Lipase-catalyzed ring-opening polymerization of 16-hexadecanolide

Enzymatic ring-opening polymerization of a 17-membered lactone, 16-hexadecanolide (HDL), was performed in bulk by using lipases of different origin as catalyst. Pseudomonas fluorescens lipase exhibited high catalytic activity toward the polymerization, producing the corresponding polymer in high yields. A higher polymerization temperature (75 degrees C) resulted in the formation of the polymer with molecular weight of more than 5x10(3). HDL monomer was recovered unchanged in the polymerization without the enzyme. Michaelis-Menten kinetics of lactones in five different ring size showed that HDL had the largest enzymatic polymerizability among the lactones examined.