Surface hydrophobicity and functional properties of myofibrillar proteins of mantle from frozen-stored squid (Illex argentinus) caught either jigging machine or trawling

The surface hydrophobicity and functional properties of actomyosin from the mantle of frozen squid caught either by jigging machines (AME1) or by trawl (AME2) were investigated. Two components of 155 and 55 kDa were present in the gels at zero time of storage. Degradation of the myosin heavy chain and increase in the 155 kDa component occur earlier in AME2. Irrespective of the catch method used, no significant (P>0.05) changes in protein solubility were observed. The reduced viscosity of both AME1 and AME2 decreased up to months 3 and 5 of frozen storage, respectively. At the beginning of storage, the superficial hydrophobicity of AME2 was 30% higher than that of AME1. So 1-anilino-8-naphthalene sulfonic acid of AME2 significantly increased during 3–5 months of storage period and that of AME1 at the end of storage. The emulsion activity index (EAI) of AME2 significantly (P<0.05) increased during the first month and decreased after 3 months of storage. EAI of AME1 decreased at month 3 and remained unchanged thereafter. Emulsion stability (ES) of AME2 showed a behavior that was similar to its IAE and that of AME1 remained unchanged.