THERMAL AGGREGATION OF SARDINE MUSCLE PROTEINS DURING PROCESSING

摘要

This paper seeks to relate rheological changes occurring in sardine mince homogenized with NaCl (1.5% and 2.5%) during gelation to the formation of different types of chemical bonding and to identify the involvement of myofibrillar proteins in these bonds. Setting and modori occur in sardine muscle to a marked degree. In setting there is heavy involvement of the myosin heavy chain (MHC), which is polymerized chiefly by means of stronger bonds than hydrophobic interactions. In modori, on the other hand, hydrophobic interactions prevail. In the gel made at 90 degrees C, MHC was the main protein implicated, through disulfide bonds or other covalent bonds. In gelation of sardine muscle, in general there is little involvement of other myofibrillar proteins such as actin, tropomyosin, and troponins and other low MW proteins.