Optimum Activity and Partial Characterization of Chymotrypsin from the Sciaenids Cynoscion othonopterus, Cynoscion parvipinnis, and Cynoscion xanthulus

ABSTRACT

Optimum temperature and pH for activity, as well as molecular weights of chymotrypsin from the gastrointestinal tract of the sciaenids Cynoscion othonopterus, Cynoscion parvipinnis, and Cynoscion xanthulus were evaluated. Chymotrypsins were 27.1, 26.6, and 26.5 kDa, respectively, and exhibited higher hydrolytic activity for N-benzoyl-L-tyrosine ethyl ester at 35.0–40.0°C in C. othonopterus and at 40.0°C in C. parvipinnis and C. xanthulus, whereas optimum pH values were 8.0, 7.0–9.0, and 8.0–9.0, respectively, showing a wide range of statistically similar activity for these parameters. Biochemical characteristics were comparable to chymotrypsins from other fish species already used in numerous industrial applications; thus, it is safe to assume they could be used for similar applications.

KEYWORDS:

• Chymotrypsin
• enzymatic activity
• sciaenids
• Cynoscion othonopterus
• C. parvipinnis
• C. xanthulus

Acknowledgments

We would like to thank the Consejo Nacional de Ciencia y Tecnologia (CONACYT-Mexico) for partly funding Ms. De La Reé-Rodríguez. 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 funded by [Project No. USO313006820] of the Department of Scientific and Technological Research, Biological and Health Sciences Division of the University of Sonora, Hermosillo, Sonora, Mexico.