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Stephane Guilbert - One of the best experts on this subject based on the ideXlab platform.
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mechanical and water barrier properties of Corn Protein based biodegradable plastics
Journal of Materials Research, 2000Co-Authors: Lodovico Di Gioia, Stephane GuilbertAbstract:Experiments were performed to evaluate the mechanical and water barrier properties of Corn-Protein-based materials that were compression molded from thermoplastic resins. The influence of varying concentrations of water, glycerol, and octanoic acid was studied. At 0% relative humidity, the material exhibited a linear elastic deformation and a brittle fracture at any glycerol or octanoic acid content. Raising relative humidity from 0% to 97.3%, progressively decreased the tensile strength (from 24.1 to 2.2 MPa and 19.4 to 1.0 MPa), and the modulus of elasticity (from 1.67 to 0.03 GPa and 1.87 to 0.13 GPa), respectively, for the octanoic acid- or glycerol-plasticized materials. Increasing water content did not increase the tensile strain at break of the glycerol-plasticized material, whereas this parameter changed from 1.6 to 52.3% for octanoic-acid-plasticized material. This last material was waterproof during 21 h and its water transmission rate was then 0.05 mmolmm -2 s -1 . Differences in water absorption were related to plasticizer solubility and material structure.
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Corn Protein based thermoplastic resins effect of some polar and amphiphilic plasticizers
Journal of Agricultural and Food Chemistry, 1999Co-Authors: L Di Gioia, Stephane GuilbertAbstract:Homogeneous blends of Corn gluten meal (CGM) and “polar” plasticizers (water, glycerol) or “amphiphilic” plasticizers [octanoic and palmitic acids, dibutyl tartrate and phthalate, and diacetyl tartaric acid ester of mono-diglycerides (DATEM)] were obtained by a hot-mixing procedure. The glass transition temperature (Tg) of the blends was measured by modulated differential scanning calorimetry and dynamic mechanical thermal analysis, as a function of plasticizer type and content (0−30%, dwb). The plasticizing efficiency (i.e., decrease of Tg) at equal molar content was found to be proportional to the molecular weight and inversely proportional to the percent of hydrophilic groups of the plasticizer. The migration rate of the plasticizers in the polymer was related to their physicochemical characteristics. It was assumed that polar substances interacted with readily accessible polar amino acids, whereas amphiphilic ones interacted with nonpolar zones, which are buried and accessible with difficulty. The tem...
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Corn Protein based thermoplastic resins effect of some polar and amphiphilic plasticizers
Journal of Agricultural and Food Chemistry, 1999Co-Authors: L Di Gioia, Stephane GuilbertAbstract:Homogeneous blends of Corn gluten meal (CGM) and "polar" plasticizers (water, glycerol) or "amphiphilic" plasticizers [octanoic and palmitic acids, dibutyl tartrate and phthalate, and diacetyl tartaric acid ester of mono-diglycerides (DATEM)] were obtained by a hot-mixing procedure. The glass transition temperature (T(g)) of the blends was measured by modulated differential scanning calorimetry and dynamic mechanical thermal analysis, as a function of plasticizer type and content (0-30%, dwb). The plasticizing efficiency (i.e., decrease of T(g)) at equal molar content was found to be proportional to the molecular weight and inversely proportional to the percent of hydrophilic groups of the plasticizer. The migration rate of the plasticizers in the polymer was related to their physicochemical characteristics. It was assumed that polar substances interacted with readily accessible polar amino acids, whereas amphiphilic ones interacted with nonpolar zones, which are buried and accessible with difficulty. The temperature at which a thermoplastic resin of plasticized CGM could be formed was closely connected to the T(g) of the blend.
Tibor Cserháti - One of the best experts on this subject based on the ideXlab platform.
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Quantitative Structure‐Retention Relationship Study on the Binding of Organic Solvents to the Corn Protein, Zein
Journal of Liquid Chromatography & Related Technologies, 2007Co-Authors: Monika Zagyi, Tibor CserhátiAbstract:The strength and the character of the binding of 12 organic solvents to the Corn Protein zein were determined by high performance liquid chromatography. The relationship between the physicochemical parameters and binding characteristics of solvents was elucidated by canonical correlation analyses (CCA). As the number of physicochemical parameters was higher than that of our observations, three empirical methods have been employed for the preselection of variables exerting a marked impact on the binding characteristics. Calculations established that the binding of solvents to the Protein is of mixed characters involving hydrophobic and electrostatic interactive forces. Sterical correspondence between the interacting molecules and molecular substructures also influence the binding of solvents to zein. The use of different preselection methods resulted in similar but not identical relationships.
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Effect of pH and salts on the binding of free amino acids to the Corn Protein zein studied by thin-layer chromatography.
Amino acids, 2004Co-Authors: Tibor Cserháti, Esther ForgácsAbstract:The interaction of free amino acids with the Corn Protein zein was studied by thin-layer chromatography carried out on cellulose layers covered with zein and the effect of pH and salts on the strength of interaction was elucidated. Only the binding of Arg, His, Lys, Orn and Trp to zein was verified, other amino acids were not retained. Retention of Arg, His, Lys and Orn decreased linearly with increasing concentration of salts the mobile phase indicating the hydrophilic character of amino acid–zein interaction. Both alkaline and acidic pH influenced the strength of binding. Principal component analysis indicated the different character of the influence of pH and salts on the interaction. The results suggest that these amino acid residues may account for the binding of other peptides and Proteins to zein.
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Effect of salts on the binding of some environmental pollutants to Corn Protein zein studied by HPLC.
Environmental science & technology, 2003Co-Authors: Monika Zagyi, Tibor Cserháti, Esther Forgács, Miklos Prodan, Zoltán IllésAbstract:The strength and the character of the binding of 14 organic solvents to the Corn Protein zein in distilled water and in various salt solutions were determined by preparing zein-coated carbon stationary phase and by measuring the retention characteristics of solvents on a high-performance liquid chromatographic column filled with this stationary phase. The relationship between the physicochemical parameters and binding characteristics of solvents was elucidated by principal component analysis. It was established that various interactive forces are involved in the binding of solvent to the Protein, suggesting a mixed binding mechanism. Binding characteristics are equally influenced by the molecular hydrophobicity and by the polarity parameters of the solvent. Coordination numbers, ionization, and lattice energies of the monovalent cations significantly influenced the various aspects of the binding of organic solvents to zein.
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Binding of environmental pollutants to the Corn Protein zein studied by high-performance liquid chromatography.
Journal of chromatography. A, 2003Co-Authors: Tibor Cserháti, Esther Forgács, Zdenek Deyl, Ivan Miksik, Adam EckhardtAbstract:The interaction of 16 ring-substituted phenols and anilines with the Corn Protein zein was studied by reversed-phase high-performance liquid chromatography by preparing silica- and alumina-based stationary phases coated with various concentrations of zein. The relationship between the strength of interaction and the physicochemical parameters of solutes was elucidated by principal component analysis followed by the nonlinear mapping technique. The binding of each phenol and aniline derivative to zein has been demonstrated. It was established that the electrostatical parameters of solutes exert the highest influence on the interaction and the involvement of hydrophobic binding forces is of secondary importance. The binding characteristics of phenol and aniline derivatives were different.
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TLC study of the binding of nonionic surfactants to the Corn Protein zein
Journal of Liquid Chromatography & Related Technologies, 2003Co-Authors: Tibor Cserháti, E. Forgács, Zoltán IllésAbstract:Abstract The binding of 18 nonionic surfactants with various lengths of apolar ethylene oxide chains to the Corn Protein zein was studied by thin‐layer chromatography (TLC) carried out on alumina layers covered with zein, and the effect of methanol, monovalent cations, and pH on the strength and selectivity of interaction was elucidated by using the spectral mapping technique and stepwise regression analysis. The binding of surfactants to zein has been demonstrated. It has been established that the number of hydrophilic ethylene oxide units in the surfactant molecule exerts the highest influence on the strength of interaction, and that the role of methanol and salt concentration is of secondary importance. The character of the cation and pH influenced both the strength and selectivity of the surfactant–zein interaction.
Esther Forgács - One of the best experts on this subject based on the ideXlab platform.
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Effect of pH and salts on the binding of free amino acids to the Corn Protein zein studied by thin-layer chromatography.
Amino acids, 2004Co-Authors: Tibor Cserháti, Esther ForgácsAbstract:The interaction of free amino acids with the Corn Protein zein was studied by thin-layer chromatography carried out on cellulose layers covered with zein and the effect of pH and salts on the strength of interaction was elucidated. Only the binding of Arg, His, Lys, Orn and Trp to zein was verified, other amino acids were not retained. Retention of Arg, His, Lys and Orn decreased linearly with increasing concentration of salts the mobile phase indicating the hydrophilic character of amino acid–zein interaction. Both alkaline and acidic pH influenced the strength of binding. Principal component analysis indicated the different character of the influence of pH and salts on the interaction. The results suggest that these amino acid residues may account for the binding of other peptides and Proteins to zein.
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Effect of salts on the binding of some environmental pollutants to Corn Protein zein studied by HPLC.
Environmental science & technology, 2003Co-Authors: Monika Zagyi, Tibor Cserháti, Esther Forgács, Miklos Prodan, Zoltán IllésAbstract:The strength and the character of the binding of 14 organic solvents to the Corn Protein zein in distilled water and in various salt solutions were determined by preparing zein-coated carbon stationary phase and by measuring the retention characteristics of solvents on a high-performance liquid chromatographic column filled with this stationary phase. The relationship between the physicochemical parameters and binding characteristics of solvents was elucidated by principal component analysis. It was established that various interactive forces are involved in the binding of solvent to the Protein, suggesting a mixed binding mechanism. Binding characteristics are equally influenced by the molecular hydrophobicity and by the polarity parameters of the solvent. Coordination numbers, ionization, and lattice energies of the monovalent cations significantly influenced the various aspects of the binding of organic solvents to zein.
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Binding of environmental pollutants to the Corn Protein zein studied by high-performance liquid chromatography.
Journal of chromatography. A, 2003Co-Authors: Tibor Cserháti, Esther Forgács, Zdenek Deyl, Ivan Miksik, Adam EckhardtAbstract:The interaction of 16 ring-substituted phenols and anilines with the Corn Protein zein was studied by reversed-phase high-performance liquid chromatography by preparing silica- and alumina-based stationary phases coated with various concentrations of zein. The relationship between the strength of interaction and the physicochemical parameters of solutes was elucidated by principal component analysis followed by the nonlinear mapping technique. The binding of each phenol and aniline derivative to zein has been demonstrated. It was established that the electrostatical parameters of solutes exert the highest influence on the interaction and the involvement of hydrophobic binding forces is of secondary importance. The binding characteristics of phenol and aniline derivatives were different.
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Binding of some environmental pollutants to Corn Protein zein studied by high-performance liquid chromatography.
Analytical sciences : the international journal of the Japan Society for Analytical Chemistry, 2003Co-Authors: Monika Zagyi, Tibor Cserháti, Esther Forgács, Miklos Prodan, Dušan BerekAbstract:The strength and the character of the binding of 12 organic solvents to the Corn Protein zein was determined by preparing zein-coated carbon stationary phase and by measuring the retention of solvents on a high-performance liquid chromatographic column filled with this stationary phase. The relationship between the physicochemical parameters and binding characteristics of solvents was elucidated by principal component analysis. Various interactive forces are involved in the binding of solvent to the Protein. The strength of the binding is dominantly influenced by the molecular hydrophobicity while the Gaussian or non-Gaussian distribution of the adsorption strength is markedly dependent on the polarity parameters of the solvent. Sterical correspondences exerted considerable influence on each binding parameter.
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Effect of pH and Salts on the Binding of Ring‐Substituted Phenol Derivatives to the Corn Protein Zein, Studied by Thin‐Layer Chromatography
Journal of Liquid Chromatography & Related Technologies, 2003Co-Authors: Tibor Cserháti, Esther ForgácsAbstract:Abstract The interaction of seven ring‐substituted phenol derivatives with the Corn Protein zein was studied by reversed‐phase thin‐layer chromatography (RP‐TLC) carried out on zein‐impregnated cellulose layers, and the effect of pH and salts on the strength and selectivity of the interaction was determined and elucidated by using spectral mapping techniques (SPM) and stepwise regression analysis (SRA). The binding of each phenol derivative to zein has been demonstrated. Calculations proved that the electron withdrawing capacity of substituents and the molecular hydrophobicity of phenol derivatives exert the highest influence on the phenol–zein binding indicating the mixed character of the interaction.
Zhao Wen-yan - One of the best experts on this subject based on the ideXlab platform.
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Comprehensive utilization of Corn gluten meal
Food engineering, 2014Co-Authors: Zhao Wen-yanAbstract:Corn gluten meal is one of the by-products of the processing of Corn starch. It contains Protein,starch,and maize yellow pigment. Zein is a natural preservative and can be extracted by ethanol or ultrasonic methods. Maize yellow pigment can be extracted by organic solvents,enzymes,and ultrasonic extraction. Corn Protein was used to produce bioactive peptides by enzymatic hydrolysis. The bioactive peptide has health function.
D. Allen Davis - One of the best experts on this subject based on the ideXlab platform.
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Comparative effect of advanced soy products or Corn Protein concentrate with porcine meal on growth, body composition, and distal intestine histology of Florida pompano, Trachinotus carolinus
Journal of the World Aquaculture Society, 2018Co-Authors: Romi Novriadi, Elizabeth Spangler, D. Allen DavisAbstract:The present study was designed to investigate the effects of diets containing advanced soy products (enzyme‐treated soy and fermented soy) or Corn Protein concentrate (CPC) in combination with porcine meal (PM) to completely replace poultry byproduct meal (PBM) on growth performance, body composition, and distal intestine histology of Florida pompano, Trachinotus carolinus. Four experimental diets were formulated to be isonitrogenous and isolipidic, to contain 400 g/kg crude Protein and 80 g/kg lipid. A reference diet (PBM diet [PBMD]) contained 150 g/kg PBM and 495 g/kg soybean meal (SBM), and three test diets were formulated replacing PBM with 15 g/kg of CPC (CPC diet [CPCD]) or replacing all SBM and PBM with 535 g/kg fermented soy (fermented soybean meal diet [FSBMD]) or 451.3 g/kg enzyme‐treated soy (enzyme‐treated soybean meal diet [ESBMD]). All three test diets were supplemented with 38 g/kg of PM. Diets were fed based on a percentage of bodyweight adjusted after sampling the fish every 2 weeks to triplicate groups of Florida pompano juveniles (mean weight 8.06 ± 0.22 g). After 8 weeks of feeding, fish fed CPCD and ESBMD performed equally well in terms of final body weight, thermal growth coefficient, and percentage weight gain in comparison to fish fed PBMD. In all cases, feeding FSBMD resulted in poor feed conversion and lower feed intake compared to other treatments. Protein retention efficiency, whole‐body proximate composition, phosphorus, sulfur, potassium, magnesium, calcium, sodium, and zinc contents were not significantly influenced by the dietary treatments. The results obtained in the present histological study showed no significant differences in the thickness of serous layer, muscular layer, and submucosal layer of the intestine among treatments. Fish fed CPCD showed a significant widening of the lamina propria with an increase of cellular infiltration and higher presence of goblet cells compared to other dietary treatment. Based on these results, 451 g/kg ESBM or combination of 150 g/kg of CPC and 495 g/kg SBM supplemented with 38 g/kg PM can be utilized to develop a practical diet for juvenile Florida pompano without impacting growth, nutritive parameters, and several distal intestine health parameters.
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Comparison of crystalline lysine and intact lysine used as a supplement in practical diets of channel catfish (Ictalurus punctatus) and Nile tilapia (Oreochromis niloticus)
Aquaculture, 2016Co-Authors: Lay Nguyen, D. Allen DavisAbstract:Abstract The study was conducted using channel catfish and tilapia to evaluate the production performance of these fish to increasing levels of lysine from crystalline and intact lysine supplemented in practical diets. A practical lysine deficient basal diet was developed using Corn Protein concentrate (Empyreal® 75) as a primary Protein source. To this diet either graded levels of crystalline lysine or similar levels from a high lysine Corn Protein concentrate (Lysto™) were added. In the channel catfish trial, the first five diets were designed to contain increasing levels of crystalline lysine (1.21%, 1.34%, 1.45%, 1.56%, and 1.72%) with an additional four diets using intact Protein from a high lysine Corn Protein concentrate (1.40%, 1.57%, 1.77%, and 1.91% lysine). In the tilapia trial, lysine from two sources was added to 11 diets to produce analyzed lysine levels of 0.92%, 1.11%, 1.23%, 1.34%, 1.54% 1.65% in the first six diets using crystalline lysine and 1.13%, 1.38%, 1.61%, 1.81%, 2.02% in the last five diets using intact lysine. Results indicated that channel catfish and tilapia have positive performance with increasing lysine supplementation up to the requirement. Fish fed with the higher levels of lysine had the highest weight gain and lowest feed conversion ratio. The regression analysis on the increased level of inclusion of crystalline lysine and intact lysine showed no significant difference in slope. Based on the growth, feed conversion ratio and apparent net Protein retention data obtained from this study, it can be concluded that the effectiveness of using intact lysine via high lysine Corn Protein concentrate as a lysine supplement is not significantly different from crystalline lysine. Thus, the high lysine Corn Protein concentrate is a feasible ingredient for aquaculture feeds, which can be used to balance the amino acid composition of the diet without addition of crystalline lysine. Statement of relevance Present study shows that high lysine Corn Protein concentrate is a feasible ingredient for aquaculture feeds, which can be used to balance the amino acid composition of the diet without addition of crystalline lysine.