Aminopeptidase from jumbo squid (Dosidicus gigas) hepatopancreas: Purification, characterisation, and casein hydrolysis

Idalia Osuna-Ruíz, Gloria Yepiz-Plascencia, Ofelia Rouzaud-Sández, Josafat Marina Ezquerra-Brauer*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


An aminopeptidase (AP) was partially purified from jumbo squid (Dosidicus gigas) hepatopancreas with 154.24-fold and yield of 6.15%. The purification procedure consisted of ammonium sulphate fractionation and DEAE-Sephacel chromatography. The enzyme was approximately 48-53 kDa as estimated by SDS- PAGE. With l-leu-p-NA, it had optimum activity at pH 8.0 and 30 °C. The Km and Vmax/Km values of the enzymes for l-leu-p-NA were 0.326 mm and 2787 at 37 °C, respectively. Activation energy (Ea) of the enzyme was 53.50 kJ M-1. The AP showed activity against seven synthetic substrates: L-proline > L-methionine > Ac. l-γ-glutamic > L-glycine > L-leucine > L-alanine > L-lysine-p-NA. The enzyme was strongly inhibited by Bestatin, partially inhibited by a metal-chelating agent and by PCMB, a cystein protease inhibitor. Zn2+ and (or) Ca2+ seemed to be its metal cofactor(s). Incubation of casein with the partially purified AP resulted in a degree of hydrolysis of 6%.

Original languageEnglish
Pages (from-to)387-394
Number of pages8
JournalInternational Journal of Food Science and Technology
Issue number2
StatePublished - Feb 2010


  • Aminopeptidase
  • Casein
  • Characterisation
  • Degree of hydrolysis
  • Hepatopancreas
  • Jumbo squid
  • Marine by-products
  • Purification


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