Changes in the muscle proteins during the ripening of salted anchovies have been examined using sodium dodecyl sulphate polyacrylamide gel electrophoresis. The chemical changes occurring in the muscle proteins of anchovy during the ripening process were related to the degradation of the myofibrillar structure of the muscle. In spite of a considerable protein degradation the ripened salted anchovy maintained its structure and was easily cut into fillets. Hydrolysis of muscle proteins was significant during the first 6 weeks. Proteins of molecular weight higher than 35 kDa were more likely to be hydrolysed. Myosin heavy chains were the most sensitive myofibrillar protein. α-Actinin, actin and tropomyosin were more resistant to enzymatic degradation. Due to protein build-up of peptides resulting from the breakdown of the higher molecular proteins, it was difficult to measure changes in the myosin light chains and troponin sub-units. © Springer-Verlag 2000.
|Journal||European Food Research and Technology|
|Publication status||Published - 1 Jan 2000|