Differences in denaturation of genetic variants of soy glycinin.

In heat denaturation studies conducted in the past the genetic variants of glycinin have been considered as a homogeneous group of proteins. In this work the validity of this assumption was tested. It was found by calorimetric studies that glycinin denatures heterogeneously at pH 7.

Comparison of content in phenolic compounds, polyphenol oxidase, and peroxidase in grains of fifty sorghum varieties from burkina faso.

Analysis of fifty sorghum [Sorghum bicolor (L.) Moench] varieties used in Burkina Faso showed that they have different contents of phenolic compounds, peroxidase (POX), and polyphenol oxidase (PPO). Most of the varieties (82%) had a tannin content less than 0.

Effects of ethanol on structure and solubility of potato proteins and the effects of its presence during the preparation of a protein isolate.

In this study, a protein isolate with a high solubility at neutral pH was prepared from industrial potato juice by precipitation at pH 5 in the presence of ethanol. The effects of ethanol itself and the effects of its presence during precipitation on the properties of various potato protein fractions were examined. The presence of ethanol significantly reduced the denaturation temperature of potato proteins, indicating that the preparation of this potato protein isolate should be performed at low temperature in order to retain a high solubility.

Correlations between biochemical characteristics and foam-forming and -stabilizing ability of whey and casein hydrolysates.

Whey protein and casein were hydrolyzed with 11 commercially available enzymes. Foam properties of 44 samples were measured and were related to biochemical properties of the hydrolysates using statistical data analysis. All casein hydrolysates formed high initial foam levels, whereas whey hydrolysates differed in their foam-forming abilities.

Horseradish peroxidase-catalyzed oligomerization of ferulic acid on a template of a tyrosine-containing tripeptide.

Ferulic acid (FA) is an abundantly present phenolic constituent of plant cell walls. Kinetically controlled incubation of FA and the tripeptide Gly-Tyr-Gly (GYG) with horseradish peroxidase and H2O2 yielded a range of new cross-linked products. Two predominant series of hetero-oligomers of FA linked by dehydrogenation to the peptidyl tyrosine were characterized by electrospray ionization (tandem) mass spectrometry.

Isolation and characterization of undenatured chlorogenic acid free sunflower (Helianthus annuus) proteins.

A method for obtaining sunflower protein (SFP) isolate, nondenatured and free of chlorogenic acid (CGA), has been developed. During the isolating procedure, the extent of CGA removal and protein denaturation was monitored. The defatted flour contained 2.

Effect of heat-induced aggregation on the IgE binding of patatin (Sol t 1) is dominated by other potato proteins.

The interaction of the major potato allergen patatin, Sol t 1, with IgE was investigated on a quantitative level as a function of heat treatment at different temperatures. On the basis of a number of publications, potato is considered to be a heat-labile allergen, but the molecular explanation for this behavior was not given. In this work, heat treatment of patatin in the absence and presence of other potato proteins mimicking the proteinaceous environment of the potato was studied.

Emulsion properties of casein and whey protein hydrolysates and the relation with other hydrolysate characteristics.

Casein and whey protein were hydrolyzed using 11 different commercially available enzyme preparations. Emulsion-forming ability and emulsion stability of the digests were measured as well as biochemical properties with the objective to study the relations between hydrolysate characteristics and emulsion properties. All whey protein hydrolysates formed emulsions with bimodal droplet size distributions, signifying poor emulsion-forming ability.

Effects of pH and heat treatments on the structure and solubility of potato proteins in different preparations.

The soluble potato proteins are mainly composed of patatin and protease inhibitors. Using DSC and both far-UV and near-UV CD spectroscopy, it was shown that potato proteins unfold between 55 and 75 degrees C. Increasing the ionic strength from 15 to 200 mM generally caused an increase in denaturation temperature.

Enzymatic extractability of soybean meal proteins and carbohydrates: heat and humidity effects.

To study the incomplete enzymatic extractability of proteins and carbohydrates of thermally treated soybean meals, one unheated and three heat-treated soybean meals were produced. To obtain truly enzyme-resistant material, the meals were extracted by a repeated hydrolysis procedure using excessive concentrations of different combinations of commercial protease and carbohydrase preparations. The water extractability of protein from the different meals varied considerably (13-67%).

Relative abundance and inhibitory distribution of protease inhibitors in potato juice from cv. Elkana.

Protease inhibitors from potato juice of cv. Elkana were purified and quantified. The protease inhibitors represent ca.

Peroxidase-mediated cross-linking of a tyrosine-containing peptide with ferulic acid.

The tyrosine-containing peptide Gly-Tyr-Gly (GYG) was oxidatively cross-linked by horseradish peroxidase in the presence of hydrogen peroxide. As products, covalently coupled di- to pentamers of the peptide were identified by LC-MS. Oxidative cross-linking of ferulic acid with horseradish peroxidase and hydrogen peroxide resulted in the formation of dehydrodimers.

Inactivation Kinetics Study of the Kunitz Soybean Trypsin Inhibitor and the Bowman-Birk Inhibitor.

The inactivation of trypsin inhibitors (TIs) in soy flour exhibits a two-phase inactivation behavior. It is sometimes assumed that this behavior is caused by a difference in the heat stabilities of the Kunitz soybean trypsin inhibitor (KSTI) and the Bowman-Birk inhibitor (BBI). Kinetics studies with KSTI and BBI in soy flour showed that this two-phase inactivation behavior of TIs could not be explained by the difference in the heat stabilities of KSTI and BBI.

Heat denaturation of soy glycinin: influence of pH and ionic strength on molecular structure.

The 7S/11S glycinin equilibrium as found in Lakemond et al. (J. Agric.

Soy glycinin: influence of pH and ionic strength on solubility and molecular structure at ambient temperatures.

This study describes the relationship between the solubility of glycinin, a major soy protein, and its structural properties at a quaternary, tertiary, and secondary folding level under conditions representative for food products. When the ionic strength is lowered from 0.5 to 0.

The effect of pH on heat denaturation and gel forming properties of soy proteins.

This study is focussed on the influence of pH on the gel forming properties of soy protein isolate and purified glycinin in relation to denaturation and aggregation. At pH 7.6 more fine-stranded gels were formed characterised by low G' values, and a smooth, slightly turbid appearance, whereas at pH 3.

Dephosphorylation-induced structural changes in beta-casein and its amphiphilic fragment in relation to emulsion properties.

To promote the understanding of the relationship between emulsifying and molecular properties of proteins/peptides, intact beta-casein (betaCN) and its amphipathic fragment, i.e., betaCN (1-105/107) were dephosphorylated.

Thermal aggregation of patatin studied in situ.

In this work dynamic light scattering was used to study the thermal aggregation of patatin in situ, to elucidate the physical aggregation mechanism of the protein and to be able to relate the aggregation behavior to its structural properties. The dependence of the aggregation rates on the temperature and the ionic strength suggested a mechanism of slow coagulation, being both diffusion and chemically limited. The aggregation rate dependence on the protein concentration was in accordance with the mechanism proposed.

Kinetic modeling of the thermal aggregation of patatin.

A kinetic model of the thermal aggregation of patatin is presented based on chromatographic analysis of the proportions of nonaggregated and aggregated patatin. It was observed that the decrease of the amount of nonaggregated patatin proceeded initially quickly and was followed by slower aggregation at longer incubation times. It was shown that this behavior was not due to heterogeneity of the starting material.

Isolation and characterization of patatin isoforms.

Patatin has, so far, been considered a homogeneous group of proteins. A comparison of the isoforms in terms of structural properties or stability has not been reported. A method to obtain various isoform fractions as well as a comparison of the physicochemical properties of these pools is presented.

beta-lactoglobulin hydrolysis. 2. Peptide identification, SH/SS exchange, and functional properties of hydrolysate fractions formed by the action of plasmin.

beta-Lactoglobulin (betaLg) was hydrolyzed by plasmin to a degree of hydrolysis of 4%. The hydrolysate was fractionated by ion-exchange chromatography and subsequent hydrophobic-interaction chromatography. The betaLg peptide fraction consisting of smaller peptides (mostly <2 kDa) had poor foam- and emulsion-forming and -stabilizing properties.

beta-lactoglobulin hydrolysis. 1. Peptide composition and functional properties of hydrolysates obtained by the action of plasmin, trypsin, and Staphylococcus aureus V8 protease.

beta-Lactoglobulin (betaLg) was subjected to limited hydrolysis by trypsin, plasmin, and endoproteinase from Staphylococcus aureus V8 (S.aur.V8) to degrees of hydrolysis (DH) of 1, 2, and 4%.

Functionality of beta-casein peptides: importance of amphipathicity for emulsion-stabilizing properties.

To investigate structure-function relationships with regard to emulsion-stabilizing properties, peptides from bovine beta-casein (betaCN), obtained by plasmin hydrolysis and fractionation of the hydrolysate, were isolated and identified on the basis of their masses determined by electrospray ionization mass spectrometry, the primary structure of the intact protein, and the known specificity of the enzyme. An amphipathic peptide fraction was fractionated further by ion-exchange chromatography and subsequent hydrophobic interaction chromatography resulting in the components betaCN[f 1-105/107] and betaCN[f 29-105/107]. The latter peptides had poor emulsion-stabilizing properties compared to the former ones, and the stability of an emulsion formed with betaCN[f 29-105/107] was also more sensitive to hydrophobic impurities than that of an emulsion formed with betaCN[f 1-105/107].

The adsorption-induced secondary structure of beta-casein and of distinct parts of its sequence in relation to foam and emulsion properties.

Changes in the secondary structure upon adsorption of beta-casein (betaCN) and of distinct parts of its sequence were investigated by far-ultraviolet circular dichroism in order to find suggested relationships with foam and emulsion-forming and -stabilising properties of the same protein/peptides. A teflon/water interface was used as a model system for foam and emulsion interfaces. The maximum surface loads of beta-casein and its derived peptides were investigated.