Activity and Partial Characterization of Trypsin, Chymotrypsin, and Lipase in the Digestive Tract of Totoaba macdonaldi

Emmanuel Villanueva-Gutiérrez, Carlos A. Maldonado-Othón, Martin Perez-Velazquez, Mayra L. González-Félix

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Molecular weights of trypsin, chymotrypsin, and lipase from anterior intestine and pyloric caeca of Totoaba macdonaldi were evaluated, as well as optimum temperature and pH for activity of the proteases. Trypsin was 24.1 kDa and effectively hydrolyzed Nα-benzoyl-DL-arginine 4-nitroanilide hydrochloride at optimum pH and temperature of 8 and 65°C, respectively. Chymotrypsin was 25.9 kDa and showed higher hydrolytic activity for N-benzoyl-L-tyrosine ethyl ester at pH 8 and 45°C, with a wider range of statistically similar activity values. Two pancreatic lipases of 70.2 and 47.5 kDa were detected, which could be the uncleaved and the final form of a colipase-dependent pancreatic lipase, since enzyme activity was detected without supplementation of bile salts and supplementing them inhibited activity.
Original languageEnglish
Pages (from-to)322-334
Number of pages13
JournalJournal of Aquatic Food Product Technology
Volume29
Issue number4
DOIs
StatePublished - 20 Apr 2020

Bibliographical note

Publisher Copyright:
© 2020, © 2020 Taylor & Francis Group, LLC.

Keywords

  • chymotrypsin
  • enzymatic activity
  • pancreatic lipase
  • Totoaba macdonaldi
  • Trypsin

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