Enzyme-embedded polymer
degradation was reported to be an attractive
alternative approach to the conventional surface pouring method for
efficient degradation of polymers using fungal-derived enzyme
Candida antarctica
lipase B. Despite the enormous
potential, this approach is still in its infancy. In the present study,
a probiotic lipase obtained from
Lactobacillus plantarum
has been employed for the first time to study the enzyme-embedded
polymer degradation approach using poly(ε-caprolactone) (PCL)
as the semicrystalline polymer candidate. PCL films embedded with
2 to 8 wt % lipase are studied under static conditions for their enzymatic
degradation up to 8 days of incubation. Thermogravimetric analyses
(TGA) have shown a clear trend in decreasing thermal stability of
the polymer with increasing lipase content and number of incubation
days. Differential thermal analyses have revealed that the percentage
crystallinity of the leftover PCL films increases with progress in
enzymatic degradation because of the efficient action of lipase over
the amorphous regions of the films. Thus, the higher lipase loading
in the PCL matrix and more number of incubation days have resulted
in higher percentage crystallinity in the leftover PCL films, which
has further been corroborated by X-ray diffraction analyses. In a
similar line, higher percentage mass loss of the PCL films has been
observed with increased enzyme loading and number of incubation days.
Field emission scanning electron microscopy (FE-SEM) has been employed
to follow the surface and cross-sectional morphologies of the polymer
films, which has revealed micron-scale pores on the surface as well
as a bulk polymer matrix with progress in enzymatic polymer degradation.
Additionally, FE-SEM studies have revealed the efficient enzyme-catalyzed
hydrolysis of the polymer matrix in a three-dimensional fashion, which
is unique to this approach. In addition to the first-time utility
of a probiotic lipase for the embedded polymer degradation approach,
the present work provides insight into the PCL degradation under static
and ambient temperature conditions with no replenishment of enzymes.