Controllable Synthesis of Monolayer Poly(acrylic acid) on the Channel Surface of Mesoporous Alumina for Pb(II) Adsorption.

Polymer/inorganic nanocomposites exhibit special properties due to highly intimate interactions between organic and inorganic phases and thus have been deployed for various applications. Among them, nanocomposites with monolayer polymer coverage on the inorganic surface demonstrate the highest efficiency for applications. However, the controllable synthesis of the polymer monolayer in mesopores of inorganic substrates remains a challenge. In this study, poly(acrylic acid)/γ-alumina nanocomposites (PAA/alumina) were synthesized via the in situ polymerization of acrylic acid impregnated in mesopores of alumina. By applying the preneutralization of monomers, the polymerization was found to be highly controllable in generating monolayer PAA coverage. The formation of monolayers was verified by thermogravimetry, semiquantitative Fourier transform infrared spectroscopy, N2 adsorption-desorption, and Pb(II) adsorption. Alternatively, the organic loadings of PAA/alumina composite samples could be controlled in the range of 0.2 to 1.0 equiv of monolayer, together with the linearly correlated metal ion adsorption capacity. As calculated by the complexation model, one Pb(II) is combined with two carboxylate groups of PAA. The formation of the monolayer polymer inside mesoporous oxide channels represents a method for the development of highly promising functional nanocomposites.

Effect of ultrasonic pretreatment on kinetics of gelatin hydrolysis by collagenase and its mechanism.

Gelatin is a mixture of soluble proteins prepared by partial hydrolysis of native collagen. Gelatin can be enzymatically hydrolyzed to produce bioactive hydrolysates. However, the preparation of gelatin peptide with expected activity is usually a time-consuming process. The production efficiency of gelatin hydrolysates needs to be improved. In present work, effect of ultrasonic pretreatment on kinetic parameters of gelatin hydrolysis by collagenase was investigated based on an established kinetic model. With ultrasonic pretreatment, reaction rate constant and enzyme inactivation constant were increased by 27.5% and 27.8%, respectively. Meanwhile, hydrolysis activation energy and enzyme inactivation energy were reduced by 36.3% and 43.0%, respectively. In order to explore its possible mechanism, influence of sonication on structural properties of gelatin was determined using atomic force microscopy, particle size analyzer, fluorescence spectroscopy, protein solubility test and Fourier transform infrared spectroscopy. Moreover, hydrogen peroxide was used as a positive control for potential sonochemical effect. It was found that reduction of gelatin particle size was mainly caused by physical effect of ultrasound. Increased solubility and variation in ß-sheet and random coil elements of gelatin were due to sonochemical effect. Both physical and chemical effects of sonication contributed to the change in α-helix and ß-turn structures. The current results suggest that ultrasound can be potentially applied to stimulate the production efficiency of gelatin peptides, mainly due to its effects on modification of protein structures.

Effect of ultrasound on the activity and conformation of α-amylase, papain and pepsin.

The effect of ultrasound on the activity of α-amylase, papain and pepsin was investigated and the mechanism of the effect was explored by determining their conformational changes. With the irradiation of power ultrasound, the activity of α-amylase and papain was inhibited, while the activity of pepsin was activated. According to the analysis of circular dichroism, Fourier transform infrared and fluorescence spectroscopy, the πo → π(∗) amide transitions and secondary structural components, especially ß-sheet, of these three enzymes were significantly influenced by ultrasound. The tryptophan fluorescence intensity of the three enzymes was also observed to be affected by sonication. Furthermore, it was found that the pepsin molecule might gradually be resistant to prolonged ultrasonic treatment and recover from the ultrasound-induced damage to its original structure. The results suggested that the activity of α-amylase, papain and pepsin could be modified by ultrasonic treatment mainly due to the variation of their secondary and tertiary structures.

Adsorption and separation of proteins by collagen fiber adsorbent.

The separation of proteins is a key step in biomedical and pharmaceutical industries. In the present investigation, the collagen fiber adsorbent (CFA) was exploited as column packing material to separate proteins. Bovine serum albumin (BSA), bovine hemoglobin (Hb) and lysozyme (LYS) that have different isoelectric points (pIs) were selected as model proteins to investigate the separation ability of CFA to proteins. In batch adsorption, the adsorption behaviors of these proteins on CFA under different pHs and ionic strengths indicated that the electrostatic interaction plays a predominant role in the adsorption of proteins on CFA. CFA exhibited high adsorption capacity to Hb and LYS. In column separation, the proteins were completely separated by adjusting pH and ionic strength of the eluent. The increase of flow rate could reduce the separation time with no influence on the recovery of protein in the experimental range. The protein recovery was higher than 90% even when the CFA column was re-used for 4 times in separation of BSA and LYS, and the retention time of BSA or LYS was almost constant during the repeated applications. In addition, as a practical application, LYS was successfully separated from chicken egg white powder by CFA column.

Complex oxide-noble metal conjugated nanoparticles.

Hybrid nanoparticles (NPs) composed of multiple components offer new opportunities for next-generation materials. In this study, a paradigm for the noble metal/ternary complex oxide hybrid NPs is reported by adopting pulsed laser ablation in liquids. As model hybrids, gold-spinel heterodimer (Au-CoFe2O4) and gold-pervoskite heterodimer (Au-SrTiO3) NPs are investigated. This work has demonstrated the diverse playgroup of NP conjugation enlarged by complex oxides.

Adsorptive removal of Cu(II) from aqueous solutions using collagen-tannin resin.

The collagen-tannin resin (CTR), as a novel adsorbent, was prepared via a reaction of collagen with black wattle tannin and aldehyde, and its adsorption properties to Cu(II) were systematically investigated, including pH effect, adsorption equilibrium, adsorption kinetics, and column adsorption. The adsorption capacity of Cu(II) on CTR was pH-dependent, and it increased with the increase of solution pH. The adsorption isotherms were well described by Langmuir isotherm model with correlating constant (R(2)) higher than 0.99. The adsorption capacity determined at 303 K was high up to 0.26 mmol/g, which was close to the value (0.266 mmol/g) estimated from Langmuir equation. The adsorption capacity was increased with the increase of temperature, and thermodynamic calculations suggested that the adsorption of Cu(II) on CTR is an endothermic process. The adsorption kinetics were well fitted by the pseudo-second-order rate model. Further column studies suggested that CTR was effective for the removal of Cu(II) from solutions, and more than 99% of Cu(II) was desorbed from column using 0.1 mol/L HNO(3) solution. The CTR column can be reused to adsorb Cu(II) without any loss of adsorption capacity.

Adsorptive recovery of UO2(2+) from aqueous solutions using collagen-tannin resin.

Collagen-tannin resin (CTR), as a novel adsorbent, was prepared via reaction of collagen with black wattle tannin and aldehyde, and its adsorption properties to UO(2)(2+) were investigated in detail, including pH effect, adsorption kinetics, adsorption equilibrium and column adsorption kinetics. The adsorption of UO(2)(2+) on CTR was pH-dependent, and the optimal pH range was 5.0-6.0. CTR exhibited excellent adsorption capacity to UO(2)(2+). For instance, the adsorption capacity obtained at 303 K and pH 6.0 was as high as 0.91 mmol UO(2)(2+)/g when the initial concentration of UO(2)(2+) was 1.0 mmol/L. In kinetics studies, the adsorption equilibrium can be reached within 300 min, and the experimental data were well fitted by the pseudo-second-order rate model, and the equilibrium adsorption capacities calculated by the model were almost the same as those determined by experiments. The adsorption isotherms could be well described by the Freundlich equation with the correlation coefficients (R(2)) higher than 0.99, the adsorption behaviors of UO(2)(2+) on CTR column were investigated as well. Present study suggested that the CTR can be used for the adsorptive recovery of UO(2)(2+) from aqueous solutions.

Collagen fiber immobilized Fe(III): a novel catalyst for photo-assisted degradation of dyes.

A novel catalyst for the Fenton reaction was prepared by immobilizing Fe(III) onto collagen fiber and its high activity as a catalyst for degradation of dyes under irradiation of UVC was proved.

Adsorption of fluoride on zirconium(IV)-impregnated collagen fiber.

A novel adsorbent, zirconium(IV)-impregnated collagen fiber, was prepared. Zr(IV) was uniformly dispersed in collagen fiber, mainly through chemical bonds, and was able to withstand the extraction of water. This adsorbent is effective for the removal of fluoride from aqueous solutions. The adsorption capacity was 2.29 mmol/g at pH = 5.5 when 5.00 mmol/L fluoride solution was adsorbed by use of 0.100 g of adsorbent, and the extent of removal was 97.4% when the adsorbent dose was 0.300 g. The adsorption isotherms were well fitted by the Langmuir equation, and the maximum adsorption capacities calculated by the Langmuir equation were close to those determined by experiment. The adsorption capacity increased with rising temperature. These facts imply that the mechanism of chemical adsorption might be involved in the adsorption process of fluoride on the absorbent and that fluorides are adsorbed in the form of monolayer coverage on the surface of the adsorbent. The adsorption kinetics of fluoride onto Zr(IV)-impregnated collagen fiber could be described by Lagergren's pseudo-first-order rate mode. The investigation on desorption indicated that this adsorbent is easily regenerated by use of dilute NaOH solution.