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Novel ring‐opening polymerization of lactide by lipase
Author(s) -
Matsumura Shuichi,
Mabuchi Kimihiro,
Toshima Kazunobu
Publication year - 1998
Publication title -
macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 1022-1360
DOI - 10.1002/masy.19981300125
Subject(s) - polymerization , lipase , lactide , ring opening polymerization , polymer chemistry , polymer , oligomer , chemistry , molar mass distribution , materials science , enzyme , organic chemistry
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 ( M w ) 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 M w 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.