18 shows little change between the unsaturated and the saturated melt transitions

suggesting that the aromatic side chains may play a large role in the crystallization of the

polymer. The polymer is predominantly influenced by the phenyl interactions and has

nearly the same melt if the backbone were saturated or not. The leucinol polymer (16)

was not characterized due to difficulty finding a sample that would remain intact

throughout the heating and cooling cycle.

 The hydrogenated polymers (13-18) were subjected to degradation by four enzymes

and two control solutions. The results were gathered after four and one half days of

constant shaking at 37 C and pH 7.2. These conditions were chosen to simulate

biological conditions, human blood has a pH of 7.4 and the human body temperature is

98.6 F (37 C). The enzymes chosen had peak reactivity between pH 6.0 and pH 7.0, so

a buffer closer to pH 7.0 was used rather than a buffer at pH 7.4. The overall percent

weight loss of the degraded polymers was intended as a means of quantifying the results

of the degradation under these various conditions. The final calculations for the percent

weight loss of the polymers proved inconclusive. The obvious degradation of some of

the polymers by the corresponding enzymes was encouraging. Initially, there had been

concern about the water solubility of the alcohol-carboxylic acid byproduct of the

proposed ester bond cleavage degradation pathway.

 The alaninol polymer (13) was readily degradable in both control solutions and all

but one (Lipase from Rhizopus Arrhizus) of the enzyme solutions. The 1HNMR spectra

for the by-products revealed the elimination of the ester peaks at 6 2.1 and the appearance

of H-bonded alcohol peaks at 6 1.6 2.0. These spectra confirmed the degradation of the

polymers via the proposed mechanism based on ester cleavage in the polymer backbone.