Lysyl oxidase from jumbo squid (Dosidicus gigas) muscle: Purification and partial characterization

Wilfrido Torres-Arreola*, Josafat Marina Ezquerra-Brauer, Ramón Pacheco-Aguilar, Elisa M. Valenzuela-Soto, Ofelia Rouzaud-Sandez, Maria E. Lugo-Sanchez, Gisela Carvallo-Ruiz

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


Lysyl oxidase (LOX; E.C. was purified from jumbo squid muscle (Dosidicus gigas) with 1900-fold and yield 1.9%, and characterized for the first time. The purification procedure consisted of fractionation with urea and a combination of size-exclusion and anion-exchange chromatography. The enzyme had a molecular weight of 32kDa, as estimated by SDS-PAGE. Using a specific LOX substrate (1,5-diaminopentane), its optimum activity was determined at pH 8.2 and 65°C. Activation energy (E a) of the enzyme was 69.94kJK -1mol -1. The enzyme was strongly inhibited by β-aminopropionitrile fumarate (BAPN), a specific LOX inhibitor. Moreover, purified LOX was able to work at different temperatures (20-90°C) at pH 8.2. Although further research is needed, the results from this work suggest that based on LOX activity, this enzyme may be of practical use in preventing textural changes in jumbo squid during storage or processing.

Original languageEnglish
Pages (from-to)947-953
Number of pages7
JournalInternational Journal of Food Science and Technology
Issue number5
StatePublished - May 2012


  • Characterization
  • Collagen
  • Jumbo squid
  • Lysyl oxidase
  • Purification


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