Identification and comparison of cutinases for synthetic polyester degradation

Peter James Baker, Christopher Poultney, Zhiqiang Liu, Richard Gross, Jin Kim Montclare

Research output: Contribution to journalArticlepeer-review


Cutinases have been exploited for a broad range of reactions, from hydrolysis of soluble and insoluble esters to polymer synthesis. To further expand the biotechnological applications of cutinases for synthetic polyester degradation, we perform a comparative activity and stability analysis of five cutinases from Alternaria brassicicola (AbC), Aspergillus fumigatus (AfC), Aspergillus oryzae (AoC), Humicola insolens (HiC), and the well-characterized Fusarium solani (FsC). Of the cutinases, HiC demonstrated enhanced poly(ε-caprolactone) hydrolysis at high temperatures and under all pH values, followed by AoC and AfC. Both AbC and FsC are least stable and function poorly at high temperatures as well as at acidic pH conditions. Surface charge calculations and phylogenetic analysis reveal two important modes of cutinase stabilization: (1) an overall neutral surface charge within the "crowning area" by the active site and (2) additional disulfide bond formation. These studies provide insights useful for reengineering such enzymes with improved function and stability for a wide range of biotransformations.

Original languageEnglish (US)
Pages (from-to)229-240
Number of pages12
JournalApplied Microbiology and Biotechnology
Issue number1
StatePublished - Jan 2012


  • Cutinase
  • Hydrolysis
  • Polymer degradation
  • Residual activity
  • Thermostability
  • pH stability

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology


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