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Superactive β-galactosidase inclusion bodies.

Sandra S Flores1, Verónica Nolan1, María A Perillo1

  • 1Universidad Nacional de Córdoba, Facultad de Ciencias Exactas, Físicas y Naturales, ICTA and Departamento de Química, Cátedra de Química Biológica, Córdoba, Argentina; CONICET, Instituto de Investigaciones Biológicas y Tecnológicas (IIBYT), Córdoba, Argentina.

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Bacterial inclusion bodies (IBs) containing beta-galactosidase are functional and stable enzyme reservoirs. Releasing the enzyme from these aggregates yields active protein with altered kinetic properties.

Keywords:
Catalytic activityInclusion bodiesProtein desorption processβ-Galactosidase

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Bacterial inclusion bodies (IBs) were traditionally viewed as inactive protein aggregates, hindering recombinant protein production.
  • Recent findings suggest IBs can contain active protein, challenging previous assumptions.

Purpose of the Study:

  • To investigate the functionality and characteristics of recombinant beta-galactosidase inclusion bodies (IBβ-Gal).
  • To determine if IBβ-Gal serves as a stable and active enzyme source.

Main Methods:

  • Characterization of IBβ-Gal activity under varying pH and temperature conditions.
  • Analysis of enzyme release kinetics and associated changes in protein structure and activity.
  • Measurement of kinetic parameters (specific activity, Michaelis-Menten constant) during enzyme release.

Main Results:

  • Recombinant beta-galactosidase inclusion bodies (IBβ-Gal) were confirmed as functional and highly active enzyme aggregates.
  • IBβ-Gal exhibited stability at physiological and acidic pH, and retained activity after high-temperature pre-incubation.
  • Enzyme release upon IBβ-Gal washing or dilution resulted in altered kinetic parameters and a shift towards soluble-like secondary structures.

Conclusions:

  • Recombinant beta-galactosidase inclusion bodies (IBβ-Gal) function as a packed reservoir of active and stable enzyme.
  • The release process from IBβ-Gal yields active enzyme with modified kinetic properties, distinct from the aggregated form.