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Comparison of proteolytic activities of the enzyme complex from mammalian pancreas and pancreatin

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Abstract

The proteolytic activity and thermal stability of the enzyme complex of a cell suspension from pig and bovine pancreas glands was compared with those of pancreatin. The enzyme complex displayed the highest thermal stability and activity at 50°C. The kinetic constants, energies of activation and inactivation of the enzyme complex, and pH optimum (7.0 ± 0.1) at which this complex had the maximum proteolytic activity were determined. Pancreatin had a pH optimum of 8.0 ±0.1.

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Authors and Affiliations

  1. All-Russia Institute of the Meat Industry, 109316, Moscow, Russia

    A. V. Berdutina, A. D. Neklyudov, A. I. Ivankin, B. S. Karpo & S. I. Mitaleva

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  1. A. V. Berdutina
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  2. A. D. Neklyudov
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  3. A. I. Ivankin
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  4. B. S. Karpo
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  5. S. I. Mitaleva
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Berdutina, A.V., Neklyudov, A.D., Ivankin, A.I. et al. Comparison of proteolytic activities of the enzyme complex from mammalian pancreas and pancreatin. Appl Biochem Microbiol 36, 363–367 (2000). https://doi.org/10.1007/BF02738043

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  • DOI: https://doi.org/10.1007/BF02738043

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