Water mobility and distribution of a dual-protein system of surf clam myofibrillar protein (MP) and soy protein (SP) was investigated by the nondestructive low field nuclear magnetic resonance (LF-NMR) technique. Four proton populations were found in the contour plots of T2 relaxation times for the SP-MP system. The first component, (T21), was assigned to the highly integrated water located in protein macromolecules with a relaxation time of approximately 1.15 ms. The second signal, T22, with a relaxation time of 2.20 to 38.00 ms was regarded as the inter-myofibrillar water trapped in organized protein structures. The third component, T23, with a relaxation time of around 100 ms was ascribed to the extra-myofibrillar water. With an increase in temperature, T24 appeared which was assigned to the free water within the extra-myofibrillar space. The gelation behavior occurred at 70, 62, and 52 °C as the proportion of SP/MP was 4:6, 2:8, and 0:10, respectively. The principal component analysis (PCA) and heatmap of LF-NMR data analysis showed potential for distinguishing the different dual-protein systems formed at various temperatures. The analysis of storage modulus G', loss modulus G″, and tanδ confirmed the change trend of the LF-NMR results. The measurements of cooking loss, water holding capability, and gel strength further revealed that the SP and MP were likely to form a gel network with an increase of additional clam protein. The hydrophobicity analysis showed, for the systems with the SP/MP proportions of 4:6, 2:8, and 0:10, more hydrophobic groups were exposed when the temperature was over 50 °C. Scanning electron microscopy showed that the number of the micropores increased with an addition of MP in the dual-protein system of SP/MP. All the results demonstrated that LF-NMR has great potential for characterizing the gelation process of a dual-protein system.
Keywords: LF-NMR; gelation; myofibrillar protein; soy protein.