Process for producing beta-lactoglobulin isolates and related methods and uses
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example 1
f Analysis
Example 1.1: Determination of Protein Nativeness by Intrinsic Tryptophan Fluorescence
[0952]Tryptophan (Trp) fluorescence spectroscopy is a well-described tool to monitor protein folding and unfolding. Trp residues buried within native proteins typically display highest fluorescence emission around 330 nm than when present in more solvent exposed positions such as unfolded proteins. In unfolded proteins, the wavelengths for Trp fluorescence emission typically shift to higher wavelengths and are often measured around 350 nm. We here exploit this transition to monitor thermally induced unfolding by calculating the ratio between fluorescence emission at 330 nm and 350 nm to investigate the influence of heating temperature.
[0953]The analysis comprises the following steps:[0954]Beverage compositions were diluted to 0.6 mg / ml in MQ water.[0955]300 μl sample was transferred to white 96-well plate avoiding bubbles or 3 mL was transferred to 10 mm quartz cuvette.[0956]The tryptophan...
example 1.2
ity at pH 3.9
[0961]Heat-Stability at pH 3.9:
[0962]The heat-stability at pH 3.9 is a measure of the ability of protein composition to stay clear upon prolonged pasteurization at pH 3.9.
[0963]The heat-stability at pH 3.9 is determined by forming an aqueous solution having a pH of 3.9 and comprising 6.0% w / w protein by mixing a sample of the powder or liquid to be tested with water (or alternatively concentrating it by low temperature evaporation if it is a dilute liquid) and adjusting the pH to 3.9 with the minimum amount of 0.1 M NaOH or 0.1 M HCl required.
[0964]The pH-adjusted mixture is allowed to rest for 30 minutes after which 25 mL of the mixture is transferred to a 30 mL thin-walled glass test tube. It is heated to 75.0 degrees C. for 300 seconds by immersion into a water-bath having a temperature of 75.0 degrees C. Immediately after the heating, the glass test tube is cooled to 1-5 degrees C. by transferring it to an ice bath and the turbidity of the heat-treated sample is mea...
example 1.3
on of the Degree of Protein Denaturation of a Whey Protein Composition
[0965]Denatured whey protein is known to have a lower solubility at pH 4.6 than at pH values below or above pH 4.6, therefore the degree of denaturation of a whey protein composition is determined by measuring the amount of soluble protein at pH 4.6 relative to the total amount of protein at a pH where the proteins in the solution are stable.
[0966]More specifically for whey proteins, the whey protein composition to be analysed (e.g. a powder or an aqueous solution) is converted to:[0967]a first aqueous solution containing 5.0% (w / w) total protein and having a pH of 7.0 or 3.0, and[0968]a second aqueous solution containing 5.0% (w / w) total protein and having a pH of 4.6.
[0969]pH adjustments are made using 3% (w / w) NaOH (aq) or 5% (w / w) HCI (aq).
[0970]The total protein content (PpH 7.0 or 3.0) of the first aqueous solution is determined according to example 1.5.
[0971]The second aqueous solution is stored for 2 h at ...
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