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SDS-PAGE Analysis of Soluble Proteins in Reconstituted Milk Exposed to Different Heat Treatments

View Article: PubMed Central

ABSTRACT

This paper deals with the investigation of the impact of the heat treatment of reconstituted skim milk conducted at different temperatures, and the adding of demineralized whey on the protein solubility, soluble protein composition and interactions involved between proteins in a chemical complex. Commercial skim milk has been reconstituted and heat treated at 75°C, 85°C and 90°C for 20 minutes. Demineralized whey has been added in concentrations of 0.5%, 1.0 and 2.0%. The soluble protein composition has been determined by the polyacrilamide gel electrophoresis (SDS-PAGE) and by the densitometric analysis. Due to the different changes occurred during treatments at different temperatures, proteins of heat-treated samples containing added demineralized whey have had significantly different solubility. At lower temperatures (75°C and 85°C) the adding of demineralized whey decreased the protein solubility by 5.28%-26.41%, while the addition of demineralized whey performed at 90°C increased the soluble protein content by 5.61%-28.89%. Heat treatments, as well as the addition of demineralized whey, have induced high molecular weight complex formation. β-Lg, α-La and κ-casein are involved in high molecular weight complexes. The disulfide interactions between denatured molecules of these proteins are mostly responsible for the formation of coaggregates. The level of their interactions and the soluble protein composition are determined by the degree of temperature.

No MeSH data available.


The densitometric analysis of the soluble proteins (without 2-mercaptoethanol) of the reconstituted skim milk.
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f2-sensors-07-00371: The densitometric analysis of the soluble proteins (without 2-mercaptoethanol) of the reconstituted skim milk.

Mentions: The SDS-PAGE profile of soluble proteins of the untreated reconstituted skim milk is shown in Fig.1, while densitometric analysis is shown in fig. 2.


SDS-PAGE Analysis of Soluble Proteins in Reconstituted Milk Exposed to Different Heat Treatments
The densitometric analysis of the soluble proteins (without 2-mercaptoethanol) of the reconstituted skim milk.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3756726&req=5

f2-sensors-07-00371: The densitometric analysis of the soluble proteins (without 2-mercaptoethanol) of the reconstituted skim milk.
Mentions: The SDS-PAGE profile of soluble proteins of the untreated reconstituted skim milk is shown in Fig.1, while densitometric analysis is shown in fig. 2.

View Article: PubMed Central

ABSTRACT

This paper deals with the investigation of the impact of the heat treatment of reconstituted skim milk conducted at different temperatures, and the adding of demineralized whey on the protein solubility, soluble protein composition and interactions involved between proteins in a chemical complex. Commercial skim milk has been reconstituted and heat treated at 75°C, 85°C and 90°C for 20 minutes. Demineralized whey has been added in concentrations of 0.5%, 1.0 and 2.0%. The soluble protein composition has been determined by the polyacrilamide gel electrophoresis (SDS-PAGE) and by the densitometric analysis. Due to the different changes occurred during treatments at different temperatures, proteins of heat-treated samples containing added demineralized whey have had significantly different solubility. At lower temperatures (75°C and 85°C) the adding of demineralized whey decreased the protein solubility by 5.28%-26.41%, while the addition of demineralized whey performed at 90°C increased the soluble protein content by 5.61%-28.89%. Heat treatments, as well as the addition of demineralized whey, have induced high molecular weight complex formation. β-Lg, α-La and κ-casein are involved in high molecular weight complexes. The disulfide interactions between denatured molecules of these proteins are mostly responsible for the formation of coaggregates. The level of their interactions and the soluble protein composition are determined by the degree of temperature.

No MeSH data available.