title: Correlation between chemical and solid-state structures and enzymatic hydrolysis in novel biodegradable polyesters. The case of poly(propylene alkanedicarboxylate)s.
abstract: A series of seven fast-biodegrading aliphatic polyesters were prepared from 1,3-propanediol and aliphatic diacids with increasing number of methylene units (x). Melting points decreased from PPSu to PPAd and then increased again to PPAz and PPSeb. Crystallization rates and thermal stability increased steadily with increasing x. Glass transition temperatures decreased steadily to PPPim and subsequently increased. Enzymatic degradation of the polymers in the presence of a mixture of Rhizopus delemar and Pseudomonas cepacia lipases was much faster than that of poly(epsilon-caprolactone). All the polyester specimens were almost disintegrated within 36 h. PPSub exhibited the fastest enzymatic hydrolysis rates, PPAd and PPSuc the slowest.
authors.affiliation: Laboratory of Organic Chemical Technology, Chemistry Department, Aristotle University of Thessaloniki, 54124 Thessaloniki, Greece. dbic@chem.auth.gr
authors.forename: Dimitrios N
authors.initials: DN
authors.lastname: Bikiaris
authors.forename: George Z
authors.initials: GZ
authors.lastname: Papageorgiou
authors.forename: Dimitrios J
authors.initials: DJ
authors.lastname: Giliopoulos
authors.forename: Charalampos A
authors.initials: CA
authors.lastname: Stergiou
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D016956:Burkholderia cepacia / Q000201:enzymology*; D005656:Fungal Proteins / Q000737:chemistry*; D006868:Hydrolysis; D008049:Lipase / Q000737:chemistry*; D015394:Molecular Structure; D011091:Polyesters / Q000138:chemical synthesis / Q000737:chemistry*; D012233:Rhizopus / Q000201:enzymology*; D013329:Structure-Activity Relationship
chemical_list: D001426:Bacterial Proteins; D005656:Fungal Proteins; D011091:Polyesters; D008049:Lipase