Hydroxylation of polypropylene using the monooxygenase mutant 139-3 from Bacillus megaterium BM3

Abstract

Enzymatic hydroxylation of polypropylene (PP) was investigated in order to increase hydrophilicity. A mutant (139-3) of the P450monooxygenase from Bacillus megaterium expressed in E. coli DH5α was purified using anion exchange chromatography. Hydroxylation of PP fabrics led to a dramatic increase of hydrophilicity as indicated by a water drop dissipation time of below 1 s compared to the hydrophobic reference material. Likewise, a 4.9 cm increase of rising height was measured which remained consistent after 144 h of storage. Similarly, enzymatic hydroxylation of PP films lead to a decrease of the WCA from 104.6° to 77.3° with no major change after exposure to air for 6 days. Using X-ray photoelectron spectroscopy, an increase in normalized atomic concentrations of oxygen from 1.40 to 4.98% for the CO-inhibited and enzyme treated sample, respectively, was measured confirming enzymatic hydroxylation.