructure of myofibrillar proteins

The aim of this study was to evaluate water-holding capacity, texture, rheological properties, interactions and microstructure of myofibrillar proteins (MP) gel with the addition of fibrin during the heat-induced process. Compared with the control, whiteness, water-holding capacity and hardness of MP gel with the addition of 2% fibrin increased by 9.70%, 79.36%, 323.07%, respectively. Storage modulus and loss modulus values in 2% fibrin addition group were higher than those of the control. The conformation of random coil gradually transformed to beta-sheet and beta-turn with the increase of fibrin content; nonspecific association and hydrophobic interactions increased from 14.27 g L-1 and 9.00 g L-1 in the control to 28.96 g L-1 and 12.90 g L-1 in the addition of 2% fibrin, respectively, indicating that these interactions played a key role in the improvement of gelling and rheological properties of MP. Scanning electron microscopy revealed that the incorporation of fibrin facilitated the formation of composited gel with a more ordered and homogeneous gel network structure. These results indicated that fibrin enhanced the functionality of MP, which could be beneficial to the development of gel-type meat products.