Inhibitory impact of the anticancer drug doxorubicin on anaerobic microbial community.

The inhibitory effect of the anticancer drug doxorubicin (DOX) on biogas production was evaluated in short-term and long-term exposure assays. The short-term assays reached the DOX IC50 value on 648 ± 50 µg·L-1. In addition, it was found that inhibition caused by the exposure of 10×103 µg·L-1 was reversible after removing DOX from the feeding synthetic medium. Furthermore, DOX can be rapidly sorbed by the biomass (despite the low Kow), which might contribute to the inhibitory effect. The results of long-term exposure assays, when the DOX volumetric loading rate was increased from 100 µgDOX·L-1·day-1 to 200 µgDOX·L-1·day-1, showed that biogas production and COD removal decreased rapidly. However, the methanogenic Archaeas could recover from this exposure, corroborating the results on short-term exposure assays. In conclusion, DOX can play a key role in inhibiting biological wastewater treatment processes if its concentration in hospital wastewater treatment plants increases abruptly.

Laccase as an efficacious approach to remove anticancer drugs: A study of doxorubicin degradation, kinetic parameters, and toxicity assessment.

The degradation of an anticancer drug by laccase was investigated for the first time, bringing a new approach to treat these hazardous substances through the direct enzymatic application. Degradations of doxorubicin by laccase were performed in different enzymatic concentrations, pH values and temperatures through kinetic studies. The highest enzymatic degradation of doxorubicin was achieved at pH 7 and 30 ºC, which resembles effluent characteristics from wastewater treatment plants. Assays were carried out in different doxorubicin concentrations to comprehend the enzymatic kinetics of degradation. Michaelis-Menten kinetic parameters obtained were maximum velocity obtained (Vmax) of 702.8 µgDOX h-1 L-1 and Michaelis-Menten constant (KM) of 4.05 µM, which showed a good affinity for the substrate. The toxicity was evaluated against L-929 cell line, and the degraded doxorubicin solution did not show a reduction in cell viability in the concentration of 250 µg L-1. In contrast, the doxorubicin shows a reduction of 27% in cell viability. Furthermore, in the highest tested concentration (1000 µg L-1), enzymatic degradation reduced in up 41.4% the toxicity of doxorubicin, which indicates laccase degrades doxorubicin to non-toxic compounds. In conclusion, this study provides a new application to laccase since the results showed great potential to remove anticancer drugs from effluents.

Potential of enzymatic process as an innovative technology to remove anticancer drugs in wastewater.

Anticancer drugs are a class of pharmaceutical compounds that have been found in hospital, domestic, and industrial wastewaters and also in surface waters. They have been showing recalcitrance to conventional wastewater treatment technologies and present a potential risk to environment and human health, since they exhibit cytotoxic, teratogenic, and carcinogenic among other effects in higher organisms, even at low concentrations. The presence of these compounds in the environment is a recent challenge for wastewater treatment and some alternative strategies to remove them were already studied, such as white-rot fungi (WRF) technologies. Despite promising results, processes involving fungi are complex, have high reaction times, and require nutrient addition for fungus growth and maintenance. Due to this potential, strategies to make the technology feasible were studied, such as the possibility for direct application of enzymes secreted by WRF. Enzymatic processes were studied in the removal of other pharmaceuticals such as antibiotics, anti-inflammatory, and steroid hormones; however, to the best of our knowledge, there is a gap on literature about their direct action on anticancer drugs.

Newly Isolated Penicillium sp. for Cellulolytic Enzyme Production in Soybean Hull Residue

Abstract (1) Background: The aim of this study was to evaluate the production and partial characterization of xylanase and avicelase by a newly isolated Penicillium sp. in solid-state fermentation, using soybean hulls as substrate. (2) Methods: Temperature, time, number of spores, and substrate moisture on xylanase and avicelase bioproduction were evaluated, maximizing activity with 30°C, 1x106 spores/g substrate, 14 and 7 days of fermentation with 70 and 76% substrate moisture contents, for xylanase and avicelase, respectively. (3) Results: Different solvents, temperatures, and agitation in the enzymatic extraction were evaluated, obtaining higher activities, 430.77 and 26.77 U/g for xylanase and avicelase using 30 min extraction and 0.05 M citrate buffer solution (pH 4.5 ), respectively at 60°C and 175 rpm and 50°C and 125 rpm. The optimum pH and temperature for enzymatic activity determination were 5.3 and 50°C. Enzyme extract stability was evaluated, obtaining higher stability with pH between 4.5 and 5.5, higher temperature of up to 40°C. The kinetic thermal denaturation (Kd), half-life time, D-value, and Z-value were similar for both enzymes. The xylanase Ed value (89.1 kJ/mol) was slightly lower than the avicelase one (96.7 kJ/mol), indicating higher thermostability for avicelase. (4) Conclusion: In this way, the production of cellulases using alternative substrates is a way to reduce production costs, since they represent about 10% of the world demand of enzymes, with application in animal feed processing, food production and breweries, textile processing, detergent and laundry production, pulp manufacturing and the production of biofuels.