The Experts below are selected from a list of 38292 Experts worldwide ranked by ideXlab platform
J De Groot - One of the best experts on this subject based on the ideXlab platform.
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mild Isolation Procedure discloses new protein structural properties of β lactoglobulin
Journal of Dairy Science, 2001Co-Authors: H H J De Jongh, T Groneveld, J De GrootAbstract:To explore the potentially available functional properties of beta-lactoglobulin in, for example, the processing of food products, it is important to isolate the protein by a Procedure that avoids all possible denaturing conditions, such as low pH, high ionic strength, or low or elevated temperatures that could cause the protein to undergo irreversible conformational changes. In this work, a mild Isolation protocol for beta-lactoglobulin from bovine milk is presented, applicable to semi large-scale Isolations (50 to 200 g). The protein could be isolated with a high efficiency (>80%) and a good purity (>98%). Biochemical characterization of the material demonstrated no lactosylation of the protein, nor the formation of irreversibly associated dimers. Also, no proteose peptones could be detected. The ability of beta-lactoglobulin to undergo conformational changes is studied by far and near-ultraviolet circular dichroism and differential scanning calorimetry. A "global" unfolding of the protein is detected around 72 (tertiary level) and 77 degrees C (secondary level). The dimer-monomer dissociation occurring around 52 degrees C could also be monitored at a secondary structural level. Remarkably, a low temperature transition around 30 degrees C was observed, where approximately 10 beta-stranded residues unfold cooperatively, not been reported previously. This low temperature transition is irreversible at temperatures higher than 35 degrees C or upon freezing the material at -20 degrees C. The addition of 20% glycerol could prevent this irreversible conformational change. The effect of the low temperature transition on the protein's functionality remains to be investigated.
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Mild Isolation Procedure discloses new protein structural properties of b-lactoglobulin
2001Co-Authors: H H J De Jongh, Groneveld T., J De GrootAbstract:To explore the potentially available functional properties of β-lactoglobulin in, for example, the processing of food products, it is important to isolate the protein by a Procedure that avoids all possible denaturing conditions, such as low pH, high ionic strength, or low or elevated temperatures that could cause the protein to undergo irreversible conformational changes. In this work, a mild Isolation protocol for β-lactoglobulin from bovine milk is presented, applicable to semi large-scale Isolations (50 to 200 g). The protein could be isolated with a high efficiency (>80€and a good purity (>98Ž Biochemical characterization of the material demonstrated no lactosylation of the protein, nor the formation of irreversibly associated dimers. Also, no proteose peptones could be detected. The ability of β-lactoglobulin to undergo conformational changes is studied by far and near-ultraviolet circular dichroism and differential scanning calorimetry. A βglobalβ unfolding of the protein is detected around 72 (tertiary level) and 77°C (secondary level). The dimer-monomer dissociation occurring around 52°C could also be monitored at a secondary structural level. Remarkably, a low temperature transition around 30°C was observed, where approximately 10 β-stranded residues unfold cooperatively, not been reported previously. This low temperature transition is irreversible at temperatures higher than 35°C or upon freezing the material at -20°C. The addition of 20␐lycerol could prevent this irreversible conformational change. The effect of the low temperature transition on the protein's functionality remains to be investigated
Adam Strzebonski - One of the best experts on this subject based on the ideXlab platform.
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real root Isolation for exp log functions
International Symposium on Symbolic and Algebraic Computation, 2008Co-Authors: Adam StrzebonskiAbstract:We present a real root Isolation Procedure for univariate functions obtained by composition and rational operations from exp, log, and real constants. We discuss implementation of the Procedure and give empirical results. The Procedure requires the ability to determine signs of exp-log functions at simple roots of other exp-log functions. The currently known method to do this depends on Schanuel's conjecture [6].
George A Somkuti - One of the best experts on this subject based on the ideXlab platform.
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Isolation of sagi a new haeiii isoschizomer from streptococcus agalactiae
Applied Microbiology and Biotechnology, 1995Co-Authors: M T Poch, George A SomkutiAbstract:A new HaeIII isochizomer from Streptococcus agalactiae was isolated by a single-step purification method. The highly active restriction endonuclease, SagI, was free of nonspecific nuclease activity and was suitable for use in molecular biology Procedures. The rapid Isolation Procedure may be applicable for the recovery of other restriction endonucleases from bacteria.
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Isolation of sag i a new hae iii isoschizomer from streptococcus agalactiae
Applied Microbiology and Biotechnology, 1995Co-Authors: M T Poch, George A SomkutiAbstract:A new HaeIII isochizomer from Streptococcus agalactiae was isolated by a single-step purification method. The highly active restriction endonuclease, SagI, was free of nonspecific nuclease activity and was suitable for use in molecular biology Procedures. The rapid Isolation Procedure may be applicable for the recovery of other restriction endonucleases from bacteria.
H H J De Jongh - One of the best experts on this subject based on the ideXlab platform.
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mild Isolation Procedure discloses new protein structural properties of β lactoglobulin
Journal of Dairy Science, 2001Co-Authors: H H J De Jongh, T Groneveld, J De GrootAbstract:To explore the potentially available functional properties of beta-lactoglobulin in, for example, the processing of food products, it is important to isolate the protein by a Procedure that avoids all possible denaturing conditions, such as low pH, high ionic strength, or low or elevated temperatures that could cause the protein to undergo irreversible conformational changes. In this work, a mild Isolation protocol for beta-lactoglobulin from bovine milk is presented, applicable to semi large-scale Isolations (50 to 200 g). The protein could be isolated with a high efficiency (>80%) and a good purity (>98%). Biochemical characterization of the material demonstrated no lactosylation of the protein, nor the formation of irreversibly associated dimers. Also, no proteose peptones could be detected. The ability of beta-lactoglobulin to undergo conformational changes is studied by far and near-ultraviolet circular dichroism and differential scanning calorimetry. A "global" unfolding of the protein is detected around 72 (tertiary level) and 77 degrees C (secondary level). The dimer-monomer dissociation occurring around 52 degrees C could also be monitored at a secondary structural level. Remarkably, a low temperature transition around 30 degrees C was observed, where approximately 10 beta-stranded residues unfold cooperatively, not been reported previously. This low temperature transition is irreversible at temperatures higher than 35 degrees C or upon freezing the material at -20 degrees C. The addition of 20% glycerol could prevent this irreversible conformational change. The effect of the low temperature transition on the protein's functionality remains to be investigated.
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Mild Isolation Procedure discloses new protein structural properties of b-lactoglobulin
2001Co-Authors: H H J De Jongh, Groneveld T., J De GrootAbstract:To explore the potentially available functional properties of β-lactoglobulin in, for example, the processing of food products, it is important to isolate the protein by a Procedure that avoids all possible denaturing conditions, such as low pH, high ionic strength, or low or elevated temperatures that could cause the protein to undergo irreversible conformational changes. In this work, a mild Isolation protocol for β-lactoglobulin from bovine milk is presented, applicable to semi large-scale Isolations (50 to 200 g). The protein could be isolated with a high efficiency (>80€and a good purity (>98Ž Biochemical characterization of the material demonstrated no lactosylation of the protein, nor the formation of irreversibly associated dimers. Also, no proteose peptones could be detected. The ability of β-lactoglobulin to undergo conformational changes is studied by far and near-ultraviolet circular dichroism and differential scanning calorimetry. A βglobalβ unfolding of the protein is detected around 72 (tertiary level) and 77°C (secondary level). The dimer-monomer dissociation occurring around 52°C could also be monitored at a secondary structural level. Remarkably, a low temperature transition around 30°C was observed, where approximately 10 β-stranded residues unfold cooperatively, not been reported previously. This low temperature transition is irreversible at temperatures higher than 35°C or upon freezing the material at -20°C. The addition of 20␐lycerol could prevent this irreversible conformational change. The effect of the low temperature transition on the protein's functionality remains to be investigated
Zorica Stojanović-radić - One of the best experts on this subject based on the ideXlab platform.
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A new antimicrobial glucosinolate autolysis product, 4-isothiocyanatobutanoic acid, from the diffuse wallflower (Erysimum diffusum): Methyl 4-isothiocyanatobutanoate, a long unrecognized artifact of the Isolation Procedure?
Food Chemistry, 2011Co-Authors: Niko S. Radulović, Milan S. Dekić, Zorica Stojanović-radićAbstract:Abstract A GC–MS analysis of Erysimum diffusum Ehrh. (Brassicaceae) glucosinolate autolysis products led to the identification of a new mustard oil constituent – 4-isothiocyanatobutanoic acid. The identity of the new glucosinolate breakdown product was confirmed by means of co-injection of the synthetic compound in the GC with the root autolysate and derivatization reaction to the well known methyl ester. Methyl ester of this acid was long believed to be a genuine glucosinolate hydrolysis product but we now provide evidence that it could be an artifact of the Isolation Procedure. 4-Isothiocyanatobutanoic acid was assayed for antimicrobial activity and demonstrated significant inhibitory (10–220 μg/ml) and microbicidal (10–1175 μg/ml) activity against important human pathogens.
