Literature DB >> 28832833

Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus.

F B Candiotto1, A C V Freitas-Júnior2, R C A Neri3, R S Bezerra3, R V Rodrigues1, L A Sampaio1, M B Tesser1.   

Abstract

Knowledge of specific enzyme activity, along with animal habits and digestive capacity is essential in formulating an appropriate diet for any species. In this study, we evaluated and characterized the activity of digestive enzymes present in the liver, intestine, and stomach of Paralichthys orbignyanus. The effects of pH and temperature on enzyme activity were also evaluated via the use of specific substrates. The use of specific substrates and inhibitors showed strong evidence of the presence of trypsin (BApNA= 0.51 ± 0.2 mU mg-1), chimotrypsin (SApNA= 2.62 ± 1.8 mU mg-1), and aminopeptidases (Leu-p-Nan =0.9709 ± 0.83 mU mg-1) in the intestine. Optimum pH for the activity of trypsin, chemotrypsin, leucino aminopeptidase, amilase, and pepsin were 9.5, 9.0, 8.0, 7.5, and 3.5, respectively, while optimum temperatures were 50, 50, 50, 40, and 45 °C, respectively. These results provide additional information regarding the biology of Brazilian flounder and can be used as a basis for further studies regarding fish feeding physiology.

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Year:  2017        PMID: 28832833     DOI: 10.1590/1519-6984.06616

Source DB:  PubMed          Journal:  Braz J Biol        ISSN: 1519-6984            Impact factor:   1.651


  1 in total

1.  Expression and Functional Analysis of Hepcidin from Mandarin Fish (Siniperca chuatsi).

Authors:  Yawei Shen; Ziwei Zhao; Jinliang Zhao; Xiaowu Chen; Ming Cao; Minglin Wu
Journal:  Int J Mol Sci       Date:  2019-11-09       Impact factor: 5.923

  1 in total

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