Question

If a protein is partially hydrolyzed, e.g. through trypsin digestion, how would you expect the results of this assay to change? On the other hand, how would you expect the results of the assay to change if a protein was glycated e.g. with maltodextrin?

Answer 1

Partial hydrolysis of protein by enzyme trypsin increased solubility of protein in water. in optimal condition for the enzyme reaction

However some amino acid like lysine and arginine are not soluble as it were peptide bound. it forms precipitate of peptide mixture which cannot be solubilized by urea, mercaptoethanol or sodium dodecyl sulphate

Enzymatic hydrolysis may release short peptides and polypeptides that have improved functionality, such as enhanced surface properties. Also bioactive peptides, such as angiotensin converting enzyme (ACE) inhibitory peptides, can be released upon hydrolysis. Limited hydrolysis is not sufficient to ensure the cleavage of all potential epitopes. On the other hand, extensive hydrolysis can reduce protein allergenicity.

Through Maillard-induced glycation it can be reduced. The initial stage of the Maillard reaction induces a covalent linkage between an amine group of a protein and a reducing carbonyl end of a carbohydrate to produce a glycated protein. This glycation may alter some of the epitopes’ structural integrity and mask some epitopes due to the steric hindrance of the carbohydrate group, thus reducing the proteins’ allergenicity.