Protein modifications - Heating: Changes in protein tertiary or quarternary structure
5 important questions on Protein modifications - Heating: Changes in protein tertiary or quarternary structure
Caseins cannot unfold, as they do not have a secondary or tertiary structure, however the native structure of the casein macro-micelle can be disrupted by heating, how do you call this and what happens then?
The total extent of aggregation of globular proteins depends a lot on the conditions, such as?
- Concentration. In highly diluted systems, the proteins will not meet each other frequently. Whereas in concentrated systems the collision frequency is much higher.
- Electrostatic repulsion influences type of aggregates formed. Changing the pH of the solution, towards the pI --> aggregation can also occur when they are in their globular state, without unfolding.
What is the denaturation temperature?
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What happens during spray-drying of proteins?
- Evaporation of water effectively cools down the droplet, slightly delaying the increase of temperature in the droplet
- As the water evaporates, the water activity in the droplet goes down, which results in an increase of denaturation temperature of the proteins
Why are there particle that do not dissolve after spray-drying of proteins?
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