Characteristics of the Salt-Soluble Fraction of Hake (Merluccius merluccius) Fillets Stored at −20 and −30 °C

Abstract

Natural actomyosin (NAM) extracted in 0.6 M NaCl from hake fillets stored at -20 and -30 degrees C for up to 49 weeks was studied. The extracted protein decreased as storage progressed and became poorer in myosin while the proportion of actin remained constant. Two major peaks composed of myosin plus actin and actin plus tropomyosin plus troponins were obtained by size exclusion chromatography. SDS-PAGE analysis of the protein retained in the precolumn filter showed that there was protein aggregated by covalent bonding. Surface hydrophobicity increased while Ca(2+)-ATPase activity, apparent viscosity, and SH groups decreased as storage progressed. The loss of Ca(2+)-ATPase activity was due mainly to denaturation of the extracted myosin, whereas the minimum viscosity values occurred earlier and were not directly due to the lower proportion of myosin in the extracts. Thus, the extracted NAM exhibited changes during frozen storage. The temperature-dependent difference was mainly quantitative due to a smaller amount of protein extracted at -20 degrees C.

Comparative Study of Sodium Bicarbonate on Gelling Properties of Alaska Pollock Surimi Prepared at Different Freezing Rates

“…Frozen storage induces denaturation and aggregation of SSPs, which are major contributors to muscle functionality (Del Mazo et al . ). Extracted protein has been used to detect protein changes in frozen fish muscle (Jiménez‐Colmenero et al .…”

“…Consequently, SSPs can be used to measure/monitor changes in proteins when subjected to frozen storage (Del Mazo et al . ).…”

EFFECT OF NaCl ON GELATION CHARACTERISTICS OF ACID- AND ALKALI-TREATED PACIFIC WHITING FISH PROTEIN ISOLATES

“…These high MW proteins possibly resulted from both the pH/NaCl treatments and frozen storage of raw materials. Several studies have demonstrated that protein denaturation during frozen storage resulted in lower extractable proteins, especially myosin, with a decrease in SH groups and an increase in surface hydrophobicity (Owusu‐Ansah and Hultin 1987; LeBlanc and LeBlanc 1992; Del Mazo et al. 1999; Sultanbawa and Li‐Chan 2001).…”

Measuring parvalbumin levels in fish muscle tissue: Relevance of muscle locations and storage conditions

“…Proteins in the myofibrillar groups are more susceptible to denaturation than the sarcoplasmic proteins (Sikorski, Olley, & Kostuch, 1976). Most studies have examined the biochemical changes of myofibrillar proteins in frozen stored fish muscles (del Mazo, Torrejón, Careche, & Tejada, 1999;Jiang & Lee, 1985;Tejada et al, 1996), but no research on the alteration of parvalbumin during frozen storage has been reported.…”