Comparison of polymer induced and solvent induced trypsin denaturation: the role of hydrophobicity
| Autor: | Surendra Ponrathnam, Uma Addepally, Siona Daniels, Nitin W. Fadnavis, Sarika Deokar, Lakshmi Swarnalatha Jasti |
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| Rok vydání: | 2013 |
| Předmět: |
Protein Denaturation
Polymers Surface Properties chemistry.chemical_compound Colloid and Surface Chemistry Side chain medicine Copolymer Organic chemistry Denaturation (biochemistry) Trypsin Physical and Theoretical Chemistry Alkyl chemistry.chemical_classification Aryl technology industry and agriculture Surfaces and Interfaces General Medicine Enzymes Immobilized Solvent chemistry Solvents Amine gas treating Adsorption Hydrophobic and Hydrophilic Interactions Biotechnology medicine.drug |
| Zdroj: | Colloids and surfaces. B, Biointerfaces. 116 |
| ISSN: | 1873-4367 |
| Popis: | 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 logPoctanol 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 (C50) is dependent on logPoctanol of the co-solvent. |
| Databáze: | OpenAIRE |
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