M. Careche et al., IMPORTANCE OF FROZEN STORAGE-TEMPERATURE IN THE TYPE OF AGGREGATION OF MYOFIBRILLAR PROTEINS IN COD (GADUS-MORHUA) FILLETS, Journal of agricultural and food chemistry, 46(4), 1998, pp. 1539-1546
Cod fillets were examined to determine the effect of two frozen storag
e temperatures (-20 and -30 degrees C) on the formation of aggregates
and if this relates to changes in texture and functionality. The evolu
tion of apparent viscosity during frozen storage was similar at either
storage temperature. Loss of extractability in 0.6 M NaCl was slightl
y greater at -20 degrees C. The aggregate which formed at -30 degrees
C was extractable in solutions which cleave secondary interactions [2%
sodium dodecyl sulfate (SDS)] whereas at -20 degrees C the role of no
n-disulfide covalent bonds was more important, so that this aggregate
was not totally extracted in 2% SDS plus 5% beta-mercaptoethanol. The
aggregates consisted largely of myosin and actin, but myosin was the m
ost important constituent, contributing more to the formation of coval
ent bonds, particularly at the higher temperature. This difference in
aggregation was accompanied with a difference in the evolution over ti
me of shear resistance, which was higher at -20 degrees C.