A comparative analysis of mass losses of some aliphatic polyesters upon enzymatic degradation

Results of investigation of mass losses, geometrical surface structure changes and variations in crystallinity of poly(lactic acid) (PLA), poly(ɛ-caprolactone) (PCL) and commercially available material (PHB) consisting of poly(3,4-hydroxybutyrate) and poly(lactic acid) are presented. These structura...

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Veröffentlicht in:Polymer testing 2013-04, Vol.32 (2), p.209-214
Hauptverfasser: Żenkiewicz, Marian, Richert, Agnieszka, Malinowski, Rafał, Moraczewski, Krzysztof
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Sprache:eng
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Zusammenfassung:Results of investigation of mass losses, geometrical surface structure changes and variations in crystallinity of poly(lactic acid) (PLA), poly(ɛ-caprolactone) (PCL) and commercially available material (PHB) consisting of poly(3,4-hydroxybutyrate) and poly(lactic acid) are presented. These structural changes occurred due to degradation of these polymers in the presence of the following enzymes: proteinase K, protease, esterase or lipase. Independently of the enzyme type, the largest mass loss was found for PLA and the smallest for PHB. Thus, under the experimental conditions, the processes of enzymatic degradation proceeded most rapidly in PLA, more slowly in PCL, and the most slowly in PHB. It was also found that proteinase K caused the largest mass losses, protease caused smaller mass losses, and both esterase and lipase produced the least mass losses, while lipase did not bring about mass loss in PHB. Images of surfaces of individual samples, obtained by scanning electron microscopy (SEM), indirectly confirmed the results of the mass loss examination. Crystallinity of the studied polyesters increased with degradation in the presence of proteinase K and protease, while changes in the crystallinity due to esterase and lipase were not observed. The presented results illustrate well the relative susceptibilities of the individual polyesters toward degradation induced by various enzymes.
ISSN:0142-9418
1873-2348
DOI:10.1016/j.polymertesting.2012.10.011