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Enzymatic degradations of copolymers of L ‐lactide with cyclic carbonates
Author(s) -
Tsutsumi Chikara,
Nakagawa Katsuhiko,
Shirahama Hiroyuki,
Yasuda Hajime
Publication year - 2002
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/1616-5195(200206)2:5<223::aid-mabi223>3.0.co;2-d
Subject(s) - esterase , chemistry , copolymer , lipase , trimethylene carbonate , lactide , monomer , polymer chemistry , biodegradation , diphenyl carbonate , toluene , carbonate , biodegradable polymer , enzyme , lipoprotein lipase , polymer , stereochemistry , organic chemistry , transesterification , catalysis
Syntheses and biodegradation of random copolymers of L ‐lactide ( L ‐LA) with trimethylene carbonate (TMC), 1,1‐dimethyltrimethylene carbonate (1,1‐DTMC) and 2,2‐dimethyltrimethylene carbonate (2,2‐DTMC) were investigated at various monomer ratios using SmMe(C 5 Me 5 ) 2 THF as an initiator at 80 °C for 24 h in toluene. Enzymatic degradation of these polymers were performed using cholesterol esterase, lipoprotein lipase, and proteinase K. Poly(TMC) was effectively biodegraded by cholesterol esterase and lipoprotein lipase, while poly(2,2‐DTMC) and all the copolymers were hardly degraded using these enzymes. Biodegradations of poly( L ‐LA‐ co ‐TMC) (97:3) and poly( L ‐LA‐ co ‐2,2,DTMC) (95:5) show rapid degradations using TES buffer, a compost and proteinase K. The physical properties of these copolymers were also examined.Enzymatic degradation of L ‐LA/2,2‐DTMC copolymers by proteinase K in Tricine buffer (pH 8.0) at 37 °C: a 98:2, b 82:18, c 100:0, d 66:34, e 34:66, f 0:100.