Biochemical characterization and biocatalytic application of a novel d-tagatose 3-epimerase from Sinorhizobium sp.

Sinorhizobium sp. d-tagatose 3-epimerase (sDTE) catalyzes the conversion of d-tagatose to d-sorbose. It also recognizes d-fructose as a substrate for d-allulose production. The optimal temperature and pH of the purified sDTE was 50 °C and 8.0, respectively. Based on the sDTE homologous model, Glu154, Asp187, Gln213, and Glu248, form a hydrogen bond network with the active-site Mn²⁺ and constitute the catalytic tetrad. The amino acid residues around O-1, -2, and -3 atoms of the substrates (d-tagatose/d-fructose) are strictly conserved and thus likely regulate the catalytic reaction. However, the residues at O-4, -5, and -6, being responsible for the substrate-binding, are different. In particular, Arg65 and Met9 were found to form a unique interaction with O-4 of d-fructose and d-tagatose. The whole cells with recombinant sDTE showed a higher bioconversion rate of 42.5% in a fed-batch bioconversion using d-fructose as a substrate, corresponding to a production of 476 g L⁻¹d-allulose. These results suggest that sDTE is a potential industrial biocatalyst for the production of d-allulose in fed-batch mode.

Sinorhizobium sp. d-tagatose 3-epimerase (sDTE) catalyzes the conversion of d-tagatose to d-sorbose.     

Biocatalytic kinetic resolution of d,l-pantolactone by using a novel recombinant d-lactonase

d-Pantolactone is a key chiral intermediate for the synthesis of d-pantothenic acid and its derivatives. Biocatalytic kinetic resolution of d,l-pantoyl lactone using d-lactonase is an efficient route to synthesize d-pantolactone. In this study, we report the expression of a novel d-lactonase TSDL in Escherichia coli host. The recombinant TSDL exhibited high hydrolysis activity and enantioselectivity toward d-pantolactone. The reaction conditions of the recombinant TSDL-catalyzed kinetic resolution of d,l-pantolactone was systematically investigated by whole cell biocatalysis. In addition, a preparative-scale reaction for bioproduction of d-pantoic acid was examined under optimized reaction conditions. This study presented an alternative enzymatic process for kinetic resolution of d,l-pantolactone.

d-Pantolactone is a key chiral intermediate for the synthesis of d-pantothenic acid and its derivatives.     

Highly selective synthesis of d-amino acids from readily available l-amino acids by a one-pot biocatalytic stereoinversion cascade

d-Amino acids are key intermediates required for the synthesis of important pharmaceuticals. However, establishing a universal enzymatic method for the general synthesis of d-amino acids from cheap and readily available precursors with few by-products is challenging. In this study, we constructed and optimized a cascade enzymatic route involving l-amino acid deaminase and d-amino acid dehydrogenase for the biocatalytic stereoinversions of l-amino acids into d-amino acids. Using l-phenylalanine (l-Phe) as a model substrate, this artificial biocatalytic cascade stereoinversion route first deaminates l-Phe to phenylpyruvic acid (PPA) through catalysis involving recombinant Escherichia coli cells that express l-amino acid deaminase from Proteus mirabilis (PmLAAD), followed by stereoselective reductive amination with recombinant meso-diaminopimelate dehydrogenase from Symbiobacterium thermophilum (StDAPDH) to produce d-phenylalanine (d-Phe). By incorporating a formate dehydrogenase-based NADPH-recycling system, d-Phe was obtained in quantitative yield with an enantiomeric excess greater than 99%. In addition, the cascade reaction system was also used to stereoinvert a variety of aromatic and aliphatic l-amino acids to the corresponding d-amino acids by combining the PmLAAD whole-cell biocatalyst with the StDAPDH variant. Hence, this method represents a concise and efficient route for the asymmetric synthesis of d-amino acids from the corresponding l-amino acids.

An efficient one-pot biocatalytic cascade was developed for synthesis of d-amino acids from readily available l-amino acids via stereoinversion.     

Synthesis and stereocomplex formation of enantiomeric alternating copolymers with two types of chiral centers,poly(lactic acid-alt-2-hydroxybutanoic acid)s

Stereocomplex (SC) formation was reported for the first time for enantiomeric alternating copolymers consisting of repeating units with two types of chiral centers, poly(lactic acid-alt-2-hydroxybutanoic acid)s [P(LA-alt-2HB)s]. l,l-Configured poly(l-lactic acid-alt-l-2-hydroxybutanoic acid) [P(LLA-alt-l-2HB)] and d,d-configured poly(d-lactic acid-alt-d-2-hydroxybutanoic acid) [P(DLA-alt-d-2HB)] were amorphous. Blends of P(LLA-alt-l-2HB) and P(DLA-alt-d-2HB) were crystallizable and showed typical SC-type wide-angle X-ray diffraction profiles similar to those reported for stereocomplexed blends of poly(l-lactic acid) and poly(d-lactic acid) homopolymers and of poly(l-2-hydroxybutanoic acid) and poly(d-2-hydroxybutanoic acid) homopolymers, and of l,l-configured poly(l-lactic acid-co-l-2-hydroxybutanoic acid) [P(LLA-co-l-2HB)] and d,d-configured poly(d-lactic acid-co-d-2-hydroxybutanoic acid) [P(DLA-co-d-2HB)] random copolymers. The melting temperature values and melting enthalpy values at 100% crystallinity for stereocomplexed solvent-evaporated and precipitated P(LLA-alt-l-2HB)/P(DLA-alt-d-2HB) blends were correspondingly 187.5 and 187.9 °C, and 98.1 and 91.8 J g⁻¹. Enantiomeric polymer blending of P(LLA-alt-l-2HB) and P(DLA-alt-d-2HB) can confer crystallizability by stereocomplexation and the biodegradable materials with a wide variety of physical properties and biodegradability are highly expected to be prepared by synthesis of alternating copolymers of various combinations of two types of chiral α-substituted 2-hydroxyalkanoic acid monomers and their SC crystallization.

Stereocomplex formation was reported for alternating copolymers of chiral α-substituted 2-hydroxyalkanoic acids which can be utilized for preparation of biodegradable materials with a variety of physical properties and biodegradability.     

Computational study on the polymerization reaction of d-aminopeptidase for the synthesis of d-peptides

Almost all natural proteins are composed exclusively of l-amino acids, and this chirality influences their properties, functions, and selectivity. Proteases can recognize proteins composed of l-amino acids but display lower selectivity for their stereoisomers, d-amino acids. Taking this as an advantage, d-amino acids can be used to develop polypeptides or biobased materials with higher biostability. Chemoenzymatic peptide synthesis is a technique that uses proteases as biocatalysts to synthesize polypeptides, and d-stereospecific proteases can be used to synthesize polypeptides incorporating d-amino acids. However, engineered proteases with modified catalytic activities are required to allow the incorporation of d-amino acids with increased efficiency. To understand the stereospecificity presented by proteases and their involvement in polymerization reactions, we studied d-aminopeptidase. This enzyme displays the ability to efficiently synthesize poly d-alanine-based peptides under mild conditions. To elucidate the mechanisms involved in the unique specificity of d-aminopeptidase, we performed quantum mechanics/molecular mechanics simulations of its polymerization reaction and determined the energy barriers presented by the chiral substrates. The enzyme faces higher activation barriers for the acylation and aminolysis reactions with the l-stereoisomer than with the d-substrate (10.7 and 17.7 kcal mol⁻¹ higher, respectively). The simulation results suggest that changes in the interaction of the substrate with Asn155 influence the stereospecificity of the polymerization reaction.

We studied the molecular mechanism of d-aminopeptidase for the synthesis of polypeptides incorporating d-amino acids.     

Highly reactive 2-deoxy-2-iodo-d-allo and d-gulo pyranosyl sulfoxide donors ensure β-stereoselective glycosylations with steroidal aglycones

The preparation of well-defined d-xylo and d-ribo glycosides represents a synthetic challenge due to the limited configurational availability of starting materials and the laborious synthesis of homogeneous 2-deoxy-β-glycosidic linkages, in particular that of the sugar-steroid motif, which represents the “stereoselective determining step” of the overall synthesis. Herein we describe the use of 2-deoxy-2-iodo-glycopyranosyl sulfoxides accessible from widely available d-xylose and d-ribose monosaccharides as privileged glycosyl donors that permit activation at very low temperature. This ensures a precise kinetic control for a complete 1,2-trans stereoselective glycosylation of particularly challenging steroidal aglycones.

Highly stereoselective synthesis of challenging steroidal 2-deoxy-β-glycosides with d-xylo and d-ribo configurations enabled by low temperature activation of 2-deoxy-2-iodoglycopyranosyl sulfoxides.     

Stereoselective synthesis of (+)-5-thiosucrose and (+)-5-thioisosucrose

(+)-5-Thiosucrose 1, a novel isosteric sulfur analog of sucrose, was synthesized stereoselectively for the first time via indirect β-d-fructofuranosidation involving selective β-d-psicofuranosidation, followed by stereo-inversion of the secondary hydroxy group at the C-3 position on the furanose ring. Glycosidation of protected 5-thio-d-glucose with a d-psicofuranosyl donor provided β-d-psicofuranosyl 5-thio-α-d-glucopyranoside and that with d-fructofuranosyl donor gave α-d-fructofuranosyl 5-thio-α-d-glucopyranoside. Two anomeric stereocenters of the glycosyl donor and acceptor were controlled correctly to provide a single disaccharide among four possible anomeric isomers in the glycosylation. Conversion of the resulting disaccharides afforded (+)-5-thiosucrose 1 and (+)-5-thioisosucrose 2 in excellent yields, respectively. Inhibitory activities of 1 and 2 against α-glucosidase in vitro were also examined.

(+)-5-Thiosucrose and (+)-5-thioisosucrose were stereoselectively synthesized among four possible anomeric isomers using 5-thio-d-glucose as an α-directing glycosyl acceptor.     

Hydrogenation of crude and purified d-glucosone generated by enzymatic oxidation of d-glucose

d-Fructose is an important starting material for producing furfurals and other industrially important chemicals. While the base-catalyzed and enzymatic conversion of d-glucose to d-fructose is well known, the employed methods typically provide limited conversion. d-Glucosone can be obtained from d-glucose by enzymatic oxidation at the C2 position and, subsequently, selectively hydrogenated at C1 to form d-fructose. This work describes an investigation on the hydrogenation of d-glucosone, using both chromatographically purified and crude material obtained directly from the enzymatic oxidation, subjected to filtration and lyophilization only. High selectivities towards d-fructose were observed for both starting materials over a Ru/C catalyst. Hydrogenation of the crude d-glucosone was, however, inhibited by the impurities resulting from the enzymatic oxidation process. Catalyst deactivation was observed in the case of both starting materials.

Investigation on the hydrogenation of both chromatographically purified and crude d-glucosone directly from its enzymatic production process to yield d-fructose.     

Biochemical characterization of a novel ulvan lyase from Pseudoalteromonas sp. strain PLSV

Ulvans, complex polysaccharides found in the ulvales (green seaweed) cell wall, contain predominantly 3-sulfated rhamnose (Rha3S) linked to either d-glucuronic acid, l-iduronic acid or d-xylose. The ulvan lyase endolytically cleaves the glycoside bond between Rha3S and uronic acid via a β-elimination mechanism. Ulvan lyase has been identified as belonging to the polysaccharide lyase family PL24 or PL25 in the carbohydrate active enzymes database, in which fewer members have been characterized. We present the cloning and characterization of a novel ulvan lyase from Pseudoalteromonas sp. strain PLSV (PsPL). The enzymes were heterologously expressed in Escherichia coli BL21 (DE3) and purified as the His-tag fusion protein using affinity chromatography, ion-exchange chromatography and size-exclusion chromatography. The degradation products were determined by thin-layer chromatography (TLC), liquid chromatography-mass spectrometry (LC-MS) to be mainly disaccharides and tetrasaccharides. Ulvan lyase provides an example of degrading ulvales into oligosaccharides. Arg265, His152 and Tyr249 were considered to serve as catalytic residues based on PsPL structural model analysis.

Ulvans, complex polysaccharides found in the ulvales (green seaweed) cell wall, contain predominantly 3-sulfated rhamnose (Rha3S) linked to either d-glucuronic acid, l-iduronic acid or d-xylose.     

Remarkable diastereomeric effect on thermoresponsive behavior of polyurethane based on lysine and tartrate ester derivatives

This study describes the long-distance diastereomeric effect on thermoresponsive properties in water-soluble diastereomeric polyurethanes (PUs) composed of an l-lysine ethyl ester diisocyanate and a trimethylene glycol l-/d-tartrate ester, which have differences in spatial arrangements of the ethyl esters in the mirror image. The PUs based on l-lysine and l-/d-tartrate ester, named l-PU and d-PU, were synthesized with various number average molecular weights from 4700 to 13 100. In turbidimetry, l-PU showed a steep phase transition from 100%T to 0%T within about 10 °C at 4 g L⁻¹, whereas d-PU did not change completely to 0%T transmittance even at 80 °C at 4 g L⁻¹. In addition, the thermoresponsive properties of l-PU were less affected by concentration than those of d-PU. This long-distance diastereomeric effect on thermoresponsive behavior between l-PU and d-PU appeared in common among 6 samples with 4700 to 13 100 number average molecular weight. In the dynamic light scattering experiments at each transmittance, the hydrodynamic diameter (D_h) of l-PU increased up to 1000 nm, while the D_h of d-PU remained almost at 200–300 nm. The C O stretching vibration of FT-IR spectra showed that d-PU has more hydrogen-bonded ester groups than L-PU. Thus, we speculated that the difference in the retention of polymer chains in the micelle to promote intermicellar bridging generates the long-distance diastereomeric effect.

The long-distance diastereomeric effect on thermoresponsive properties in a polyurethane system consisting of chiral monomers was reported.     

Investigation on the chirality mechanism of chiral carbon quantum dots derived from tryptophan

Chiral carbon quantum dots (CQDs) with chirality, fluorescence and biocompatibility were synthesized by a one-step method with l-/d-tryptophan (l-/d-Trp), as both carbon source and chiral source. Levogyration-/dextrorotation-CQDs (l-/d-CQDs) were characterized by transmission electron microscopy, Fourier transform infrared spectrometry, ultraviolet-visible absorption, excitation and emission spectrometry and circular dichroism (CD) spectrometry. Results show that l-CQDs and d-CQDs present similar spherical morphology, functional groups and optical properties. The CD signal, around 220, 240 and 290 nm are opposite and symmetric, which conclusively demonstrates that l-CQDs and d-CQDs are enantiomers. Besides the CD signal around 220 nm from the inheritance of l-/d-Trp, two new chiral signals around 240 and 290 nm were induced by chiral environment.

To clarify the chirality mechanism of chiral CQDs prepared by l-/d-tryptophan, the chirality origin in CQD structure was revealed.     

d-Glucosamine production from chitosan hydrolyzation over a glucose-derived solid acid catalyst

A glucose-based solid acid catalyst (GSA) was synthesized by hydrothermal carbonization and its physicochemical properties were explored by various characterization techniques including IR, TG and SEM. In addition, its catalytic performance towards d-glucosamine formation from the hydrolysis of chitosan was extensively investigated to determine the effects of reaction parameters, such as reaction temperature, time and mass ratio of catalyst and reactants. The experimental results revealed that the yield of targeted product d-glucosamine could reach as high as 98.1% under optimal conditions (temperature: 110 °C; time: 6 h). After six catalytic cycles, no evident deactivation was observed, suggesting the satisfactory stability of the investigated solid acid catalyst. This might provide insight on the development of suitable catalyst systems for d-glucosamine formation to replace homogeneous catalysts.

A method for preparing d-glucosamine in aqueous phase by chitosan degradation by a solid acid, which resulted in high yields.     

Structural analysis and antioxidant activity of an arabinoxylan from Malvastrum coromandelianum L. (Garcke)

Malvastrum coromandelianum L. (Garcke) is extensively used in traditional medicinal systems to treat various ailments. In the present study, an alkali-soluble polysaccharide (MAP) was isolated from the leaves of M. coromandelianum in 1.15% (w/w) yield. MAP was composed of l-rhamnose, l-arabinose, d-xylose, d-glucose and d-galactose in a 1.00 : 6.04 : 19.88 : 1.07 : 3.03 molar ratio along with d-glucuronic acid (1.95). Methylation/linkage analysis revealed a backbone of →4)-β-d-Xylp(1→ (30.09 mol%) with a side chain of →3)-α-l-Araf(1→ (15.21 mol%) residues. The structure of MAP was elucidated by a combination of degradative and derivatization techniques, including hydrolysis, alditol acetate derivatization, methylation, GC-MS, partial hydrolysis, ESI-MS and NMR (1D, 2D) spectral analysis. Based on correlation analysis, MAP was found to be an arabinoxylan comprising a backbone of →4)-β-d-linked Xylp(1→ with branching at O-2 by a →3)-α-l-Araf(1→ and →3)-β-d-Xylp(1→ chain. MAP also exhibited ferric ion reducing activity, with a reducing power of 0.914 ± 0.01 (R² = 0.972) at 1 mg mL⁻¹ concentration, which showed dose-dependent behavior. MAP can be utilized as a potential antioxidant.

The structure of MAP was studied by degradative, derivatization and spectroscopic methods, and it was found to be an arabinoxylan comprising a backbone of →4)-β-d-linked Xylp(1→ with branching at O-2 by →3)-α-l-Araf(1→ and →3)-β-d-Xylp(1→ chains.     

Gram scale production of 1-azido-β-d-glucose via enzyme catalysis for the synthesis of 1,2,3-triazole-glucosides

The production of analytical amounts of azido sugars is used as a means of verifying catalytic acid/base mutations of retaining glycosidase, but application of this process to preparative synthesis has not been reported. The catalytic acid/base mutant of Thermoanaerobacterium xylanolyticus GH116 β-glucosidase, TxGH116D593A, catalyzed the gram scale production of 1-azido-β-d-glucose (1) from p-nitropheyl-β-d-glucopyranoside (pNPGlc) and azide via a transglucosylation reaction. Overnight reaction of the enzyme with pNPGlc and NaN₃ in aqueous MES buffer (pH 5.5) at 55 °C produced 1 (3.27 g), which was isolated as a white foamy solid in 96% yield. This 1 was successfully utilized for the synthesis of fifteen 1,2,3-triazole-β-d-glucosyl derivatives (2–16) containing a variety of functional groups, via click chemistry.

The retaining β-glucosidase acid/base mutant TxGH116D593A catalyzed the production of 1-azido-β-d-glucose for synthesis of 15 1,2,3-triazole β-glucosyl derivatives.     

Peptidoglycan Cross-Linking in Glycopeptide-Resistant Actinomycetales

Synthesis of peptidoglycan precursors ending in d-lactate (d-Lac) is thought to be responsible for glycopeptide resistance in members of the order Actinomycetales that produce these drugs and in related soil bacteria. More recently, the peptidoglycan of several members of the order Actinomycetales was shown to be cross-linked by l,d-transpeptidases that use tetrapeptide acyl donors devoid of the target of glycopeptides. To evaluate the contribution of these resistance mechanisms, we have determined the peptidoglycan structure of Streptomyces coelicolor A(3)2, which harbors a vanHAX gene cluster for the production of precursors ending in d-Lac, and Nonomuraea sp. strain ATCC 39727, which is devoid of vanHAX and produces the glycopeptide {"type":"entrez-nucleotide","attrs":{"text":"A40296","term_id":"2296392","term_text":"A40296"}}A40296. Vancomycin retained residual activity against S. coelicolor A(3)2 despite efficient incorporation of d-Lac into cytoplasmic precursors. This was due to a d,d-transpeptidase-catalyzed reaction that generated a stem pentapeptide recognized by glycopeptides by the exchange of d-Lac for d-Ala and Gly. The contribution of l,d-transpeptidases to resistance was limited by the supply of tetrapeptide acyl donors, which are essential for the formation of peptidoglycan cross-links by these enzymes. In the absence of a cytoplasmic metallo-d,d-carboxypeptidase, the tetrapeptide substrate was generated by hydrolysis of the C-terminal d-Lac residue of the stem pentadepsipeptide in the periplasm in competition with the exchange reaction catalyzed by d,d-transpeptidases. In Nonomuraea sp. strain ATCC 39727, the contribution of l,d-transpeptidases to glycopeptide resistance was limited by the incomplete conversion of pentapeptides into tetrapeptides despite the production of a cytoplasmic metallo-d,d-carboxypeptidase. Since the level of drug production exceeds the level of resistance, we propose that l,d-transpeptidases merely act as a tolerance mechanism in this bacterium.     

Iodonium salts as efficient iodine(iii)-based noncovalent organocatalysts for Knorr-type reactions

Hypervalent iodine(iii)-derivatives display higher catalytic activity than other aliphatic and aromatic iodine(i)– or bromine(i)-containing substrates for a Knorr-type reaction of N-acetyl hydrazides with acetyl acetone to give N-acyl pyrazoles. The highest activity was observed for dibenziodolium triflate, for which 10 mol% resulted in the generation of N-acyl pyrazole from acyl hydrazide and acetyl acetone typically at 50 °C for 3.5–6 h with up to 99% isolated yields. ¹H NMR titration data and DFT calculations indicate that the catalytic activity of the iodine(iii) is caused by the binding with a ketone.

The dibenziodolium cation displays high catalytic activity for the Knorr-type reactions via binding with the carbonyl O atom.     

A novel surface plasmon resonance sensor based on a functionalized graphene oxide/molecular-imprinted polymer composite for chiral recognition of l-tryptophan

Herein, a novel surface plasmon resonance (SPR) sensor based on a functionalized graphene oxide (GO)/molecular-imprinted polymer composite was developed for the chiral recognition of l-tryptophan (l-Trp). The composite''s recognition element was prepared via a facile and green synthesis approach using polydopamine as both a reducer of GO and a functional monomer as well as a cross-linker for molecular imprinting. The composite was characterized via Fourier transform infrared spectroscopy, scanning electron microscopy, X-ray diffraction, and Raman spectroscopy. After attaching the composite onto the gold surface of an SPR chip, the sensor was characterized using contact-angle measurements. The sensor exhibited excellent selectivity and chiral recognition for the template (i.e., l-Trp). Density functional theory computations showed that the difference in hydrogen bonding between the composite element and l-Trp and d-Trp played an important role in chiral recognition.

Novel SPR sensor for chiral recognition of l-tryptophan using a functionalized graphene oxide/molecularly-imprinted polymer composite as a recognition element.     

Biogenetic origin of the D-isoleucine and N-methyl-L-alloisoleucine residues in the actinomycins.

Studies with ¹⁴C-labeled isoleucine stereisomers have established that l-alloisoleucine, d-alloisoleucine, and d-isoleucine may function as precursors for the biogenesis of d-isoleucine and N-methyl-l-alloisoleucine residues in actinomycin. l-[¹⁴C]isoleucine appears to be employed chiefly for d-alloisoleucine (and N-methylisoleucine [?] formation); however, its role in the biosynthesis of d-isoleucine and N-methylalloisoleucine remains unclear. The potential pathway of biosynthesis of d-isoleucine and N-methyl-l-isoleucine is discussed.     

Cu(ii)-alginate-based superporous hydrogel catalyst for click chemistry azide–alkyne cycloaddition type reactions in water

A novel sustainable hydrogel catalyst based on the reaction of sodium alginate naturally extracted from brown algae Laminaria digitata residue with copper(ii) was prepared as spherical beads, namely Cu(ii)-alginate hydrogel (Cu(ii)-AHG). The morphology and structural characteristics of these beads were elucidated by different techniques such as SEM, EDX, BET, FTIR and TGA analysis. Cu(ii)-AHG and its dried form, namely Cu(ii)-alginate (Cu(ii)-AD), are relatively uniform with an average pore ranging from 200 nm to more than 20 μm. These superporous structure beads were employed for the copper catalyzed [3 + 2] cycloaddition reaction of aryl azides and terminal aryl alkynes (CuAAC) via click chemistry at low catalyst loading, using water as a solvent at room temperature and pressure. The catalytic active copper(i) species was generated by the reduction of copper(ii) by terminal alkyne via the oxidative alkyne homocoupling reaction. The prepared catalysts were found to be efficient (85–92%) and regioselective by affording only 1,4-disubstituted-1,2,3-triazoles. They were also recoverable and reused in their dried form for at least four consecutive times without a clear loss of efficiency. A mechanistic study was performed through density functional theory (DFT) calculations in order to explain the regioselectivity outcome of Cu(ii)-alginate in CuAAC reactions. The analysis of the local electrophilicity (ω_k) at the electrophilic reagent and the local nucleophilicity (N_k) at the nucleophilic confirms the polar character of CuAAC. This catalyst has the main advantage of being sustainably ligand-free and recyclable.

The Cu(ii)-alginate-based superporous hydrogel was prepared and used as a heterogenous catalyst in the regioselective click of 1,4-disubstituted-1,2,3-triazoles by CuAAC reactions.     

Synthesis of alginate–polycation capsules of different composition: characterization and their adsorption for [As(iii)] and [As(v)] from aqueous solutions

The uptake of arsenite [As(iii)] and arsenate [As(v)] by functionalized calcium alginate (Ca-Alg) beads from aqueous solutions was investigated. Ca-Alg beads were protonated with poly-l-lysine (PLL) or polyethyleneimine (PEI) using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide/N-hydroxysuccinimide (EDC/NHS) or glutaraldehyde (GA) as crosslinking agents. Four types of protonated beads were prepared: Ca-Alg-EDC/NHS (PLL or PEI) and Ca-Alg-GA (PLL or PEI). Fourier transform infrared spectroscopy in total attenuated reflection mode (FTIR-ATR), analysis showed presence and increased intensity of bands corresponding to OH, NH, CH₂ and CH₃ groups in modifications with both polycations. In addition, thermogravimetric analysis and atomic force microscopy of all modified capsules showed an increase in thermal stability and uniformity of the capsules, respectively. Ca-Alg-EDC/NHS-PLL beads had the maximum adsorption capacity of [As(v)] (312.9 ± 4.7 μg g⁻¹ of the alginate) at pH 7.0 and 15 minute exposure, while Ca-Alg-EDC/NHS-PEI beads had the maximum adsorption capacity of [As(iii)] (1052.1 ± 4.6 μg g⁻¹ of alginate). However, all these EDC containing beads were degraded in the presence of citrate. Ca-Alg-GA-PEI beads removed 252.8 ± 9.7 μg of [As(v)] μg g⁻¹ of alginate and 524.7 ± 5.3 de [As(iii)] μg g⁻¹ of alginate, resulting the most stable capsules and suitable for As removal.

A simple protonation of alginate beads allows the absorption of arsenate and arsenite.