Enzymatic Degradation of Alaninol Polymer (14)

 A 10.1 mg film was placed in buffered aqueous solution (1.0 mL, 0.02 M). A 8.9

mg film was placed in the pH 11.0 aqueous solution (1.0 mL). A 6.8 mg film was placed

in a solution containing 70,000 units of the lipase from Rhizopus Arrhizus (dissolved in

0.2 mL de-ionized water), 0.6 mL de-ionized water and 0.2 mL (0.1 M) phosphate buffer.

A 8.4 mg film was placed in a solution containing 11,000 units of ao-chymotrypsin

(dissolved in 0.2 mL de-ionized water), 0.6 mL de-ionized water and 0.2 mL (0.1 M)

phosphate buffer. A 5.3 mg film was placed in a solution containing 235,000 units of

Trypsin (dissolved in 0.2 mL de-ionized water), 0.6 mL de-ionized water and 0.2 mL

(0.1 M) phosphate buffer. A 8.8 mg film was placed in a solution containing 500 units of

papain (dissolved in 0.2 mL de-ionized water), 0.6 mL de-ionized water and 0.2 mL (0.1

M) phosphate buffer. The solutions were shaken and incubated for approximately 100

hours. The resulting solutions were filtered on a Kontes apparatus using a 0.45 micron

Teflon filter. The resultant film and residue were dried in a vacuum oven at 50 C until a

constant weight was reached. Each film was visually inspected for evidence of

degradation. Filter paper residue 1H NMR (300 MHz, CDC13, ppm): 6 0.7-1.4 (m,

32H), 1.39-2.02 (m, 4H), 2.22-2.39 (t, 2H), 3.60-3.68 (d, 2H), 8.09-8.12 (s, 1H). The

1HNMR of the rotary evaporated filtrates revealed no degradation by products only

phosphate buffer.

Enzymatic Degradation of Valinol Polymer (15)

 A 15.6 mg film was placed in buffered aqueous solution (1.0 mL, 0.02 M). A 7.1

mg film was placed in the pH 11.0 aqueous solution (1.0 mL). A 7.0 mg film was placed

in a solution containing 70,000 units of the lipase from Rhizopus Arrhizus (dissolved in