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Using titrimetric method, enzymatic behavior of lipase AK against fullerene end-capped polycaprolactone (C 60 -PCL) was studied for the first time, compared with polycaprolactone (PCL). The results showed that degradation of both C 60 -PCL and PCL by lipase followed Mechaelis-Menten equation, with the degradation parameters of PCL and C 60 -PCL were 0.75 mg mL -1 and 0.16 mg mL -1 for K m , and 0.90 mL h -1 and 0.43 mL h -1 for V max , respectively. C 60 -PCL had a slower degradation rate than PCL under the same conditions. These data indicated that the introduction of fullerene enabled PCL hard to be degraded by lipase. fullerene end-capped polycaprolactone, polycaprolactone, lipase AK, titrimetry Citation: Peng Q Y, Kang F, Li J, et al. Degradation of a fullerene end-capped polycaprolactone by lipase AK.

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An aqueous nanoparticle suspension of a bis-methanophosphonate fullerene (n-BMPF) was tested to clarify its effects on polymerase chain reaction (PCR) with the catalyst of Taq DNA polymerase and DNA exonuclease Exo Ⅲ and the template of super-coiled plasmid pEGFP-N1. It was found that the product amounts from PCR decreased significantly with addition of the n-BMPF. The inhibition by the n-BMPF was dose-dependent and IC50 values for reactions of PCR were 2.7 μmol/L. Increase of Taq DNA polymerase amounts in PCR system antagonized the activities of the n-BMPF. However, addition of two scavengers of reactive oxygen species (ROS), mannitol and azide at the concentrations of 2~10 mmol/L did not antagonize the activities of the n-BMPF against PCR. These data implied that this inhibition probably did not correlate to ROS. Meanwhile, the inhibition for the DNA exonuclease Exo Ⅲ by the n-BMPF was evident and dose-dependent.