title: Adsorption induced enzyme denaturation: the role of protein surface in adsorption induced protein denaturation on allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) copolymers.
abstract: 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.
authors: Biotransformations Laboratory, Indian Institute of Chemical Technology, Hyderabad, India.
authors: Lahari
authors: L
authors: Thudi
authors: Lakshmi S
authors: LS
authors: Jasti
authors: Y
authors: Y
authors: Swarnalatha
authors: Nitin W
authors: NW
authors: Fadnavis
authors: Khudbudin
authors: K
authors: Mulani
authors: Sarika
authors: S
authors: Deokar
authors: Surendra
authors: S
authors: Ponrathnam
mesh_terms: D000327:Adsorption; D000426:Alcohol Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D000469:Alkaline Phosphatase / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D001709:Biotechnology; D002417:Cattle; D004795:Enzyme Stability; D004852:Epoxy Compounds / Q000737:chemistry / Q000378:metabolism; D020576:Gluconobacter; D042843:Glucose 1-Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D006027:Glycosides / Q000737:chemistry* / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D008689:Methacrylates / Q000737:chemistry / Q000378:metabolism; D008970:Molecular Weight; D011485:Protein Binding; D011489:Protein Denaturation; D012441:Saccharomyces cerevisiae; D012996:Solutions; D013499:Surface Properties; D014357:Trypsin / Q000737:chemistry* / Q000378:metabolism
chemical_list: D004852:Epoxy Compounds; D006027:Glycosides; D008689:Methacrylates; D012996:Solutions; C004919:ethylene dimethacrylate; D000426:Alcohol Dehydrogenase; D042843:Glucose 1-Dehydrogenase; D000469:Alkaline Phosphatase; D014357:Trypsin; C054361:allyl glycidyl ether