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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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