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[On the changes in alpha-chymotrypsin stability after its modification by polyelectrolytes]

L Ia Bessmertnaia, L V Kozlov, V K Antonov

    Biokhimiia (Moscow, Russia)
    |October 1, 1977
    PubMed
    Summary

    The study shows that binding alpha-chymotrypsin (an enzyme) to polymers alters its native state, making it more like a denatured state. This affects enzyme stability and denaturation parameters but not renaturation.

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    Area of Science:

    • Biochemistry
    • Polymer Science
    • Enzyme Kinetics

    Context:

    • Investigating protein stability and denaturation.
    • Understanding enzyme-polymer interactions.
    • Exploring modifications of alpha-chymotrypsin.

    Purpose:

    • To study the reversible thermal denaturation of alpha-chymotrypsin.
    • To analyze the effects of electrostatic complexation and covalent binding with carboxyl-containing polymers on enzyme stability.
    • To compare the denaturation and renaturation parameters of the native enzyme with its polymer-bound derivatives.

    Summary:

    • The study examined the thermal denaturation of alpha-chymotrypsin and its complexes/covalently bound forms with carboxyl-containing polymers.
    • Enzyme stability was found to be matrix-dependent, indicated by decreased enthalpy and entropy of denaturation and activation.

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  • Renaturation parameters remained largely unaffected, suggesting differences in the initial states but similarity in activated states between the enzyme and its derivatives.

    • Impact:

    • Reveals that polymer matrices significantly alter the native state of alpha-chymotrypsin, mimicking aspects of denaturation.
    • Provides insights into how protein structure and stability are modulated by conjugation with polymers.
    • Contributes to understanding enzyme immobilization and its thermodynamic consequences.