Enzymatic hydrolysis of polyester: Degradation of poly(ε-caprolactone) by Candida antarctica lipase and Fusarium solani cutinase

• Published in: International journal of biological macromolecules 2020-02, Vol.144, p.183-189
• Main Authors: Shi, Ke, Jing, Jing, Song, Li, Su, Tingting, Wang, Zhanyong
• Format: Article
• Language: English
• Subjects: Biodegradation; Cutinase; Lipase; Poly(ε-caprolactone)
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2019.12.105

Poly(ε-caprolactone) (PCL) particles were melt-pressed into films using a hot press and then subjected to degradation by lipase from Candida antarctica and cutinase from Fusarium solani, respectively. The differences in weight loss, degradation modes, thermal stability, and crystallization were investigated after degradation by two kinds of enzymes. The result showed that mass loss of PCL films degraded by lipase was higher than that degraded by cutinase at the same enzyme concentrations. The degradation mode of PCL films is layered for cutinase degradation and penetrated for lipase degradation. Crystallinity of PCL had no obvious decrease after degradation by cutinase, but it markedly decreased after lipase-degradation. PCL films occurred one-step decomposition during heating and the cutinase-degraded products had similar thermal stability. Whereas the thermal stability of lipase-degraded PCL decreased significantly and the weight loss of the PCL occurred in several steps with increasing lipase hydrolysis time. •Effect of cutinase and lipase on the degradation of PCL were studied.•The thermal stability of lipase-degraded PCL decreased.•PCL is the optimal substrate for lipase between PBS and PCL.