Polyesters from Macrolactones Using Commercial Lipase NS 88011 and Novozym 435 as Biocatalysts

Appl Biochem Biotechnol. 2018 Feb;184(2):659-672. doi: 10.1007/s12010-017-2583-4. Epub 2017 Aug 23.

Abstract

The demand for environmentally friendly products allied with the depletion of natural resources has increased the search for sustainable materials in chemical and pharmaceutical industries. Polyesters are among the most widely used biodegradable polymers in biomedical applications. In this work, aliphatic polyesters (from globalide and ω-pentadecalactone) were synthesized using a new commercial biocatalyst, the low-cost immobilized NS 88011 lipase (lipase B from Candida antarctica immobilized on a hydrophobic support). Results were compared with those obtained under the same conditions using a traditional, but more expensive, commercial biocatalyst, Novozym 435 (lipase B from C. antarctica immobilized on Lewatit VP OC). When NS 88011 was used in the polymerization of globalide, longer reaction times (240 min)-when compared to Novozym 435-were required to obtain high yields (80-90 wt%). However, higher molecular weights were achieved. When poly(ω-pentadecalactone) was synthesized, high yields and molecular weights (130,000 g mol-1) were obtained and the enzyme concentration showed strong influence on the polyester properties. This is the first report describing NS 88011 in polymer synthesis. The use of this cheaper enzymatic preparation can provide an alternative for polyester synthesis via enzymatic ring-opening polymerization.

Keywords: Enzyme-catalyzed polymerization; NS 88011; Novozym 435; Poly(globalide); Poly(ω-pentadecalactone).

MeSH terms

  • Catalysis
  • Enzymes, Immobilized / chemistry*
  • Fungal Proteins / chemistry*
  • Lipase / chemistry*
  • Polyesters* / chemical synthesis
  • Polyesters* / chemistry

Substances

  • Enzymes, Immobilized
  • Fungal Proteins
  • Polyesters
  • Novozyme 435
  • Lipase
  • lipase B, Candida antarctica