Proteins - Characterization of hydrolysates
11 important questions on Proteins - Characterization of hydrolysates
What is the problem with studying protein hydrolysates of food products?
Not populair anymore since they use animals.
However in vivo is hard because there are many properties that you need so simulate. So it is hard to connect your data to the body.
What is the downside of a multifactorial design?
What are the main questions of protein hydrolysis?
- What happens during hydrolysis
- How do the conditions affect the outcome.
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How manny compleces can a protein have?
For beta-casein – PrtP1 around 30 possible cutting sites
have been identified so 496possible peptides
How do you used the pH stat method to determine the degree of hydrolysation?
During hydrolysis:
- Release of COOH and NH2 groups
- Depending on pH: Release of protons (COO-) or uptake of protons (NH3+) from solution
- pH stat: Automatic re-adjustment of pH by addition of HCl / NaOH
What are the 2 types of meganisms for protein hydrolysation?
V8 is for globular proteins. First one protein is hydrolyzed completely and then the next. Gives a shallow slope.
BLP is for random coil proteins. More proteins are hydrolyzed at the same time. Gives a steep slope.
How can you measure the molecular weight distribution of the peptides?
- RP-UPLC (-UV / - MS) (at alkaline or udner reduced conditions)
- Size-exclusion chromatography (at natural conditions)
For what is knowing the molecular weight distribution of use?
How do they use MALDI-TOF-MS for identification of peptides?
How do they use LC-MS for identification of peptides?
How does the quantification of peptides go?
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