Application and comparison in biosynthesis and biodegradation by Fusarium solani and Aspergillus fumigatus cutinases

Int J Biol Macromol. 2017 Nov;104(Pt A):1238-1245. doi: 10.1016/j.ijbiomac.2017.06.118. Epub 2017 Jun 30.

Abstract

In this study, two synthesized cutinase genes from Fusarium solani and Aspergillus fumigatus were expressed in Pichia pastoris X33. The characteristics of these two cutinases were investigated and compared. The results indicated that F. solani and A. fumigatus cutinases hydrolyzed p-nitrophenyl substrates with different carbon chain lengths. A. fumigatus cutinase predominately hydrolyzed p-nitrophenyl butyrate, but F. solani cutinase preferred p-nitrophenyl decanoate. The abilities of polymer synthesis and bioplastic degradation were tested and compared between F. solani and A. fumigatus cutinases. The results showed that F. solani cutinase had degradation ability on poly(ε-caprolactone) (PCL) and synthesized polymer with a molecular weight (MW) of 2300 in organic solvent. However, A. fumigatus cutinase completely degraded PCL and synthesized molecules with a MW of 25,000, suggesting that A. fumigatus cutinase has more promising applications.

Keywords: A. fumigatus; Biodegradation; Biosynthesis; Characterization; Cutinase; F. solani.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Aspergillus fumigatus / enzymology*
  • Aspergillus fumigatus / genetics
  • Biocatalysis
  • Carboxylic Ester Hydrolases / chemistry*
  • Carboxylic Ester Hydrolases / genetics
  • Carboxylic Ester Hydrolases / metabolism*
  • Cloning, Molecular
  • Enzyme Stability
  • Fusarium / enzymology*
  • Fusarium / genetics
  • Hydrogen-Ion Concentration
  • Models, Molecular
  • Polyesters / metabolism
  • Protein Structure, Secondary
  • Substrate Specificity
  • Temperature

Substances

  • Polyesters
  • Carboxylic Ester Hydrolases
  • cutinase