Purification and Properties of Extracellular Poly(3-hydroxybutyrate) Depolymerase Produced by <Emphasis Type="Italic">Aspergillus fumigatus</Emphasis> 202

An extracellular poly(3-hydroxybutyrate) (PHB) depolymerase produced by a thermotolerant fungal soil isolate, Aspergillus fumigatus 202, was purified and characterized. Maximum PHB depolymerase production was obtained at the end of 48 h with initial medium pH 7.0 and 45 °C in Bushnell Haas Minerals medium containing PHB as sole source of carbon. The PHB depolymerase was purified using size exclusion chromatography to a fold purification of 20.62 and 61.62% yield. SDS-PAGE and isoelectric focusing revealed the molecular weight and pI of the purified enzyme as 63,744 Da and 4.2, respectively. N-terminal amino acid sequence of purified enzyme was HAXDAYLVK. This non-glycosylated enzyme was most active at pH 9.0 and 45 °C. Purified enzyme was inactivated by N-bromosuccinimide and dithiothreitol suggesting the involvement of tryptophan residues and disulfide bonds at its active site. Nonionic detergents like Tween 20, Tween 80 and Triton X-100 inhibited the enzyme activity. Ions like Ca⁺² and Mg⁺² (5 mM) increased the enzyme activity 1.5 times. Fe⁺² effectively inhibited the enzyme activity to 88% whereas Hg⁺² completely inhibited the enzyme.     

Properties of a Poly(3-hydroxybutyrate) Depolymerase from Penicillium funiculosum

A poly(3-hydroxybutyrate) (PHB) depolymerase was purified from a fungus, Penicillium funiculosum (IFO6345), with phenyl-Toyopearl and its properties were compared with those of other PHB depolymerases. The molecular mass of the purified enzyme was estimated at about 33 kDa by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The pH optimum and pI were 6.5 and 6.5, respectively. The purified protein showed affinity to Con A-Sepharose, indicating that it is a glycoprotein. Diisopropylfluorophosphate and dithiothreitol inhibited the depolymerase activity completely. The N-terminal amino acid sequence of the purified enzyme was TALPAFNVNPNSVSVSGLSSGGYMAAQL, which contained a lipase box sequence. This purified enzyme is one of the extracellular PHB depolymerase which belong to serine esterase. The purified enzyme showed relatively strong hydrolytic activity against 3-hydroxybutyrate oligomers compared with its PHB-degrading activity. PHB-binding experiments showed that P. funiculosum depolymerase has the weakest affinity for PHB of all the depolymerases examined.     

Biodegradation of Poly(3-hydroxybutyrate-co-3-hydroxyvalerate) by a Tropical Marine Bacterium, Pseudoalteromonas sp. NRRL B-30083

Pseudoalteromonas sp. NRRL B-30083 was isolated as the predominant PHBV-degrading organism from a tropical marine environment. In complex medium, the isolate grew well at temperatures between 23°C and 33°C, with an optimal doubling time of about 30 min. NaCl was required at concentrations between 0.2 N and 0.8 N. Optimal pH levels for growth were between pH 6.5 and pH 8.5. Liquid cultures grew modestly on PHBV as a sole carbon source under optimal conditions, although PHBV depolymerase activity was not detected.     

Gene Cloning and Characterization of a Poly(<Emphasis Type="SmallCaps">l</Emphasis>-Lactic Acid) Depolymerase from <Emphasis Type="Italic">Pseudomonas</Emphasis> sp. Strain DS04-T

A gene encoding a poly(l-lactic acid) (PLA) depolymerase from Pseudomonas sp. strain DS04-T was cloned and overexpressed in Escherichia coli. The recombinant PLA depolymerase with a molecular weight of 19.2 kDa was purified to homogeneity. The optimum pH and temperature of the PLA depolymerase are 8.5 and 60 °C, respectively. K⁺, Ca²⁺ and Ni²⁺ enhance the enzyme activity, while Na⁺, Zn²⁺, Mg²⁺, Cu²⁺, Fe²⁺, Mn²⁺ and Co²⁺ inhibit it. The inhibition of different chemicals on the PLA depolymerase activity were examined, in which EDTA was found to have a significantly inhibitory effect. The main degradation product of the depolymerase is identified as lactic acid monomer by mass spectrometric analysis. Physicochemical properties, substrate specificity and sequence analysis indicated that PME is a new type of PLA depolymerase.     

Purification and Properties of a Poly (β-hydroxybutyrate) Depolymerase From Penicillium sp.

An extracellular poly (β-hydroxybutyrate) (PHB) depolymerase was purified from a Penicillium sp. DS9701-09a by centrifugation, ultrafiltration, precipitation and gel filtration chromatography. The specific activity of the purified enzyme was 37.9-folds higher than that of the culture supernatant and the recovery yield was 11.8%. The PHB deploymerase molecular mass was 44.8 kDa from analysis of both Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Matrix-assisted laser desorption-time-of-flight (MALDI-TOF) mass spectrometer. The isoelectric point of 6.7 for the enzyme was determined by a two-dimensional electrophoresis. The optimum enzyme activity was observed at a temperature of 50 °C and pH 5.0. The apparent K _m of the enzyme was found to be 1.35 mg/mL. The PHB depolymerase consisted of 16 kinds of normal amino acids. The secondary structure of the enzyme was determined by CD spectrum. α-helix and β-turn were found to be 66% and 34% for the enzyme without ammonium sulphite. Chemical inhibition on the PHB depolymerase activity was examined and EDTA was found to have a significantly inhibitory effect.     

Characterization of a poly(3-hydroxybutyrate) depolymerase fromaureobacterium saperdae: Active site and kinetics of hydrolysis studies

An extracellular poly(3-hydroxybutyrate) (PHB) depolymerase was purified fromAureobacterium saperdae cultural medium by using hydrophobic interaction chromatography. The isolated enzyme was composed of a single polypeptide chain with a molecular mass of 42.7 kDa as determined by SDS-PAGE and by native gel filtration on TSK-HW-55S. The enzyme was not a glycoprotein. Its optimum activity occurred at pH 8.0 and it showed a broad pH stability, ranging from pH 3 to pH 11.N-Bromosuccinamide and 2-hydroxy-5-nitrobenzyl bromide completely inactivated the enzyme, suggesting the involvement of tryptophan residues at the active site of the protein. The enzyme was very sensitive to diisopropyl fluorophosphate and diazo-dl-norleucine methyl ester, showing the importance of serine and carboxyl groups. The modification of cysteine residues byp-hydroxy mercuricbenzoate did not cause a loss of activity, whereas dithiothreitol rapidly inactivated the enzyme, revealing the presence of disulfide bonds.A saperdae depolymerase acted on the surface layer of PHB films and the degradation proceeded by surface erosion releasing monomers and dimers of 3-hydroxybutric acid. The degradation of PHB films byA. saperdae depolymerase was partially inhibited in the presence of excess amounts of enzyme. This phenomenon, already observed by Mukaiet al. with poly(hydroxyalkanoates) depolymerases fromAlcaligenes faecalis, Pseudomonas pickettii, andComamonas testosteroni, was analyzed according to the kinetic model proposed by these authors. The experimental data evidenced a general agreement with the kinetic model, although higher initial degradation rates were found withA. saperdae depolymerase.     

Biochemical and Genetic Characterization of an Extracellular Poly(3-Hydroxybutyrate) Depolymerase from Acidovorax Sp. Strain TP4

To determine the properties of enzymes from bacteria that degrade polypropiolactone (PPL), we isolated 13 PPL-degrading bacteria from pond water, river water, and soil. Nine of these strains were identified as Acidovorax sp., three as Variovorax paradoxus, and one as Sphingomonas paucimobilis. All the isolates also degraded poly(3-hydroxybutyrate) (PHB). A PPL-degrading enzyme was purified to electrophoretical homogeneity from one of these bacteria, designated Acidovorax sp. TP4. The purified enzyme also degraded PHB. The molecular weight of the enzyme was estimated as about 50,000. The enzyme activity was inhibited by diisopropylfluorophosphate, dithiothreitol, and Triton X-100. The structural gene of the depolymerase was cloned in Escherichia coli. The nucleotide sequence of the cloned DNA fragment contained an open reading frame (1476 bp) specifying a protein with a deduced molecular weight of 50,961 (491 amino acids). The deduced overall sequence was very similar to that of a PHB depolymerase of Comamonas acidovorans YM1609. From these results it was concluded that the isolated PPL-degrading enzyme belongs to the class of PHB depolymerases. A conserved amino acid sequence, Gly-X₁-Ser-X₂-Gly (lipase box), was found at the N-terminal side of the amino acid sequence. Site-directed mutagenesis of the TP4 enzyme confirmed that ²⁰Ser in the lipase box was essential for the enzyme activity. This is the first report of the isolation a PHB depolymerase from Acidovorax.     

An Original Halo-Alkaline Protease from <Emphasis Type="Italic">Bacillus halodurans</Emphasis> Strain US193: Biochemical Characterization and Potential Use as Bio-Additive in Detergents

Over a hundred of halophilic/halotolerant microorganisms were screened for alkaline protease production. The bacterium showing the highest enzyme production was characterized and identified as Bacillus halodurans US193 on the basis of 16S rRNA gene analysis. It was alkalophilic, thermophilic and halotolerant since it grew optimally at pH 9.7 and 50?°C with tolerance of up to 125 g NaCl l^?1. The alkaline protease was purified 4.9 times with about 40186.1 U/mg as specific activity. It exhibited optimal activity at pH 10, 70?°C and 0.25 M NaCl with perfect stability at wide ranges of pH (6–12), temperatures (30–60?°C) and NaCl concentrations (0–2 M). The serine alkaline protease maintained high stability in the presence of Cu²⁺, Mg²⁺, Ba²⁺ and Ca²⁺ ions, various organic solvents [50% (v/v)] and ionic and non ionic detergent additives. In addition, it was more compatible with various commercialized detergents than other reported detergent proteases, and was very efficient in blood stain removal. These findings let B. halodurans US193 alkaline protease be an ideal candidate for many industrial processes at harsh conditions, especially as a bio-additive in detergent industry.     

Degradation of poly(3-hydroxybutyrate), PHB,by bacteria and purification of a novel PHB depolymerase fromComamonas sp.

Bacteria capable of growing on poly(3-hydroxybutyrate), PHB, as the sole source of carbon and energy were isolated from various soils, lake water, activated sludge, and air. Although all bacteria utilized a wide variety of monomeric substrates for growth, most of the strains were restricted to degrade PHB and copolymers of 3-hydroxybutyrate and 3-hydroxyvalerate, P(3HB-co-3HV). Five strains were also able to decompose a homopolymer of 3-hydroxyvalerate, PHV. Poly(3-hydroxyoctanoate), PHO, was not degraded by any of the isolates. One strain, which was identified asComamonas sp., was selected, and the extracellular depolymerase of this strain was purified from the medium by ammonium sulfate precipitation and by chromatography on DEAE-Sephacel and Butyl-Sepharose 4B. The purified PHB depolymerase was not a glycoprotein. The relative molecular masses of the native enzyme and of the subunits were 45,000 or 44,000, respectively. The purified enzyme hydrolyzed PHB, P(3HB-co-3HV), and—at a very low rate—also PHV. Polyhydroxyalkanoates, PHA, with six or more carbon atoms per monomer or characteristic substrates for lipases were not hydrolyzed. In contrast to the PHB depolymerases ofPseudomonas lemoignei andAlcaligenes faecalis T₁, which are sensitive toward phenylmethylsulfonyl fluoride (PMSF) and which hydrolyze PHB mainly to the dimeric and trimeric esters of 3-hydroxybutyrate, the depolymerase ofComamonas sp. was insensitive toward PMSF and hydrolyzed PHB to monomeric 3-hydroxybutyrate indicating a different mechanism of PHB hydrolysis. Furthermore, the pH optimum of the reaction catalyzed by the depolymerase ofComamonas sp. was in the alkaline range at 9.4.     

Biosorptive removal of Pb(II) and Cu(II) from wastewater using activated carbon from cassava peels

The ability of activated carbon from cassava peels to remove heavy metals like Cu(II) and Pb(II) from hospital wastewater was investigated. The study showed that a pH of 8 was the best for the sorption of both metal ions onto the biosorbent. The time-dependent experiments for the metal ions showed that the binding of the metal ions to the biomass was rapid and occurred within 20–120 min. Sorption efficiency increased with a rise in adsorbent dosage. It increased from 12 to 73 % for Pb(II) and 26 to 79 % for Cu(II) when the adsorbent dose increased from 2 to 12 g. An increase in temperature led to an increase in sorption for both metal ions. The Langmuir model showed that the biomass has a higher sorption capacity for Cu(II) than Pb(II), with q _m = 5.80 mg g^?1 for Pb(II) and 8.00 mg g^?1 for Cu(II). The Freundlich isotherm K _f was 1.4 for Pb(II) and 1.8 for Cu(II), indicating a preferential sorption of Cu(II) onto the biosorbent. Adsorption capacity was found to decrease with an increase in particle sizes. Sorption occurred by physical mechanisms and was mainly controlled by intraparticle diffusion.     

Purification and characterization of extracellular poly(3-hydroxybutyrate) depolymerases

Five extracellular PHB depolymerases of bacteria isolated from various sources were purified to electrophoretic homogeneity and compared with known extracellular PHB depolymerase fromAlcaligenes faecalis T1. The molecular mass of these enzymes were all around 40–50 kDa. Nonionic detergent, diisopropylfluorophosphate and dithiothreitol inhibited the PHB depolymerase activity of all these enzymes. Trypsin abolished PHB depolymerase activity, but not theD-3-hydroxybutyric acid dimer hydrolase activity of all the enzymes. These results showed that the basic properties of these PHB depolymerases resemble those of theA. faecalis T1 enzyme. Analysis ofN-terminal amino acid sequence of the purified enzymes revealed that these enzymes includingA. faecalis T1 enzyme fall into three groups.     

Optimization of Poly(<Emphasis Type="SmallCaps">dl</Emphasis>-Lactic Acid) Degradation and Evaluation of Biological Re-polymerization

Poly(dl-lactic acid) or PLA is a biodegradable polymer. It has received much attention since it plays an important role in resolving the global warming problem. The protease produced by Actinomadura keratinilytica strain T16-1 was previously reported as having PLA depolymerase potential and being applicable to PLA biodegradation, which was used in this work. Therefore, this research demonstrates the important basic knowledge on the biological degradation process by the crude PLA-degrading enzyme from strain T16-1. Its re-polymerization was evaluated. The optimization of PLA degradation by statistical methods based on central composite design was determined. Approximately 6700 mg/l PLA powder was degraded by the crude enzyme under optimized conditions: an initial enzyme activity of 200 U/ml, incubated at 60 °C for 24 h released 6843 mg/l lactic acid with 82% conversion, which was similar to the commercial enzyme proteinase K (81%). The degradable products were re-polymerized repeatedly by using commercial lipase as a catalyst under a nitrogen atmosphere for 6 h. A PLA oligomer was achieved with a molecular weight of 378 Da (n = 5). This is the first report to demonstrate the high efficiency of the enzyme to degrade 100% of PLA powder and to show the biological recycling process of PLA, which is promising for the treatment and utilization of biodegradable plastic wastes in the future.     

Biosynthesis and Characterization of Poly-(3-hydroxybutyrate-co-3-hydroxyvalerate) from Bacillus cereus S10

The biodegradable and biocompatible copolymer poly-(3-hydroxybutyrate-co-5 mol% 3-hydroxyvalerate), poly-(3HB-co-5 mol% 3HV), was synthesized by Bacillus cereus S10 and the highest yield was determined as 69.91 % at pH 7 and 30 °C after 48 h of incubation using a glucose as the sole carbon source. Poly-(3HB-co-5 mol% 3HV) was purified from bacterial biomass using chloroform. FTIR analysis showed absorption bands at 1,723, 1,274, 1,373, 1,453, 2,932 cm^?1 corresponding to C=O, C–O stretching, CH₃, –CH₂ and –CH groups, respectively. ¹H-NMR and ¹³C-NMR analysis confirmed that the copolymer was composed of 95 mol% of 3-hydroxybutrate and 5 mol% of 3-HV monomeric units. Poly-(3-HB-co-5 mol% 3HV) was used for nanoparticles preparation. The diameter of nanoparticles was 202 nm.     

The Influence of Artificial Photodegradation on Properties of Poly(3-hydroxybutyrate-<Emphasis Type="Italic">co</Emphasis>-3-hydroxyvalerate)(PHBV)/Graphite Nanosheets (GNS) Nanocomposites

The potential use of poly(3-hydroxybutyrate-co-3-hydroxyvalerate)/graphite nanosheets (GNS) as a biodegradable nanocomposite has been explored. PHBV/GNS nanocomposites films were prepared by solution casting at various concentrations of GNS—0.25, 0.50 and 1.00 wt% GNS. The films were exposed to artificial ultraviolet radiation (UV) during 52 h. The effect of GNS on PHBV photodegradation was investigated and compared to neat PHBV film. The artificial photodegradation induced changes in physical (weight loss), chemical carbonyl index by Fourier transform infrared spectroscopy, thermal degree of crystallinity and melting temperature by differential scanning calorimetry and morphological scanning electron microscopy characteristics. Based on the results obtained from aforementioned analyzes it was verified that GNS inhibits the oxidative degradation of PHBV matrix.     

The Effect of Chain Extender on Poly(3-hydroxybutyrate-co-3-hydroxyvalerate): Thermal Degradation,Crystallization, and Rheological Behaviours

Poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (PHBV), a semi-polycrystalline biopolymer from the polyhydroxyalkanonate family has in recent years become a commercial bioplastic with mechanical properties comparable to isotactic polypropylene and enhanced O₂, CO₂ and H₂O barrier properties. However, its brittleness and sensitivity to thermal and hydrolysis degradations restrict its applications. To overcome the problems associated with degradation during processing blending of PHBV and an epoxy-functionalized chain extender (Joncryl^® ADR-4368 S) was conducted in a twin screw extruder. The effect of concentration of the chain extender on thermal, crystallization and rheological behaviours of PHBV was investigated. Thermal gravimetric analysis results indicated improvement in the resistance to thermal decomposition of PHBV by introducing the chain extender. This was accompanied with calculation of thermal degradation activation energy (E_a) using the Flyn–Walls–Ozawa method which confirmed increase of E_a with the increase in content of the chain extender. The rheological behaviour and crystallization of modified PHBV was characterized by rotational rheometry and differential scanning calorimetry techniques, respectively. The results show that addition of chain extender enhanced viscosity of PHBV and also reduce the rate of crystallization.     

Blending Modification of PHBV/PCL and its Biodegradation by <Emphasis Type="Italic">Pseudomonas mendocina</Emphasis>

Poly(3-hydroxybutyrate-co-hydroxyvalerate) (PHBV) is a biodegradable polymer synthesized in microorganisms. The application of PHBV is limited by certain material disadvantages. Poly(ε-caprolactone) (PCL) possesses excellent thermodynamic and mechanical properties and was used to modify PHBV in the presence of triethyl citrate (TEC) and dicumyl peroxide (DCP), which was used as plasticizer and grafting agent, respectively. The effects of PCL and additive agents on the mechanical, thermal, amphipathic and degradability behaviors of the blends were investigated. The results showed that the mechanical properties of the PHBV blends improved by PCL incorporation and improved even further after TEC and DCP addition. The addition of DCP could not induce an increase in crystallization temperature but improved the crystallization degree of the blends. The presence of hydrophilic groups in TEC leads to an apparent increases in the hydrophilicity of the PHBV blends. A PHBV/PCL blend (40/60) with TEC (20 wt.%) and DCP (0.5 wt.%) was chosen for its good mechanical properties and hydrophilicity. The chosen ratio of the blends was also shown a preferable degradation activity by biodegradation assay using Pseudomonas mendocina. The addition of TEC and DCP has no conspicuous negative effect on the biodegradation.     

Cobalt separation from waste mobile phone batteries using selective precipitation and chelating resin

Separation of cobalt from mixed-waste mobile phone batteries containing LiCoO₂ cathodic active material was investigated using selective precipitation and chelating resin. Cobalt was recovered from the active powder materials containing 47 % Co oxide together with Mn, Cu, Li, Al, Fe, and Ni oxides. The metal ions were leached sufficiently using 4 M HCl. The metal ions detected spectrophotometrically were removed from the leaching solution by selective precipitation at pH 5.5, with cobalt loss of 27.5 %. Conditions for achieving a recovery of Co in the filtrate by chelating resin were determined experimentally by varying the pH and time of the reaction, as well as the initial resin-to-liquid ratio. The cobalt was efficiently determined by absorption spectrometry at λ _max 510 nm. Chelating polyamidoxime resin was synthesized by polymerization of acrylonitrile and followed by amidoximation reaction. Physically cross-linked gel of polyacrylonitrile was made by a cooling technique.     

Synthesis,Characterization and Environmental Applications of a New Bio-Composite Gelatin-Zr(IV) Phosphate

Gelatin-Zr(IV) phosphate composite (GT/ZPC) was synthesized by sol–gel method. Different techniques viz. Fourier transform infrared spectroscopy (FTIR), thermogravimetric analysis (TGA), X-ray powdered diffraction (XRD), scanning electron microscopy (SEM) and transmission electron microscopy (TEM) were used for the characterisation of GT/ZPC composite ion exchanger. The ion exchange capacity (IEC) of GT/ZPC was observed to be better (1.04 meq g^?1) than its inorganic counterpart (0.64 meq g^?1). The pH studies revealed the monofunctional nature of GT/ZPC with one inflection point. The distribution studies showed that the GT/ZPC was highly selective for Cd²⁺ as compare to other metal ions. The environmental applicability of ion exchanger has been analysed for binary separations of metal ions using column method. Cd²⁺ was effectively removed from synthetic mixture of metal ions (Zn²⁺, Pb²⁺, Ni²⁺, Co²⁺ and Cu²⁺).     

Purification of Aspergillus fumigatus (Pdf1) Poly(β-hydroxybutyrate) (PHB) Depolymerase Using a New, Single-Step Substrate Affinity Chromatography Method: Characterization of the PHB Depolymerase Exhibiting Novel Self-Aggregation Behavior

The extracellular poly(-hydroxybutyrate) (PHB) depolymerase of Aspergillus fumigatus Pdf1 was purified by a new, simple, one-step affinity chromatography method using the substrate PHB. The purified enzyme was glycosylated, with the molecular mass of 40 KD, and exhibited a novel self-aggregation behavior by means of hydrophobic interaction that was resolved by Triton X-100 (TX-100) pretreatment of enzyme and also TX-100 incorporation in the native gel. The apparent K _m value of purified enzyme for PHB was 119 g/mL and 3-hydroxybutyrate was detected as the main endproduct of PHB hydrolysis. The depolymerase was insensitive to phenylmethyl sulfonyl fluoride (PMSF), sodium azide, ethylenediaminetetraacetic acid (EDTA), and para-chloromercuric benzoic acid (PCMB), but was inactivated by dithioerythritol (DTT) and showed specificity for short chain-length poly(-hydroxyalkanoates) (PHAs) such as PHB, poly(hydroxyvalerate) (PHV), and copolymers of 3-hydroxybutyrate (3HB) and 3-hydroxyvalerate (3HV). Medium-chain-length PHA failed to get hydrolyzed. The enzyme, however, exhibited strong cross reactivity with the Comamonas sp. PHB depolymerase antibodies, but not with PHV depolymerase antibodies of Pseudomonas lemoignei. Southern hybridization and dot blot analysis of A. fumigatus Pdf1 genomic DNA with alkaline phosphatase labeled probes of P. lemoignei PHB and PHV depolymerase genes revealed no homology, although the enzyme hydrolyzed both PHB and PHV.     

Arsenic Removal from Dilute Solutions by High Surface Area Mesoporous Iron Oxyhydroxide

Mesostructured iron oxyhydroxide (FeO _x ) and iron oxyhydroxide–phosphate (FeO _x P) composites were organized using dodecylsulfate surfactant as a template. X-ray diffraction studies depicted a lamellar structure of the product. Ion exchange and solvent extraction methods were employed for the removal of the surfactant. Carboxylate ions exchanged lamellar type mesostructured material reorganized to a wormhole-like mesoporous material when heated under N₂ atmosphere. Surfactant was completely removed by carboxylate ions as observed by the Fourier transform infrared spectra. High surface area acetate-exchanged FeO _x (230 m² g^?1) was obtained after the surfactant removal from the composite (2.8 m² g^?1). Surface area of acetate-exchanged FeO _x P was the highest (240 m²g^?1) after the removal of the surfactant. Local structure of iron species of FeO _x was investigated by X-ray absorption fine structure spectroscopy. Further, Fe···Fe bond appeared at 3.21–3.25 Å with coordination number 2–3, showing a high degree of un-saturation of Fe···Fe bonds. As compared with bulk iron oxyhydroxide and iron-intercalated montmorillonite, the mesoporous iron materials were highly effective for arsenic removal from low concentrations of aqueous solutions. Furthermore, mesoporous iron materials were stable in aqueous phase.