The industrial versatility of Gluconobacter oxydans: current applications and future perspectives.

Gluconobacter oxydans is a well-known acetic acid bacterium that has long been applied in the biotechnological industry. Its extraordinary capacity to oxidize a variety of sugars, polyols, and alcohols into acids, aldehydes, and ketones is advantageous for the production of valuable compounds. Relevant G. oxydans industrial applications are in the manufacture of L-ascorbic acid (vitamin C), miglitol, gluconic acid and its derivatives, and dihydroxyacetone. Increasing efforts on improving these processes have been made in the last few years, especially by applying metabolic engineering. Thereby, a series of genes have been targeted to construct powerful recombinant strains to be used in optimized fermentation. Furthermore, low-cost feedstocks, mostly agro-industrial wastes or byproducts, have been investigated, to reduce processing costs and improve the sustainability of G. oxydans bioprocess. Nonetheless, further research is required mainly to make these raw materials feasible at the industrial scale. The current shortage of suitable genetic tools for metabolic engineering modifications in G. oxydans is another challenge to be overcome. This paper aims to give an overview of the most relevant industrial G. oxydans processes and the current strategies developed for their improvement.

Decolorization and detoxification of different azo dyes by Phanerochaete chrysosporium ME-446 under submerged fermentation.

Azo dyes are widely used in the textile industry due to their resistance to light, moisture, and oxidants. They are also an important class of environmental contaminant because of the amount of dye that reaches natural water resources and because they can be toxic, mutagenic, and carcinogenic. Different technologies are used for the decolorization of wastewater containing dyes; among them, the biological processes are the most promising environmentally. The aim of this study was to evaluate the potential of Phanerochaete chrysosporium strain ME-446 to safely decolorize three azo dyes: Direct Yellow 27 (DY27), Reactive Black 5 (RB5), and Reactive Red 120 (RR120). Decolorization efficiency was determined by ultraviolet-visible spectrophotometry and the phytotoxicity of the solutions before and after the fungal treatment was analyzed using Lactuca sativa seeds. P. chrysosporium ME-446 was highly efficient in decolorizing DY27, RB5, and RR120 at 50 mg L-1, decreasing their colors by 82%, 89%, and 94% within 10 days. Removal of dyes was achieved through adsorption on the fungal mycelium as well as biodegradation, inferred by the changes in the dyes' spectral peaks. The intensive decolorization of DY27 and RB5 corresponded to a decrease in phytotoxicity. However, phytotoxicity increased during the removal of color for the dye RR120. The ecotoxicity tests showed that the absence of color does not necessarily translate to an absence of toxicity.

Streptomyces misionensis PESB-25 produces a thermoacidophilic endoglucanase using sugarcane bagasse and corn steep liquor as the sole organic substrates.

Streptomyces misionensis strain PESB-25 was screened and selected for its ability to secrete cellulases. Cells were grown in a liquid medium containing sugarcane bagasse (SCB) as carbon source and corn steep liquor (CSL) as nitrogen source, whose concentrations were optimized using response surface methodology (RSM). A peak of endoglucanase accumulation (1.01 U · mL(-1)) was observed in a medium with SCB 1.0% (w/v) and CSL 1.2% (w/v) within three days of cultivation. S. misionensis PESB-25 endoglucanase activity was thermoacidophilic with optimum pH and temperature range of 3.0 to 3.6 and 62° to 70 °C, respectively. In these conditions, values of 1.54 U mL(-1) of endoglucanase activity were observed. Moreover, Mn(2+) was demonstrated to have a hyperactivating effect on the enzyme. In the presence of MnSO4 (8 mM), the enzyme activity increased threefold, up to 4.34 U · mL(-1). Mn(2+) also improved endoglucanase stability as the catalyst retained almost full activity upon incubation at 50 °C for 4 h, while in the absence of Mn(2+), enzyme activity decreased by 50% in this same period. Three protein bands with endoglucanase activity and apparent molecular masses of 12, 48.5 and 119.5 kDa were detected by zymogram.

Production and partial characterization of cellulases and Xylanases from Trichoderma atroviride 676 using lignocellulosic residual biomass.

Trichoderma atroviride 676 was studied to evaluate its efficiency in the production of some lignocellulolytic enzymes, using lignocellulosic residual biomass. Best results were obtained when 3.0 % (w/v) untreated sugarcane bagasse was used (61.3 U mL(-1) for xylanase, 1.9 U mL(-1) for endoglucanase, 0.25 U mL(-1) for FPase, and 0.17 U mL(-1) for ß-glucosidase) after 3-4 days fermentation. The maximal enzymatic activity for endoglucanase, FPase, and xylanase were observed at 50-60 °C and pH 4.0-5.0, whereas thermal stability at 50 °C (CMCase and FPase) or 40 °C (xylanase) was obtained after 8 h. Zymograms have shown two bands of 104 and 200 kDa for endoglucanases and three bands for xylanase (23, 36, and 55.7 kDa). The results obtained with T. atroviride strain 676 were comparable to those obtained with the cellulolytic strain Trichoderma reesei RUT-C30, indicating, in the studied conditions, its great potential for biotechnological application, especially lignocellulose biomass hydrolysis.

Production and Partial Characterization of Cellulases from Trichoderma sp. IS-05 Isolated from Sandy Coastal Plains of Northeast Brazil.

This study evaluated the production of cellulolytic enzymes by Trichoderma sp. IS-05 strain, isolated from sand dunes, according to its ability to grow on cellulose as carbon source. Wheat bran was tested as the carbon source and peptone tested as the nitrogen source. Different concentrations of carbon and nitrogen were tested using a factorial design to identify optimal cellulase activity production. The results showed that media containing wheat bran 4.0% (w/v) and peptone 0.25% (w/v) lead to the highest production, 564.0 U L(-1) of cellulase, obtained after 2 days of fermentation. The pH and temperature profile showed optimal activity at pH 3.0 and 60°C. As for thermostability, the cellulase was most tolerant at 60°C, retaining more than 59.6% of maximal activity even after 4 hours of incubation. The combination of acid pH, high temperature tolerance, and production of cellulase from agro-industrial residues by Trichoderma sp. IS-05 offers possibilities condition for the biomass hydrolysis process to produce bioethanol.

Brewer's spent grain and corn steep liquor as alternative culture medium substrates for proteinase production by Streptomyces malaysiensis AMT-3.

Brewer's spent grain and corn steep liquor or yeast extract were used as the sole organic forms for proteinase production by Streptomyces malaysiensis in submerged fermentation. The influence of the C and N concentrations, as well as the incubation periods, were assessed. Eight proteolytic bands were detected through gelatin-gel-electrophoresis in the various extracts obtained from the different media and after different incubation periods, with apparent molecular masses of 20, 35, 43, 50, 70, 100, 116 and 212 kDa. The results obtained suggest an opportunity for exploring this alternative strategy for proteinases production by actinomycetes, using BSG and CSL as economically feasible substrates.