Enzymatic hydrolysis of poly(ethylene furanoate)

J Biotechnol. 2016 Oct 10:235:47-53. doi: 10.1016/j.jbiotec.2016.02.006. Epub 2016 Feb 17.

Abstract

The urgency of producing new environmentally-friendly polyesters strongly enhanced the development of bio-based poly(ethylene furanoate) (PEF) as an alternative to plastics like poly(ethylene terephthalate) (PET) for applications that include food packaging, personal and home care containers and thermoforming equipment. In this study, PEF powders of various molecular weights (6, 10 and 40kDa) were synthetized and their susceptibility to enzymatic hydrolysis was investigated for the first time. According to LC/TOF-MS analysis, cutinase 1 from Thermobifida cellulosilytica liberated both 2,5-furandicarboxylic acid and oligomers of up to DP4. The enzyme preferentially hydrolyzed PEF with higher molecular weights but was active on all tested substrates. Mild enzymatic hydrolysis of PEF has a potential both for surface functionalization and monomers recycling.

Keywords: Biocatalyst; Enzymatic functionalization; Enzymatic hydrolysis; Poly(ethylene furanoate) (PEF); Polyester recycling; Thermobifida cellulosilytica cutinase 1 (Thc_Cut1).

Publication types

  • Review

MeSH terms

  • Actinobacteria / enzymology
  • Bacterial Proteins / metabolism
  • Carboxylic Ester Hydrolases / metabolism*
  • Dicarboxylic Acids / chemistry
  • Dicarboxylic Acids / metabolism
  • Furans* / chemistry
  • Furans* / metabolism
  • Hydrolysis
  • Polyethylenes* / chemistry
  • Polyethylenes* / metabolism

Substances

  • Bacterial Proteins
  • Dicarboxylic Acids
  • Furans
  • Polyethylenes
  • 2,5-furandicarboxylic acid
  • Carboxylic Ester Hydrolases
  • cutinase
  • furan