02723nas a2200325 4500008004100000022001400041245019400055210006900249260007300318300001200391490000700403520146800410653003301878653001501911653002601926653002501952653002501977653001702002653003502019653002602054653001202080100001802092700003102110700002002141700002402161700002902185700003002214700002502244856012802269 2012 eng d a0927-776500aAdsorption induced enzyme denaturation: the role of protein surface in adsorption induced protein denaturation on allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) copolymers0 aAdsorption induced enzyme denaturation the role of protein surfa aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcFEB a184-1900 v903 a

The effects of protein size on adsorption and adsorption-induced denaturation of proteins on copolymers of allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) have been studied. Different responses were observed for the amount of protein adsorbed and denatured on the polymer surface for different proteins (trypsin, alchol dehydrogenase from baker's yeast (YADH), glucose dehydrogenase (GDH) from Gluconobacter cerinus, and alkaline phosphates from calf intestinal mucosa (CIAP). Protein adsorption on the copolymer with 25% crosslink density (AGE-25) was dependent not only on the size of the protein but also on the presence of glycoside residues on the protein surface. Adsorption and denaturation of proteins follows the order YADH > trypsin > GDH >> CIAP although the molecular weights of the proteins follow the order YADH > CIAP > GDH > trypsin. The lack of correlation between amount of adsorbed protein and its molecular weight was due to the presence of glycoside residues on CIAP and GDH which protect the enzyme surface from denaturation. Enzyme stabilities in aqueous solutions of 1-cyclohexyl-2-pyrrolidinone (CHP) correlate well with the trend in denaturation by the copolymer, strongly suggesting that hydrophobic interactions play a major role in protein binding and the mechanism of protein denaturation is similar to that for water-miscible organic solvents. (C) 2011 Elsevier B.V. All rights reserved.

10a1-Cyclohexyl-2-pyrrolidinone10aAdsorption10aAlcohol dehydrogenase10aAlkaline phosphatase10aallyl glycidyl ether10aDenaturation10aethylene glycol dimethacrylate10aGlucose dehydrogenase10aTrypsin1 aThudi, Lahari1 aJasti, Lakshmi, Swarnalath1 aSwarnalatha, Y.1 aFadnavis, Nitin, W.1 aMulani, Khudbudin, Baban1 aDeokar, Sarika, Babasaheb1 aPonrathnam, Surendra uhttps://library.ncl.res.in/content/adsorption-induced-enzyme-denaturation-role-protein-surface-adsorption-induced-protein-002020nas a2200265 4500008004100000022001400041245010300055210006900158260007300227300001200300490000800312520108200320653001501402653001701417653001901434653001201453653001201465100003101477700002401508700001901532700001901551700003001570700002501600856012901625 2014 eng d a0927-776500aComparison of polymer induced and solvent induced trypsin denaturation: the role of hydrophobicity0 aComparison of polymer induced and solvent induced trypsin denatu aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcAPR a201-2050 v1163 a

Trypsin adsorption from aqueous buffer by various copolymers of allyl glycidyl ether-ethylene glycol dimethacrylate (AGE-EGDM) copolymer with varying crosslink density increases with increasing crosslink density and the effect slowly wears off after reaching a plateau at 50% crosslink density. The copolymer with 25% crosslink density was reacted with different amines with alkyl/aryl side chains to obtain a series of copolymers with 1,2-amino alcohol functional groups and varying hydrophobicity. Trypsin binding capacity again increases with hydrophobicity of the reacting amine and a good correlation between logP(octanol) of the amine and protein binding is observed. The bound trypsin is denatured to the extent of 90% in spite of the presence of hydrophilic hydroxyl and amino groups. The behavior was comparable to that in mixtures of aqueous buffer and water-miscible organic co-solvents where the solvent concentration required to deactivate 50% of the enzyme (C-50) is dependent on logP(octanol) of the co-solvent. (C) 2014 Elsevier B.V. All rights reserved.

10aAdsorption10aDenaturation10aHydrophobicity10aPolymer10aTrypsin1 aJasti, Lakshmi, Swarnalath1 aFadnavis, Nitin, W.1 aAddepally, Uma1 aDaniels, Siona1 aDeokar, Sarika, Babasaheb1 aPonrathnam, Surendra uhttps://library.ncl.res.in/content/comparison-polymer-induced-and-solvent-induced-trypsin-denaturation-role-hydrophobicity-001927nas a2200229 4500008004100000022001400041245007200055210006900127260006700196300001000263490000800273520116600281653001501447653001501462653001701477653001301494653002701507100001701534700002501551700001901576856010201595 2016 eng d a0021-899500aSelective solid-phase extraction of metal for water decontamination0 aSelective solidphase extraction of metal for water decontaminati a111 RIVER ST, HOBOKEN 07030-5774, NJ USAbWILEY-BLACKWELLcJAN a428490 v1333 a

Metal-contaminated industrial effluent is a major concern for human health. Therefore, the removal of metal is of primary importance. In this study, metals were selectively extracted from water. Selective metal recovery was studied with a crown-ether-based polymer, wherein the selectivity was observed for strontium over lead. Parameters influencing the metal recovery, such as the contact time, adsorbent dosage, and metal-ion concentration, were evaluated. Interestingly, the adsorption rate of strontium was exponentially increased for the initial 4 h, and lead was adsorbed exponentially after 6 h. Notably, 98% strontium adsorption and 64% lead adsorption were obtained in 24 h. The Langmuir adsorption isotherm was in good agreement and demonstrated that the reactive sites of the adsorbent were homogeneous with monolayer metal adsorption with an adsorbent. The Freundlich adsorption isotherm was not obeyed by both metals. The pseudo-first-order and pseudo-second-order kinetics indicated that strontium was adsorbed by chemisorption and lead was adsorbed by physisorption. (c) 2015 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2016, 132, 42849.

10aAdsorption10acopolymers10acrosslinking10akinetics10aradical polymerization1 aMane, Sachin1 aPonrathnam, Surendra1 aChavan, Nayaku uhttps://library.ncl.res.in/content/selective-solid-phase-extraction-metal-water-decontamination-1