Biochar loaded with ferrihydrite and Bacillus pseudomycoides enhances remediation of co-existed Cd(II) and As(III) in solution.

Bioremediation is one of the effective ways for heavy metal remediation. Iron-modified biochar (F@BC) loaded with Bacillus pseudomycoides (BF@BC) was synthesized to remove the coexistence of cadmium (Cd) and arsenic (As) in solutions. The results showed that B. pseudomycoides significantly increased the removal rate of Cd(II) by enhancing the specific surface area and Si-containing functional groups of biochar (BC). The surface of F@BC was enriched with Fe-containing functional groups, significantly improving As(III) adsorption. The combination of ferrihydrite and strains on BF@BC enhanced the removal of Cd(II) and As(III). It also promoted the oxidation of As(III) by producing an abundance of hydroxyl radicals (·OH). The maximum saturated adsorption capacity of BF@BC for Cd(II) and As(III) increased by 52.47% and 2.99 folds compared with BC, respectively. This study suggests that biochar loaded with Fe and bacteria could be sustainable for the remediation of the coexistence of Cd(II) and As(III) in solutions.

Characterization of Agarolytic Pathway in a Terrestrial Bacterium Cohnella sp. LGH.

Previously, we have reported that an endo-type ß-agarase AgaW was responsible for the hydrolysis of agarose into the major product neoagarotetraose in a terrestrial agar-degrading bacterium Cohnella sp. LGH. Here, we identify and characterize the following depolymerization pathway in strain LGH through the genomic and enzymatic analysis. In the pathway, neoagarotetraose was depolymerized by a novel α-neoagarooligosaccharide (NAOS) hydrolase CL5012 into 3,6-anhydro-α-L-galactose (L-AHG) and agarotriose; Agarotriose was further depolymerized by a novel agarolytic ß-galactosidase CL4994 into D-galactose and neoagarobiose; Neoagarobiose was finally depolymerized by CL5012 into L-AHG and D-galactose. Although α-agarase has not been identified in strain LGH, the combined action of CL5012 and CL4994 unexpectedly plays a critical role in the depolymerization of agarotetraose, one theoretical product of α-agarase hydrolysis of agarose. In this pathway, agarotetraose was depolymerized by CL4994 into D-galactose and neoagarotriose; Neoagarotriose was then depolymerized by CL5012 into L-AHG and agarobiose. Furthermore, another novel endo-type ß-agarase CL5055 was identified as an isozyme of AgaW with different pH preference in the hydrolysis of agarose into α-NAOSs. Strain LGH seemed to lack a common exo-type ß-agarase responsible for the direct depolymerization of agarose or neoagarooligosaccharide into neoagarobiose. These results highlight the diversity of agarolytic manner in bacteria and provide a novel insight on the diversity of agarolytic pathways.