Removal of chromium(VI) from wastewater is essential as it is toxic. Thus, removal of chromium(VI) was performed using coffee polyphenol-formaldehyde/acetaldehyde resins as adsorbents. Adsorbent resins were prepared by condensation of decaffeinated coffee powder with formaldehyde/acetaldehyde and used for the removal of Cr(VI) ions from aqueous solutions. A simple and sensitive solid phase extraction procedure was applied for the determination of chromium at trace levels by spectroscopic method using 1,5-diphenylcarbazide reagent. The adsorption of Cr(VI) on the coffee polyphenol-formaldehyde/acetaldehyde resins was monitored by FTIR and EDX analysis. The metal adsorption parameters such as contact time, pH, Cr(VI) ion concentration, and adsorbent dose were investigated. For Cr(VI), the maximum adsorption capacity of coffee polyphenol-formaldehyde resins was 98% at pH 2. The experimental results showed that Cr(VI) bound strongly with coffee polyphenol-formaldehyde/acetaldehyde resins and utilization of resins could be improved greatly by reuse.
Allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) copolymer with 25% crosslink density (AGE-25) shows excellent bovine serum albumin (BSA) adsorption (up to 16% (w/w)) at pH 8.0 and the adsorbed BSA is strongly bound. This protein-coated polymer provides a novel matrix with naturally existing functional groups such as thiol, amino, and carboxylic acid that are available for covalent immobilization of functional enzymes. Employing appropriate strategies, trypsin as a model protein was covalently bound to BSA-coated matrix both independently, and in a stepwise manner on the same matrix, with less than 5% loss of enzyme activity during immobilization. Glutaraldehyde crosslinking after immobilization provide stable enzyme preparation with activity of 510 units/g recycled up to six times without loss of enzyme activity. AFM studies reveal that the polymer surface has protein peaks and valleys rather than a uniform monolayer distribution of the protein and the immobilized enzyme preparation can best be described as polymer supported cross-linked enzyme aggregates (CLEAs).
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