Branched poly(lactide) synthesized by enzymatic polymerization: effects of molecular branches and stereochernistry on enzymatic degradation and alkaline hydrolysis
2007 (English)In: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 8, no 10, 3115-3125 p.Article in journal (Refereed) Published
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 (M-n) 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 M-n of the branched poly(L-lactide) (PLLA) by alkaline hydrolysis indicated that the decrease in M-n 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 M-n of the PLA segment during the enzymatic degradation. It is suggested that the branched PDLLA was degraded preferentially by proteinase K.
Place, publisher, year, edition, pages
2007. Vol. 8, no 10, 3115-3125 p.
ring-opening polymerization, stannous octoate, organic media, proteinase-k, polylactide, lactide, weight, stereocopolymers, stereochemistry, crystallinity
IdentifiersURN: urn:nbn:se:kth:diva-17020DOI: 10.1021/bm700537xISI: 000250009900020ScopusID: 2-s2.0-35548976692OAI: oai:DiVA.org:kth-17020DiVA: diva2:335063
QC 201008182010-08-052010-08-052010-08-18Bibliographically approved