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Related Experiment Videos

Extracellular poly(hydroxyalkanoate) depolymerases and their inhibitor from Pseudomonas lemoignei.

K Mukai1, K Yamada, Y Doi

  • 1Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Yokohama, Japan.

International Journal of Biological Macromolecules
|August 1, 1992
PubMed
Summary
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Microbial copolyesters like poly(3-hydroxybutyrate-co-4-hydroxybutyrate) and poly(3-hydroxybutyrate-co-3-hydroxyvalerate) degrade at different rates with specific enzymes. An inhibitory protein was identified that affects poly(3-hydroxybutyrate) depolymerase activity.

Area of Science:

  • Biochemistry
  • Microbiology
  • Polymer Science

Background:

  • Microbial copolyesters, including poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (P(3HB-co-3HV)) and poly(3-hydroxybutyrate-co-4-hydroxybutyrate) (P(3HB-co-4HB)), are biodegradable polymers.
  • Extracellular depolymerases, particularly those degrading poly(3-hydroxybutyrate) (P(3HB)), play a crucial role in their breakdown.
  • Understanding the enzymatic degradation pathways is essential for applications of these bioplastics.

Purpose of the Study:

  • To investigate the enzymatic degradation rates of P(3HB-co-3HV) and P(3HB-co-4HB) using purified poly(3-hydroxybutyrate) depolymerases.
  • To identify and characterize any inhibitory factors affecting P(3HB) depolymerase activity in microbial culture media.

Main Methods:

  • Enzymatic degradation was assessed by measuring the weight loss (erosion) of P(3HB-co-3HV) and P(3HB-co-4HB) films.

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  • Three extracellular depolymerases, two from Pseudomonas lemoignei and one from Alcaligenes faecalis T1, were used.
  • An inhibitory protein was isolated and its molecular weight determined using polyacrylamide gel electrophoresis (SDS-PAGE).

    • Main Results:

    • Degradation rates of the copolyesters by the three P(3HB) depolymerases followed a similar trend: P(3HB-co-4HB) > P(3HB) > P(3HB-co-3HV).
    • An inhibitory protein with a molecular weight of 35,000 Da was isolated from the succinate culture medium of P. lemoignei.
    • This inhibitor, a single polypeptide chain, likely binds reversibly to serine residues in the active site of P(3HB) depolymerase.
    • The inhibitory protein was not produced when P. lemoignei was grown solely on P(3HB).

    Conclusions:

    • The composition of microbial copolyesters significantly influences their enzymatic degradation rates by P(3HB) depolymerases.
    • P(3HB-co-4HB) is degraded more readily than P(3HB) and P(3HB-co-3HV).
    • A specific inhibitory protein in P. lemoignei culture medium can modulate P(3HB) depolymerase activity, suggesting a regulatory mechanism in polyester biodegradation.