Novel ring-opening polymerization of lactide by lipase

Shuichi Matsumura, Kimihiro Mabuchi, Kazunobu Toshima

Research output: Contribution to journalArticle

44 Citations (Scopus)

Abstract

Six-membered D,L-, L,L- and D,D-lactides were polymerized by lipase over a temperature range of 80 to 130°C to yield the polylactide with a molecular weight (MW) of greater than 270000. Among the lipases tested, lipase PS gave the greatest molecular weight of polylactide. The polymerization of D,L-lactide by lipase was better than that of L,L- and D,D-lactides. The polymerization of lactide by lipase showed the characteristic features, such as induction period for the initiation of polymerization, formation of oligomer and subsequent formation of high molecular weight polylactide, which may imply the characteristic polymerization by lipase. Immobilization of lipase on celite significantly enhanced the polymerization of lactide particularly with respect to the low concentration of the enzyme and the MW of the resultant polymer. It was found that there is no clear relationship between enzymatic polymerizability and enzymatic degradability with respect to the enzyme origin and the stereochemistry of lactide.

Original languageEnglish
Pages (from-to)285-304
Number of pages20
JournalMacromolecular Symposia
Volume130
DOIs
Publication statusPublished - 1998 Apr

ASJC Scopus subject areas

  • Condensed Matter Physics
  • Organic Chemistry
  • Polymers and Plastics
  • Materials Chemistry

Fingerprint Dive into the research topics of 'Novel ring-opening polymerization of lactide by lipase'. Together they form a unique fingerprint.

Cite this