Lipase-mediated degradation of poly-ε-caprolactone in toluene: Behavior and its action mechanism

Lipase-catalyzed hydrolysis of poly(ɛ-caprolactone) (PCL) in toulene was investigated. PCL with number-average molecular weight (Mn) 10,000 g mol−1 was hydrolyzed using immobilized Candida antarctica lipase B (CALB). The increase in PCL concentration led to a decrease in degradation rate. Enhanced rate was observed when reaction temperature was increased from 30 to 50 °C. Enzymatic chain scission of PCL yielded cyclic dicaprolactone, tricaprolactone, tetracaprolactone and oligomers with Mn less than ∼1000 g mol−1. Catalytic formation of cyclic lactones via back-biting mechanism in low water content environment was attributed to CALB. Its hydrolysis of PCL displayed consecutive random- and chain-end scission with time from detailed thermal, molecular weight and structural analyses. Apparent activation energy, Ea for hydrolysis was 45 kJ mol−1 i.e. half of that reverse reaction. Dicaprolactone and oligomers from hydrolysis readily re-polymerized to produce mid-range polymer with Mn 1400 g mol−1 after 36 h in the same reaction medium.