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

Héctor M. Sarabia-Sainz, Josafat Marina Ezquerra-Brauer, Hisila C. Santacruz-Ortega, Ofelia Rouzaud-Sández, Elisa M. Valenzuela-Soto, Monica Acosta-Elias, Wilfrido Torres-Arreola*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

Muscle from mantle, fins and arms of squid (Dosidicus gigas) 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.

Original languageEnglish
Pages (from-to)57-64
Number of pages8
JournalFood Science and Biotechnology
Volume27
Issue number1
DOIs
StatePublished - 1 Feb 2018

Bibliographical note

Publisher Copyright:
© 2017, The Korean Society of Food Science and Technology and Springer Science+Business Media B.V., part of Springer Nature.

Keywords

  • Chemical structure
  • Hydroxymerodesmosine
  • Lysyl oxidase
  • Squid collagen
  • Thermal denaturation

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