title: Enzymatic hydrolysis of poly(lactide)s: effects of molecular weight, L-lactide content, and enantiomeric and diastereoisomeric polymer blending.
abstract: Nonblended poly(L-lactide) (PLLA) films having different molecular weights and nonblended poly(lactide) (PLA) films, enantiomeric blend films from PLLA and poly(D-lactide) (PDLA), and diastereoisomeric blend films of poly(DL-lactide) (PDLLA) with either PLLA or PDLA, having different L-lactide (LLA) contents (X(LLA)s) in the range of 0-0.99, were amorphous made by melt-quenching. The effects of molecular weight, X(LLA), and average L- and D-lactyl unit sequence length (l(L) and l(D), respectively) on the enzymatic hydrolysis of the films were investigated in the presence of proteinase K. The enzymatic hydrolysis rate (R(EH)) of PLLA estimated by gravimetry increased monotonically with the inverse of number-average molecular weight (M(n)). The extrapolation of R(EH) of PLLA to M(n)(-1) = 0, where no exo-chain-scission takes place, gave a positive R(EH) value (1.75 microg/(mm(2).h)), meaning that the enzymatic hydrolysis of PLLA proceeds via both endo- and exo-chain-scission. The R(EH) of the nonblended films as well as the enantiomeric and diastereoisomeric blend films decreased monotonically with the decease in X(LLA) and finally became zero for X(LLA) below 0.3. The R(EH) values of the blend films of PLLA and PDLLA with PDLA (l(D) = infinity) were lower than expected, while the R(EH) values of the blend films of PLLA with PDLLA (l(D) = 4) agreed completely with the expected values. These results reveal that the nonblended PLA films are enzymatically hydrolyzable when X(LLA) and l(L) are higher than 0.3 and 3, respectively, and l(D) is lower than 10 and that the presence of long D-lactyl unit sequences (l(D) > 4) as in PDLA hinders the enzymatic hydrolysis of long L-lactyl unit sequences even when long D- and L-lactyl unit sequences are present in the different molecules.
authors.affiliation: Department of Ecological Engineering, Faculty of Engineering, Toyohashi University of Technology, Tempaku-cho, Toyohashi, Aichi 441-8580, Japan. tsuji@eco.tut.ac.jp
authors.forename: H
authors.initials: H
authors.lastname: Tsuji
authors.forename: S
authors.initials: S
authors.lastname: Miyauchi
mesh_terms: D001672:Biocompatible Materials / Q000737:chemistry*; D002152:Calorimetry, Differential Scanning; D002384:Catalysis; D002850:Chromatography, Gel; D019286:Endopeptidase K / Q000378:metabolism*; D006868:Hydrolysis; D008970:Molecular Weight; D011091:Polyesters / Q000737:chemistry*; D013237:Stereoisomerism
chemical_list: D001672:Biocompatible Materials; D011091:Polyesters; C033616:poly(lactide); D019286:Endopeptidase K