Hydrolytic and enzymatic incubation of polyhydroxyoctanoate (PHO): a short-term in vitro study of a degradable...

The present study examined the degradation behaviour of poly(beta-hydroxy octanoate) (PHO), a bacterial poly(beta-hydroxy alkanoate), following incubation under hydrolytic or enzymatic conditions in vitro. Solution-cast PHO films were incubated in a citrate buffer solution with and without acid phosphatase and in an acetate buffer with and without beta-glucuronidase for periods ranging from 7 to 60 days. The physical characterization of the PHO films was analyzed by SEM and tensile strength studies. In addition, various analytical methods were used to detect modifications in the chemical and morphological structure of the PHO, namely, ESCA, FTIR, DSC, X-ray diffraction, and SEC. The results indicate that the enzymatic conditions selected in the present study induced no significant surface morphological or chemical modifications, and no significant weight loss was observed after 60 days of incubation. However, as revealed by weight average molecular weight Mw and number average molecular weight Mn decreases, changes in the bulk structure of the PHO were observed with acid phosphatase at 28 and 60 days, in contrast to smaller Mw and Mn decreases recorded in both the buffers and the beta-glucuronidase. The tensile properties had decreased following incubation, yet showed no difference under all of the selected conditions. With no weight loss or surface changes, the PHO films incubated in acid phosphatase showed only a chemical hydrolytic process characterized by Mw and Mn decreases with time of incubation. The present study demonstrated that the degradation of PHO films is one of slow, chemical hydrolysis only, perhaps requiring several months of incubation. The hydrophobic nature of the long alkyl pendent chain in PHO may be responsible for this slow process. The inability of enzymes to degrade PHO may be attributed to the latter's poor adsorption capacity, due to its hydrophobic nature, and to a lack of specificity in the catalytic activity of these enzymes.