Effect of temperature on the actomyosin-paramyosin structure from giant squid mantle (Dosidicus gigas).

BACKGROUND: The secondary structure of a protein determines its functional properties, such as its gelling capacity. The α-helix and ß-sheet comprise its main structures. Myofibrillar proteins from jumbo squid are composed mainly of the actomyosin-paramyosin complex; this complex contains a high percentage of α-helix, because actin, paramyosin, and myosin constitute 30%, 100%, and 55% of the α-helix, respectively. It is important to elucidate the role of the secondary structures in the gelation of giant squid proteins as they form gel. The role of the secondary structures in the gelation of giant squid proteins is therefore very important. For this reason, the objective of this work was to evaluate the effect of temperature on the structural behavior of actomyosin-paramyosin isolate (API) from Dosidicus gigas. RESULTS: The unfolding of the API system, which is composed of the actomyosin-paramyosin complex, was clarified by studying surface hydrophobicity and viscosity. Three characteristic peaks were found, associated with myosin, paramyosin, and actin. Infrared and circular dichroism corroborated the view that API undergoes major structural changes, because it proceeds from mostly an α-helix structure to 100% ß-sheet. CONCLUSION: The structural rearrangement favors gelation by cross-linking, generating new protein-protein and water-protein interactions, which create a more stable structure compared to mantle proteins (MP). Likewise, the presence of sarcoplasmic and stromal proteins in D. gigas muscle prevents the unfolding of myofibrillar proteins, favoring gelation by agglomeration, decreasing the ability to trap water and thus its gelling capacity. © 2019 Society of Chemical Industry.

Physicochemical characterization of actomyosin-paramyosin from giant squid mantle (Dosidicus gigas).

BACKGROUND: The giant squid (Dosidicus gigas) has been proposed as raw material to obtain myofibrillar protein concentrates. However, it has been observed that colloidal systems formed from squid proteins have limited stability. Therefore, the isolation and characterization of the actomyosin-paramyosin isolated (API) complex were performed, because they are the main proteins to which functionality has been attributed. RESULTS: Densitogram analysis revealed 45% of actin, 38% of myosin and 17% of paramyosin. The amino acid profile indicates a higher proportion of acidic amino acids, which gives a higher negative charge; this was supported by the zeta potential. Total sulfhydryl (TSH) content was lower compared with proteins of other aquatic species. CONCLUSION: The higher percentage of actin in relation to myosin, the presence of paramyosin, as well as the low content of sulfhydryl groups, could comprise the main causes of the low technological functional property of proteins from D. gigas mantle. © 2017 Society of Chemical Industry.

Relationship between histochemical, structural characteristics and oxidative stability of rhea limb muscles.

Histochemical and structural characteristics were investigated in Gastrocnemius pars interna (GN) and Iliofiburalis (IF) limb muscles of Rhea americana. The average myofibre area cross-section was greater in GN than IF muscle (p<0.001), whereas the fibre density per section was higher in IF than GN muscle. The only type of myofibre found in both the rhea limb muscles analysed in this study was fast-twitch oxidative-glycolytic fibres (FOG). Immunolabelling analysis and ultrastructural observation of myofibres confirmed the contractile and metabolic characteristics of rhea myofibres, revealing the absolute fast isoform of myosin heavy chain and the abundance of glycogen and mitochondria inside the cells, mainly in IF muscle. These findings converged with previous results on the biochemical and physicochemical characteristics of rhea meat to provide further evidence that myofibre composition substantially influences the oxidative reactions of the muscle and therefore the meat quality, but more in-depth examination is needed to establish the links between myofibre characteristics, myofibre glycogen concentration and meat stability during storage.