Branched poly(lactide) synthesized by enzymatic polymerization: effects of molecular branches and stereochemistry on enzymatic degradation and alkaline hydrolysis.
In this article the effects of the number of molecular branches (chain ends) and the stereochemistry of poly(lactide)s (PLAs) on the enzymatic degradation and alkaline hydrolysis are studied. Various linear and branched PLAs were synthesized using lipase PS (Pseudomonas fluorescens)-catalyzed ring-opening polymerization (ROP) of lactide monomers having different stereochemistries (L-lactide, D-lactide, and D,L-lactide). Five different alcohols were used as initiators for the ROP, and the monomer-to-initiator molar feed ratio was varied from 10 to 100 and 1000 for each branch in the polymer architecture. The properties of branched PLAs that would affect the enzymatic and alkaline degradations, i.e., the glass transition temperature, the melting temperature, the melting enthalpy, and the advancing contact angle, were determined. The PLA films were degraded using proteinase K or 1.0 M NaOH solution, and the weight loss and changes in the number average molecular weight (Mn) of the polymer were studied during 12 h of degradation. The results suggest that an increase in the number of molecular branches of branched PLAs enhances its enzymatic degradability and alkali hydrolyzability. Moreover, the change in Mn of the branched poly(L-lactide) (PLLA) by alkaline hydrolysis indicated that the decrease in Mn was in the first place dependent on the number of molecular branches and thereafter on the length of the molecular branch of branched PLA. The branched PLLA, poly(D-lactide) (PDLA), and poly(D,L-lactide) (PDLLA) differed in weight loss and change in Mn of the PLA segment during the enzymatic degradation. It is suggested that the branched PDLLA was degraded preferentially by proteinase K.
Numata
Keiji
K
Department of Innovative and Engineered Materials, Tokyo Institute of Technology, 4259 Nagatsuta, Yokohama, Japan.
Srivastava
Rajiv K
RK
Finne-Wistrand
Anna
A
Albertsson
Ann-Christine
AC
Doi
Yoshiharu
Y
Abe
Hideki
H
D001672:Biocompatible Materials / Q000737:chemistry*; D019286:Endopeptidase K / Q000737:chemistry; D004798:Enzymes / Q000737:chemistry; D006868:Hydrolysis; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D008970:Molecular Weight; D009584:Nitrogen / Q000737:chemistry; D011091:Polyesters / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry*; D015202:Protein Engineering / Q000379:methods*; D011551:Pseudomonas fluorescens / Q000378:metabolism*; D013237:Stereoisomerism; D013696:Temperature; D013816:Thermodynamics
D001672:Biocompatible Materials; D004798:Enzymes; D011091:Polyesters; D011108:Polymers; C033616:poly(lactide); D019286:Endopeptidase K; D009584:Nitrogen