The Experts below are selected from a list of 23442024 Experts worldwide ranked by ideXlab platform
Monika Pischetsrieder - One of the best experts on this subject based on the ideXlab platform.
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site specific formation of maillard oxidation and condensation products from whey proteins during reaction with lactose
Journal of Agricultural and Food Chemistry, 2007Co-Authors: Jasmin Meltretter, Silke Seeber, Andreas Humeny, Cordmichael Becker, Monika PischetsriederAbstract:Heat treatment of dairy products leads to structural changes of proteins, which can severely decrease the nutritional value [Mauron, J. J. Nutr. Sci. Vitaminol. (Tokyo) 1990, 36 (Suppl. 1), S57−69]. In this study, model solutions of the two main whey proteins, α-lactalbumin and β-lactoglobulin, respectively, were incubated with lactose, and modifications were monitored by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). Lactulosyl residues were the most abundant modifications of α-lactalbumin and β-lactoglobulin. Up to four of these adducts were identified on the proteins. Enzymatical digest with endoproteinase AspN prior to mass spectrometric analysis allowed the detection of further modifications and their localization in the amino acid sequence. Most prominent modifications were lactulosyllysine, Ne-carboxymethyllysine, oxidation of lysine to aminoadipic semialdehyde, oxidation of methionine to methionine sulfoxide, cyclization of N-terminal glutamic acid to ...
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site specific formation of maillard oxidation and condensation products from whey proteins during reaction with lactose
Journal of Agricultural and Food Chemistry, 2007Co-Authors: Jasmin Meltretter, Silke Seeber, Andreas Humeny, Cordmichael Becker, Monika PischetsriederAbstract:Heat treatment of dairy products leads to structural changes of proteins, which can severely decrease the nutritional value [Mauron, J. J. Nutr. Sci. Vitaminol. (Tokyo) 1990, 36 (Suppl. 1), S57-69]. In this study, model solutions of the two main whey proteins, alpha-lactalbumin and beta-lactoglobulin, respectively, were incubated with lactose, and modifications were monitored by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). Lactulosyl residues were the most abundant modifications of alpha-lactalbumin and beta-lactoglobulin. Up to four of these adducts were identified on the proteins. Enzymatical digest with endoproteinase AspN prior to mass spectrometric analysis allowed the detection of further modifications and their localization in the amino acid sequence. Most prominent modifications were lactulosyllysine, Nepsilon-carboxymethyllysine, oxidation of lysine to aminoadipic semialdehyde, oxidation of methionine to methionine sulfoxide, cyclization of N-terminal glutamic acid to a pyrrolidone, and oxidation of cysteine or tryptophan. The presence of methionine oxidation was deduced from a control protein that had been oxidized by hydrogen peroxide. These studies establish MALDI-TOF-MS as a reliable tool to monitor chemical modifications of nutritional proteins during food processing.
Jacob M Haus - One of the best experts on this subject based on the ideXlab platform.
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experimental hyperglycemia alters circulating concentrations and renal clearance of oxidative and advanced glycation end products in healthy obese humans
Nutrients, 2019Co-Authors: Ryan Perkins, Edwin R Miranda, Kristian Karstoft, Paul J Beisswenger, Thomas P J Solomon, Jacob M HausAbstract:The purpose of this investigation was to evaluate the effects of experimental hyperglycemia on oxidative damage (OX), advanced glycation end products (AGEs), and the receptor for AGEs (RAGE) through an in vivo approach. Obese subjects (n = 10; 31.2 ± 1.2 kg·m−2; 56 ± 3 years) underwent 24 h of hyperglycemic clamp (+5.4 mM above basal), where plasma at basal and after 2 h and 24 h of hyperglycemic challenge were assayed for OX (methionine sulfoxide, MetSO, and aminoadipic acid, AAA) and AGE-free adducts (Ne-carboxymethyllysine, CML; Ne-carboxyethyllysine, CEL; glyoxal hydroimidazolone-1, GH-1; methylglyoxal hydroimidazolone-1, MG-H1; and 3-deoxyglucosone hydroimidazolone, 3DG-H) via liquid chromatography–tandem mass spectrometry (LC–MS/MS). Urine was also analyzed at basal and after 24 h for OX and AGE-free adducts and plasma soluble RAGE (sRAGE) isoforms (endogenous secretory RAGE, esRAGE, and cleaved RAGE, cRAGE), and inflammatory markers were determined via enzyme-linked immunosorbent assay (ELISA). Skeletal muscle tissue collected via biopsy was probed at basal, 2 h, and 24 h for RAGE and OST48 protein expression. Plasma MetSO, AAA, CEL, MG-H1, and G-H1 decreased (−18% to −47%; p 0.05) with the hyperglycemic challenge. Renal clearance of MetSO, AAA, and G-H1 increased (599% to 1077%; p 0.05). Fractional excretion of MetSO, AAA, CEL, G-H1, and MG-H1 increased (5.8% to 532%; p 0.05). Muscle RAGE and OST48 expression, plasma sRAGE, IL-1β, IL-1Ra, and TNFα remained unchanged (p > 0.05), while IL-6 increased (159% vs. basal; p > 0.05). These findings suggest that individuals who are obese but otherwise healthy have the capacity to prevent accumulation of OX and AGEs during metabolic stress by increasing fractional excretion and renal clearance.
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Experimental Hyperglycemia Alters Circulating Concentrations and Renal Clearance of Oxidative and Advanced Glycation End Products in Healthy Obese Humans
MDPI AG, 2019Co-Authors: Ryan K. Perkins, Edwin R Miranda, Kristian Karstoft, Paul J Beisswenger, Thomas P J Solomon, Jacob M HausAbstract:The purpose of this investigation was to evaluate the effects of experimental hyperglycemia on oxidative damage (OX), advanced glycation end products (AGEs), and the receptor for AGEs (RAGE) through an in vivo approach. Obese subjects (n = 10; 31.2 ± 1.2 kg·m−2; 56 ± 3 years) underwent 24 h of hyperglycemic clamp (+5.4 mM above basal), where plasma at basal and after 2 h and 24 h of hyperglycemic challenge were assayed for OX (methionine sulfoxide, MetSO, and aminoadipic acid, AAA) and AGE-free adducts (Ne-carboxymethyllysine, CML; Ne-carboxyethyllysine, CEL; glyoxal hydroimidazolone-1, GH-1; methylglyoxal hydroimidazolone-1, MG-H1; and 3-deoxyglucosone hydroimidazolone, 3DG-H) via liquid chromatography–tandem mass spectrometry (LC–MS/MS). Urine was also analyzed at basal and after 24 h for OX and AGE-free adducts and plasma soluble RAGE (sRAGE) isoforms (endogenous secretory RAGE, esRAGE, and cleaved RAGE, cRAGE), and inflammatory markers were determined via enzyme-linked immunosorbent assay (ELISA). Skeletal muscle tissue collected via biopsy was probed at basal, 2 h, and 24 h for RAGE and OST48 protein expression. Plasma MetSO, AAA, CEL, MG-H1, and G-H1 decreased (−18% to −47%; p < 0.05), while CML increased (72% at 24 h; p < 0.05) and 3DG-H remained unchanged (p > 0.05) with the hyperglycemic challenge. Renal clearance of MetSO, AAA, and G-H1 increased (599% to 1077%; p < 0.05), CML decreased (−30%; p < 0.05), and 3DG-H, CEL, and MG-H1 remained unchanged (p > 0.05). Fractional excretion of MetSO, AAA, CEL, G-H1, and MG-H1 increased (5.8% to 532%; p < 0.05) and CML and 3DG-H remained unchanged (p > 0.05). Muscle RAGE and OST48 expression, plasma sRAGE, IL-1β, IL-1Ra, and TNFα remained unchanged (p > 0.05), while IL-6 increased (159% vs. basal; p > 0.05). These findings suggest that individuals who are obese but otherwise healthy have the capacity to prevent accumulation of OX and AGEs during metabolic stress by increasing fractional excretion and renal clearance
Jasmin Meltretter - One of the best experts on this subject based on the ideXlab platform.
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site specific formation of maillard oxidation and condensation products from whey proteins during reaction with lactose
Journal of Agricultural and Food Chemistry, 2007Co-Authors: Jasmin Meltretter, Silke Seeber, Andreas Humeny, Cordmichael Becker, Monika PischetsriederAbstract:Heat treatment of dairy products leads to structural changes of proteins, which can severely decrease the nutritional value [Mauron, J. J. Nutr. Sci. Vitaminol. (Tokyo) 1990, 36 (Suppl. 1), S57−69]. In this study, model solutions of the two main whey proteins, α-lactalbumin and β-lactoglobulin, respectively, were incubated with lactose, and modifications were monitored by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). Lactulosyl residues were the most abundant modifications of α-lactalbumin and β-lactoglobulin. Up to four of these adducts were identified on the proteins. Enzymatical digest with endoproteinase AspN prior to mass spectrometric analysis allowed the detection of further modifications and their localization in the amino acid sequence. Most prominent modifications were lactulosyllysine, Ne-carboxymethyllysine, oxidation of lysine to aminoadipic semialdehyde, oxidation of methionine to methionine sulfoxide, cyclization of N-terminal glutamic acid to ...
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site specific formation of maillard oxidation and condensation products from whey proteins during reaction with lactose
Journal of Agricultural and Food Chemistry, 2007Co-Authors: Jasmin Meltretter, Silke Seeber, Andreas Humeny, Cordmichael Becker, Monika PischetsriederAbstract:Heat treatment of dairy products leads to structural changes of proteins, which can severely decrease the nutritional value [Mauron, J. J. Nutr. Sci. Vitaminol. (Tokyo) 1990, 36 (Suppl. 1), S57-69]. In this study, model solutions of the two main whey proteins, alpha-lactalbumin and beta-lactoglobulin, respectively, were incubated with lactose, and modifications were monitored by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). Lactulosyl residues were the most abundant modifications of alpha-lactalbumin and beta-lactoglobulin. Up to four of these adducts were identified on the proteins. Enzymatical digest with endoproteinase AspN prior to mass spectrometric analysis allowed the detection of further modifications and their localization in the amino acid sequence. Most prominent modifications were lactulosyllysine, Nepsilon-carboxymethyllysine, oxidation of lysine to aminoadipic semialdehyde, oxidation of methionine to methionine sulfoxide, cyclization of N-terminal glutamic acid to a pyrrolidone, and oxidation of cysteine or tryptophan. The presence of methionine oxidation was deduced from a control protein that had been oxidized by hydrogen peroxide. These studies establish MALDI-TOF-MS as a reliable tool to monitor chemical modifications of nutritional proteins during food processing.
Ryan Perkins - One of the best experts on this subject based on the ideXlab platform.
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experimental hyperglycemia alters circulating concentrations and renal clearance of oxidative and advanced glycation end products in healthy obese humans
Nutrients, 2019Co-Authors: Ryan Perkins, Edwin R Miranda, Kristian Karstoft, Paul J Beisswenger, Thomas P J Solomon, Jacob M HausAbstract:The purpose of this investigation was to evaluate the effects of experimental hyperglycemia on oxidative damage (OX), advanced glycation end products (AGEs), and the receptor for AGEs (RAGE) through an in vivo approach. Obese subjects (n = 10; 31.2 ± 1.2 kg·m−2; 56 ± 3 years) underwent 24 h of hyperglycemic clamp (+5.4 mM above basal), where plasma at basal and after 2 h and 24 h of hyperglycemic challenge were assayed for OX (methionine sulfoxide, MetSO, and aminoadipic acid, AAA) and AGE-free adducts (Ne-carboxymethyllysine, CML; Ne-carboxyethyllysine, CEL; glyoxal hydroimidazolone-1, GH-1; methylglyoxal hydroimidazolone-1, MG-H1; and 3-deoxyglucosone hydroimidazolone, 3DG-H) via liquid chromatography–tandem mass spectrometry (LC–MS/MS). Urine was also analyzed at basal and after 24 h for OX and AGE-free adducts and plasma soluble RAGE (sRAGE) isoforms (endogenous secretory RAGE, esRAGE, and cleaved RAGE, cRAGE), and inflammatory markers were determined via enzyme-linked immunosorbent assay (ELISA). Skeletal muscle tissue collected via biopsy was probed at basal, 2 h, and 24 h for RAGE and OST48 protein expression. Plasma MetSO, AAA, CEL, MG-H1, and G-H1 decreased (−18% to −47%; p 0.05) with the hyperglycemic challenge. Renal clearance of MetSO, AAA, and G-H1 increased (599% to 1077%; p 0.05). Fractional excretion of MetSO, AAA, CEL, G-H1, and MG-H1 increased (5.8% to 532%; p 0.05). Muscle RAGE and OST48 expression, plasma sRAGE, IL-1β, IL-1Ra, and TNFα remained unchanged (p > 0.05), while IL-6 increased (159% vs. basal; p > 0.05). These findings suggest that individuals who are obese but otherwise healthy have the capacity to prevent accumulation of OX and AGEs during metabolic stress by increasing fractional excretion and renal clearance.
Silke Seeber - One of the best experts on this subject based on the ideXlab platform.
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site specific formation of maillard oxidation and condensation products from whey proteins during reaction with lactose
Journal of Agricultural and Food Chemistry, 2007Co-Authors: Jasmin Meltretter, Silke Seeber, Andreas Humeny, Cordmichael Becker, Monika PischetsriederAbstract:Heat treatment of dairy products leads to structural changes of proteins, which can severely decrease the nutritional value [Mauron, J. J. Nutr. Sci. Vitaminol. (Tokyo) 1990, 36 (Suppl. 1), S57−69]. In this study, model solutions of the two main whey proteins, α-lactalbumin and β-lactoglobulin, respectively, were incubated with lactose, and modifications were monitored by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). Lactulosyl residues were the most abundant modifications of α-lactalbumin and β-lactoglobulin. Up to four of these adducts were identified on the proteins. Enzymatical digest with endoproteinase AspN prior to mass spectrometric analysis allowed the detection of further modifications and their localization in the amino acid sequence. Most prominent modifications were lactulosyllysine, Ne-carboxymethyllysine, oxidation of lysine to aminoadipic semialdehyde, oxidation of methionine to methionine sulfoxide, cyclization of N-terminal glutamic acid to ...
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site specific formation of maillard oxidation and condensation products from whey proteins during reaction with lactose
Journal of Agricultural and Food Chemistry, 2007Co-Authors: Jasmin Meltretter, Silke Seeber, Andreas Humeny, Cordmichael Becker, Monika PischetsriederAbstract:Heat treatment of dairy products leads to structural changes of proteins, which can severely decrease the nutritional value [Mauron, J. J. Nutr. Sci. Vitaminol. (Tokyo) 1990, 36 (Suppl. 1), S57-69]. In this study, model solutions of the two main whey proteins, alpha-lactalbumin and beta-lactoglobulin, respectively, were incubated with lactose, and modifications were monitored by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). Lactulosyl residues were the most abundant modifications of alpha-lactalbumin and beta-lactoglobulin. Up to four of these adducts were identified on the proteins. Enzymatical digest with endoproteinase AspN prior to mass spectrometric analysis allowed the detection of further modifications and their localization in the amino acid sequence. Most prominent modifications were lactulosyllysine, Nepsilon-carboxymethyllysine, oxidation of lysine to aminoadipic semialdehyde, oxidation of methionine to methionine sulfoxide, cyclization of N-terminal glutamic acid to a pyrrolidone, and oxidation of cysteine or tryptophan. The presence of methionine oxidation was deduced from a control protein that had been oxidized by hydrogen peroxide. These studies establish MALDI-TOF-MS as a reliable tool to monitor chemical modifications of nutritional proteins during food processing.
