Md. Castillo et al., Degradation of the herbicide bentazon as related to enzyme production by Phanerochaete chrysosporium in two solid substrate fermentation systems, WORLD J MIC, 16(3), 2000, pp. 289-295
Enzyme production and degradation of the herbicide bentazon by Phanerochaet
e chrysosporium growing on straw (solid substrate fermentation, SSF) and th
e effect of nitrogen and the hydraulic retention time (HRT) were studied us
ing a small bioreactor and batch cultures. The best degradation of bentazon
was obtained in the low nitrogen treatments, indicating participation of t
he ligninolytic system of the fungus. The treatments that degraded bentazon
also had manganese peroxidase (MnP) activity, which seemed to be necessary
for degradation. Pure MnP (with Mn(II) and H2O2) did not oxidize bentazon.
However, in the presence of MnP, Mn(II) and Tween 80, bentazon was slowly
oxidized in a H2O2-independent reaction. Bentazon was a substrate of pure l
ignin peroxidase (LiP) and was oxidized significantly faster (22,000-29,000
times) as compared to the MnP-Tween 80 system. Although LiP was a better e
nzyme for bentazon oxidation in vitro, its role in the SSF systems remains
unclear since it was detected only in treatments with high nitrogen and hig
h HRT where no degradation of bentazon occurred. Inhibition of LiP activity
may be due to phenols and extractives present in the straw.