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

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.

KEYWORDS:

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

Acknowledgments

The authors are thankful to the Biological and Health Sciences Division of the University of Sonora for partly funding Project No. USO313003465. We would like to thank the Consejo Nacional de Ciencia y Tecnologia (CONACYT-Mexico) for partly funding Mr. Villanueva-Gutiérrez and Mr. Maldonado-Othón. The mention of trademarks or proprietary products does not constitute an endorsement of the product and does not imply its approval to the exclusion of other products that may also be suitable.

Disclosure statement

No potential conflict of interest was reported by the author(s).

Additional information

Funding

This study was partly funded by the Biological and Health Sciences Division of the University of Sonora, Hermosillo, Sonora, Mexico, Project No. USO313003465.