Protease activity and partial characterization of the trypsin-like enzyme in the digestive tract of the tropical sierra Scomberomorus concolor

Hermenegildo Olivas-Burrola, Josafat Marina Ezquerra-Brauer*, Ofelia Rouzaud-Sandez, Ramon Pacheco-Aguilar

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Protease and trypsin-like activities of the digestive system of the tropical sierra Scomberomorus concolor were evaluated. Sierra digestive tract extracts hydrolyzed specific substrates for trypsin, chymotrypsin, and leucine aminopeptidase. At least eight bands of activity were observed by using SDS-PAGE. In PAGE and serine-inhibition assays, one fraction resembled bovine trypsin. An ammonium sulfate (40-60%) trypsin-like fraction displayed different inhibitions with tosyllys-chloromethyl ketone (96%) and soybean trypsin inhibitor (100%). Maximum activity was found using benzoyl-L-arginine-p-nitroanilide as substrate at pH 9.0 at 25°C and around 50°C at pH 7.8. The capacity of the trypsin-like fraction to work at different pHs (4, 7, and 9) at 25°C and different temperatures (0 and 40°C) at pH 7.8 were detected.

Original languageEnglish
Pages (from-to)51-64
Number of pages14
JournalJournal of Aquatic Food Product Technology
Volume10
Issue number4
DOIs
StatePublished - 1 Dec 2001
Externally publishedYes

Keywords

  • Digestive tract
  • Protease activity
  • Scomberomorus concolor
  • Tropical fish

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