Viscosity, thickeners and gels - Gels from globular proteins
10 important questions on Viscosity, thickeners and gels - Gels from globular proteins
Which 2 methods can be used to make cold-set gels?
- Heat proteins to make aggregates, without making a gel. After cooling down, the pH of the solution can be adjusted (to around the pI of the protein) to induce formation of clusters from the pre-formed aggregates. These clusters then connect further (if the concentration is high enough) and form a gel.
- Based on (partial) hydrolysis of the proteins. Partial hydrolysis results in the formation of peptides that do not have the globular structure anymore. They may have more exposed hydrophobicity. If the pH of the hydrolysates are then adjusted to lower values, also a gel may be formed.
What is the denaturation temperature dependent on?
How are the shape of aggregates and the electrostatic interactions related?
Little electrostatic repulsion --> random aggregates
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How are the shape of aggregates and the appearance of the gel related?
How are electrostatic interactions, ionic strength, pH, aggregate structure and gel appearance related?
- electrostatic repulsion
- pH far from pI
- low ionic strength
- linear aggregates
- transparent appearance
- electrostatic attraction (low repulsion)
- pH = pI
- high ionic strength
- random aggregates (very branched)
- turbid appearance (scatters more light)
How are ionic strength and gel strength related?
What kind of interactions are important for the gel strength (the stability of the protein structure)?
What happens upon heating with the disulphide bridges?
What is the effect of hydrolysis on the gel strength?
If hydrolysis is less extreme, the peptides may still be large enough to aggregate, and form a network and gel.
How are the pH and the degree of hydrolysis related to the gel strength?
Hydrolysed --> gels are formed at higher pH values due to not 1 pI value
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