Muscle lysyl oxidase activity and structural/thermal properties of highly cross-linked collagen in jumbo squid (Dosidicus gigas) mantle, fins and arms

Abstract

Muscle from mantle, fins and arms of squid () were compared based on lysyl oxidase activity (LOX), chemical/structural and thermodynamic properties of highly cross-linked collagen. The arms collagen presented the highest temperature (Tp) and enthalpy of transition. The arms collagen thermic properties may be explained by the higher imino amino acid content, proline and lysine hydroxylation degrees. Moreover, among the regions, the collagen from the arms had a more intense β band chain, hydroxymerodesmosine peak in the resonance magnetic nuclear spectra and pyridinoline peak in the Raman spectra. Fins showed the highest LOX activity. The LOX activity was associated with the Tp, proline and lysine hydroxylation degrees. These results implied that the collagen in the arms was more intermolecularly ordered than the mantle and fins, and may provide a theoretical basis for a better understanding of the thermal behaviour of squid tissues during management and processing.

Physicochemical changes of pepsin-solubilized and insoluble collagen in jumbo squid (Dosidicus gigas) muscle after cooking process

“…Furthermore, the collagen content in the marine organism has been established within a wide range, varying from 3 to 18% in different squid species. [10,[18][19][20][21] Since there is a close relationship between the extraction yield (EY) and CS from jumbo squid muscle, this variability also could be observed in the crosslinking degree of the collagen fibers. [5] In jumbo squid muscle, Sarabia-Sainz et al [19] found a lower solubility in collagen extracted from arms compared to the collagen extracted from fins and mantle.…”

Proteomic identification and physicochemical characterisation of paramyosin and collagen from octopus (Octopus vulgaris) and jumbo squid (Dosidicus gigas)

“…, 2018; Sarabia‐Sainz et al . , 2018). The differences on the maximum denaturation temperature (Tmax, °C) could be attributed to various factors such as the protein replacement during the growth of the cephalopod.…”

“…, 2015a; Sarabia‐Sainz et al . , 2018). Likewise, the presence of the endothermic transition above the 100 °C confirms the presence of collagen (Torres‐Arreola et al .…”

Relationship between muscle texture and the crosslinking degree of collagen fibers from octopus ( Octopus vulgaris ), guitarfish ( Rhinobatos productus ), and cazon ( Mustelus lunulatus )

“…During the biogenesis of the connective tissue (CT) matrix, Lox oxidizes the Lys residues in collagen and elastin, thereby initiating the formation of covalent cross‐links that stabilize these fibrous proteins (Smith‐Mungo & Kagan, ). When the Lox activity is high, it will induce a high production of Pyr (Li et al, ; Sarabia‐Sainz et al, ). The Pyr molecule is a very active component of the extracellular matrix that gives stability and hardness to collagen fibers (Eyre & Wu, ).…”

“…When the Lox activity is high, it will induce a high production of Pyr (Li et al, 2005;Sarabia-Sainz et al, 2018). The Pyr molecule is a very active component of the extracellular matrix that gives stability and hardness to collagen fibers (Eyre & Wu, 2005).…”