Cometabolic degradation of veratryl alcohol and biphenyl by white rot fungus under nitrogen nutrition-rich condition

In this paper, changes of enzymes involved in the degradation of recalcitrant aromatic pollutants from white rot fungus Phlebia radiata I 5 6 and cometabolism of biphenyl and varatryl alcohol by this fungus under nitrogen nutrition rich were studied. Results from the experiment showed that C/N concentration ratio in the culture media played an important role on the activity of LiP. Under the condition of high concentration ratio of C/N or N/C, activity of LiP was higher, but higher activity of MnP only followed the low concentration of glucose or tartrate ammonium concentration in the media, when concentration of glucose or tartrate ammonium was more than 0 01 mol/L, the activity of MnP dropped down quickly. Veratryl alcohol increased the activity of LiP and MnP as well as the amount of ·OH radical free under different concentration of nitrogen or carbon source; ascorbic acid, a scavenger of ·OH radical free, brought the opposite effect to that of the veratryl alcohol on the LiP and MnP activity. Under nitrogen nutrition rich condition removal percentage of biphenyl was lower, however, under cometabolic condition of veratryl alcohol and biphenyl, the degradation was enhanced obviously, moreover, intermediate products accumulated in the media during the cometabolic degradation process of biphenyl and veratryl alcohol was different from these which was found in the process of separate degradation of biphenyl or veratryl alcohol.

Mycoparasitism of Nematode-Trapping Fungus Monacrosporium ellipsosporumand Its Biochemical Basis

Monacrosporium ellipsosporum, a nematode-trapping fungus, was isolated by baiting with sclerotiaof Sclerotinia sclerotiorum in soil from a tobacco field in Yuxi, Yunnan Province. Colonizationfrequency of the sclerotia by the fungus was 18% in natural soil. Reinoculation tests byplacing surface-sterilized sclerotia on fungal cultures for two weeks and then surface-sterilized again led to 32% sclerotia be infected. Dual culture tests in PDA plates did notgive rise to a suppression zone between the colonies of M. ellipsosporum and its counterpartfungi S. sclerotiorum and Rhizoctonia solani, suggesting there was little or no nutritionalcompetition and absent of antifungal compounds. However, M. ellipsosporum could grow overabsent of S. sclerotiorum and R. solani, and significantly inhibited their growth on agarplates. Scanning electron and light microscopic observations showed that hyphae of M. ellipsosporumgrew along and appressed on hypha of S. sclerotiorum and coiled around hyphae of R. solani.Assays of cell wall-degrading enzymes showed that M. ellipsosporum grew well in chitin agarmedia, with clear transparent hydrolysis zones. Activities of total chitinase, exo-chitinase,β-1, 3-glucanase and protease were 140.2±11.9, 82.9±4.1, 111.2±7.6 and 76.1±4.3 U respect-ively, after incubation for 4 days at 30 ℃ in liquid media containing ground sclerotia of S.sclerotiorum as sole nutrient source. These enzymes might be important in the mycoparasiticactivity of M. ellipsosporum.

Enzymatic Degradation of Organochlorine Insecticide Chlordane by Phlebia brevispora

[ Objective ] This study aimed to clarify the mechanism of enzymatic degradation of organochlorine insecticide chlordane by the white rot fungus Pldebia brevispora. [ Method ] The degradation characteristics of chlordane were determined by the crude enzyme extracted from P. brevispora strain by pure culture, ultrasonic fragmentation and centrifuge separation. [ Result] About 33.2% and 10.4% of chlordane were degraded respectively by intracellular enzyme and extracellular enzyme within 20 min. At pH 5.0 and 3℃, the crude enzyme showed the greatest degradation activity （49.9%）, with its Michaelis-Mentn＇s constant （Km ） and maximum degradation rate （ Vmax ） of 3.49 and 8.38 ttmol/min, respectively. [ Conclusion] Extracellular enzyme can degrade chlordane through dehydrogenation or dehydrochlorination. Intracellular enzyme plays a major role in chlordane degradation. It can transform chlordane to some hydroxylated metabolites through hydroxylation or substitution of chlorine atom by hydroxyl group.

Immobilization of an enzyme from a Fusarium fungus WZ-I for chlorpyrifos degradation

The free enzyme extracted from WZ-I, which was identified as Fusarium LK. ex Fx, could effectively degrade chlorpyrifos, an organophosphate insecticide. The methods of immobilizing this free enzyme and determined its degradation-related characteristics were investigated. The properties of the immobilized enzyme were compared with those of the free enzyme. The optimal immobilization of the enzyme was achieved in a solution of 30 g/L sodium alginate at 4℃ for 4-12 hr. The immobilized enzyme showed the maximal activity at pH 8.0, 45℃. The maximum initial rate and the substrate concentration of the immobilized enzyme were less than that of the free enzyme. The immobilized enzyme, therefore, had a higher capacity to withstand a broader range of temperatures and pH conditions than the free enzyme. With varying pH and temperatures, the immobilized enzyme was more active than the free enzyme in the degradation reaction. In addition, the immobilized enzyme exhibited only a slight loss in its initial activity, even after three repeated uses. The results showed that the immobilized enzyme was more resistant to different environmental conditions, suggesting that it was viable for future practical use.