Conclusions
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1.
α-Chymotrypsin (CT), enclosed in positively and negatively charged polyelectroiyte gels based on methacrylate, with a preservation of high catalytic activity, was produced.
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2.
The pH profile of the enzymatic activity of CT enclosed in gel is shifted in absolute magnitude by approximately 1 pH unit, while the sign of the shift agrees with the theory.
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3.
The incorporation of CT into a negatively charged gel leads to a sharp (600-fold) increase in its stability with respect to monomolecular thermal inactivation. The stabilization is due to the influence of the polymer matrix on the protein globule of the enzyme.
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Translated from Izvestiya Akademii Nauk SSSR, Seriya Khimicheskaya, No. 8, pp. 1764–1768, August, 1975.
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Chernysheva, A.V., Marinek, K., Klibanov, A.M. et al. Catalytic properties and thermal stability ofα-chymotrypsin in polyelectrolyte gels based on methacrylate. Russ Chem Bull 24, 1648–1652 (1975). https://doi.org/10.1007/BF01100013
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DOI: https://doi.org/10.1007/BF01100013