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Surendra Ponrathnam - One of the best experts on this subject based on the ideXlab platform.
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adsorption induced Enzyme Denaturation the role of protein surface in adsorption induced protein Denaturation on allyl glycidyl ether age ethylene glycol dimethacrylate egdm copolymers
Colloids and Surfaces B: Biointerfaces, 2012Co-Authors: Lahari Thudi, Lakshmi Swarnalatha Jasti, Nitin W Fadnavis, Y Swarnalatha, Khudbudin Mulani, Sarika Deokar, Surendra PonrathnamAbstract: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.
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adsorption induced Enzyme Denaturation the role of polymer hydrophobicity in adsorption and Denaturation of α chymotrypsin on allyl glycidyl ether age ethylene glycol dimethacrylate egdm copolymers
Langmuir, 2010Co-Authors: Challa Lahari, Lakshmi Swarnalatha Jasti, Nitin W Fadnavis, Sarika Deokar, Kalpana Vishwanathrao Sontakke, Ganesh Ingavle, Surendra PonrathnamAbstract:Effects of changes in hydrophobicity of polymeric support on structure and activity of α-chymotrypsin (E.C. 3.4.21.1) have been studied with copolymers of allyl glycidyl ether (AGE) and ethylene glycol dimethacrylate (EGDM) with increasing molar ratio of EGDM to AGE (cross-link density 0.05 to 1.5). The Enzyme is readily adsorbed from aqueous buffer at room temperature following Langmuir adsorption isotherms in unexpectedly large amounts (25% w/w). Relative hydrophobicity of the copolymers has been assessed by studying adsorption of naphthalene and Fmoc-methionine by the series of copolymers from aqueous solutions. Polymer hydrophobicity appears to increase linearly on increasing cross-link density from 0.05 to 0.25. Further increase in cross-link density causes a decrease in naphthalene binding but has little effect on binding of Fmoc-Met. Binding of α-chymotrypsin to these copolymers follow the trend for Fmoc-methionine binding, rather than naphthalene binding, indicating involvement of polar interactio...
Nitin W Fadnavis - One of the best experts on this subject based on the ideXlab platform.
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adsorption induced Enzyme Denaturation the role of protein surface in adsorption induced protein Denaturation on allyl glycidyl ether age ethylene glycol dimethacrylate egdm copolymers
Colloids and Surfaces B: Biointerfaces, 2012Co-Authors: Lahari Thudi, Lakshmi Swarnalatha Jasti, Nitin W Fadnavis, Y Swarnalatha, Khudbudin Mulani, Sarika Deokar, Surendra PonrathnamAbstract: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.
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adsorption induced Enzyme Denaturation the role of polymer hydrophobicity in adsorption and Denaturation of α chymotrypsin on allyl glycidyl ether age ethylene glycol dimethacrylate egdm copolymers
Langmuir, 2010Co-Authors: Challa Lahari, Lakshmi Swarnalatha Jasti, Nitin W Fadnavis, Sarika Deokar, Kalpana Vishwanathrao Sontakke, Ganesh Ingavle, Surendra PonrathnamAbstract:Effects of changes in hydrophobicity of polymeric support on structure and activity of α-chymotrypsin (E.C. 3.4.21.1) have been studied with copolymers of allyl glycidyl ether (AGE) and ethylene glycol dimethacrylate (EGDM) with increasing molar ratio of EGDM to AGE (cross-link density 0.05 to 1.5). The Enzyme is readily adsorbed from aqueous buffer at room temperature following Langmuir adsorption isotherms in unexpectedly large amounts (25% w/w). Relative hydrophobicity of the copolymers has been assessed by studying adsorption of naphthalene and Fmoc-methionine by the series of copolymers from aqueous solutions. Polymer hydrophobicity appears to increase linearly on increasing cross-link density from 0.05 to 0.25. Further increase in cross-link density causes a decrease in naphthalene binding but has little effect on binding of Fmoc-Met. Binding of α-chymotrypsin to these copolymers follow the trend for Fmoc-methionine binding, rather than naphthalene binding, indicating involvement of polar interactio...
Lakshmi Swarnalatha Jasti - One of the best experts on this subject based on the ideXlab platform.
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adsorption induced Enzyme Denaturation the role of protein surface in adsorption induced protein Denaturation on allyl glycidyl ether age ethylene glycol dimethacrylate egdm copolymers
Colloids and Surfaces B: Biointerfaces, 2012Co-Authors: Lahari Thudi, Lakshmi Swarnalatha Jasti, Nitin W Fadnavis, Y Swarnalatha, Khudbudin Mulani, Sarika Deokar, Surendra PonrathnamAbstract: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.
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adsorption induced Enzyme Denaturation the role of polymer hydrophobicity in adsorption and Denaturation of α chymotrypsin on allyl glycidyl ether age ethylene glycol dimethacrylate egdm copolymers
Langmuir, 2010Co-Authors: Challa Lahari, Lakshmi Swarnalatha Jasti, Nitin W Fadnavis, Sarika Deokar, Kalpana Vishwanathrao Sontakke, Ganesh Ingavle, Surendra PonrathnamAbstract:Effects of changes in hydrophobicity of polymeric support on structure and activity of α-chymotrypsin (E.C. 3.4.21.1) have been studied with copolymers of allyl glycidyl ether (AGE) and ethylene glycol dimethacrylate (EGDM) with increasing molar ratio of EGDM to AGE (cross-link density 0.05 to 1.5). The Enzyme is readily adsorbed from aqueous buffer at room temperature following Langmuir adsorption isotherms in unexpectedly large amounts (25% w/w). Relative hydrophobicity of the copolymers has been assessed by studying adsorption of naphthalene and Fmoc-methionine by the series of copolymers from aqueous solutions. Polymer hydrophobicity appears to increase linearly on increasing cross-link density from 0.05 to 0.25. Further increase in cross-link density causes a decrease in naphthalene binding but has little effect on binding of Fmoc-Met. Binding of α-chymotrypsin to these copolymers follow the trend for Fmoc-methionine binding, rather than naphthalene binding, indicating involvement of polar interactio...
Sarika Deokar - One of the best experts on this subject based on the ideXlab platform.
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adsorption induced Enzyme Denaturation the role of protein surface in adsorption induced protein Denaturation on allyl glycidyl ether age ethylene glycol dimethacrylate egdm copolymers
Colloids and Surfaces B: Biointerfaces, 2012Co-Authors: Lahari Thudi, Lakshmi Swarnalatha Jasti, Nitin W Fadnavis, Y Swarnalatha, Khudbudin Mulani, Sarika Deokar, Surendra PonrathnamAbstract: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.
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adsorption induced Enzyme Denaturation the role of polymer hydrophobicity in adsorption and Denaturation of α chymotrypsin on allyl glycidyl ether age ethylene glycol dimethacrylate egdm copolymers
Langmuir, 2010Co-Authors: Challa Lahari, Lakshmi Swarnalatha Jasti, Nitin W Fadnavis, Sarika Deokar, Kalpana Vishwanathrao Sontakke, Ganesh Ingavle, Surendra PonrathnamAbstract:Effects of changes in hydrophobicity of polymeric support on structure and activity of α-chymotrypsin (E.C. 3.4.21.1) have been studied with copolymers of allyl glycidyl ether (AGE) and ethylene glycol dimethacrylate (EGDM) with increasing molar ratio of EGDM to AGE (cross-link density 0.05 to 1.5). The Enzyme is readily adsorbed from aqueous buffer at room temperature following Langmuir adsorption isotherms in unexpectedly large amounts (25% w/w). Relative hydrophobicity of the copolymers has been assessed by studying adsorption of naphthalene and Fmoc-methionine by the series of copolymers from aqueous solutions. Polymer hydrophobicity appears to increase linearly on increasing cross-link density from 0.05 to 0.25. Further increase in cross-link density causes a decrease in naphthalene binding but has little effect on binding of Fmoc-Met. Binding of α-chymotrypsin to these copolymers follow the trend for Fmoc-methionine binding, rather than naphthalene binding, indicating involvement of polar interactio...
Challa Lahari - One of the best experts on this subject based on the ideXlab platform.
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adsorption induced Enzyme Denaturation the role of polymer hydrophobicity in adsorption and Denaturation of α chymotrypsin on allyl glycidyl ether age ethylene glycol dimethacrylate egdm copolymers
Langmuir, 2010Co-Authors: Challa Lahari, Lakshmi Swarnalatha Jasti, Nitin W Fadnavis, Sarika Deokar, Kalpana Vishwanathrao Sontakke, Ganesh Ingavle, Surendra PonrathnamAbstract:Effects of changes in hydrophobicity of polymeric support on structure and activity of α-chymotrypsin (E.C. 3.4.21.1) have been studied with copolymers of allyl glycidyl ether (AGE) and ethylene glycol dimethacrylate (EGDM) with increasing molar ratio of EGDM to AGE (cross-link density 0.05 to 1.5). The Enzyme is readily adsorbed from aqueous buffer at room temperature following Langmuir adsorption isotherms in unexpectedly large amounts (25% w/w). Relative hydrophobicity of the copolymers has been assessed by studying adsorption of naphthalene and Fmoc-methionine by the series of copolymers from aqueous solutions. Polymer hydrophobicity appears to increase linearly on increasing cross-link density from 0.05 to 0.25. Further increase in cross-link density causes a decrease in naphthalene binding but has little effect on binding of Fmoc-Met. Binding of α-chymotrypsin to these copolymers follow the trend for Fmoc-methionine binding, rather than naphthalene binding, indicating involvement of polar interactio...