Lipase-catalysed preferential cleavage of synthetic aliphatic copolyesters investigated by HPLC/ESI-MS

Synthetic high molar mass poly(butylenesuccinate-co-butylenesebacate), P(BS-co-BSe), and poly(butylenesuccinate-co-butyleneadipate), P(BS-co-BA), with different composition, were subjected to enzymatic hydrolysis by Lipase from M. miehei or from R. arrhizus. The enzymatic hydrolysis of P(BS-co-BSe)s and P(BS-co-BA)s films produced a mixture of water-soluble monomers and co-oligomers that were separated and identified by on-line High Performance Liquid Chromatography/ElectroSpray Ionization Mass Spectrometry. The results show that these enzymes prefer cleaving sebacic ester bonds in P(BS-co-BSe) copolymers, whereas succinic ester bonds appear to be hydrolyzed faster than adipic ester bonds in P(BS-co-BA) copolyesters.