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Fusarium polycaprolactone depolymerase is cutinase

C A Murphy1, J A Cameron, S J Huang

  • 1Department of Molecular and Cell Biology, University of Connecticut, Storrs 06269-3044, USA.

Applied and Environmental Microbiology
|February 1, 1996
PubMed
Summary
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Fusarium cutinase, an enzyme that degrades plant cuticles, also breaks down the synthetic polymer polycaprolactone (PCL). This study shows cutinase is responsible for PCL degradation by phytopathogenic fungi.

Area of Science:

  • Microbiology
  • Biochemistry
  • Polymer Science

Background:

  • Polycaprolactone (PCL) is a synthetic polyester biodegradable by various microorganisms.
  • Phytopathogens often secrete cutinase, a hydrolase enzyme targeting plant cuticle polymers.

Purpose of the Study:

  • To investigate if Fusarium cutinase functions as a polycaprolactone (PCL) depolymerase.
  • To elucidate the role of cutinase in the microbial degradation of PCL.

Main Methods:

  • Comparative analysis of wild-type and cutinase-negative mutant strains of Fusarium species.
  • Growth experiments using PCL, cutin, and PCL hydrolysates as carbon sources.
  • Assays for PCL depolymerase activity and cutinase esterase activity.

Main Results:

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  • Wild-type Fusarium strains degraded PCL and utilized it for growth, unlike the cutinase-negative mutant.
  • Cutinase expression and activity were induced by cutin and PCL oligomers in wild-type strains.
  • PCL depolymerase activity correlated directly with cutinase activity.

Conclusions:

  • Fusarium cutinase is confirmed as the primary enzyme responsible for polycaprolactone (PCL) depolymerization.
  • Cutinase plays a crucial role in the degradation and assimilation of PCL by phytopathogenic fungi.