7. 4 Points Give an example of a food processing treatment which results in prot

Question

7. 4 Points Give an example of a food processing treatment which results in protein hydrolysis. Discuss the effects of the processing treatment on the 1°, 20, and 3° structure of the protein. Identify the bonds that are altered by the processing treatment 8. 5 points For some proteins, mild heat denaturation, improves the functional properties of the protein. Identify a functional property in which mild denaturation improves a protein's functional property. Discuss how the changes in protein structure that occur during denaturation are beneficial

Explanation / Answer

1) Protein hydrolysis is used in food processing industry in order to improve the quality of food.

Protein hydrolysis may occur due to the presence of proteinases present in the food itself.

Example : autolytic reactions in the meat

Protein hydrolysis may occur due to the microbial proteinases

Example : Addition of pure cultures of selected microorganisms during the production of cheese.

There are two subgroups for protein hydrolysis :

a) Exopeptidases : which cleave the peptide bonds from the terminal ends of protein

b) Endopeptidases : which hydrolyse the linkages within the peptide chain and not attacking the terminal end side of a protein.

Primary structure of a protein : Mainly contains specific amino acids joined by peptide bonds along the protein chain. During protein hydrolysis of food processing treatment, this disrupts the peptide bonds in the protein either by exopeptidases or endopeptidases

Secondary structure of a protein : It is 3d organisation of a segments of a polypeptide chain either in

alpha-helix - stabilised by intrachain hydrogen bonds

beta pleated sheet - interchain hydrogen bonds

or random coil. - it is formed when amino acids side chains prevent to form either alpha or beta form

This protein hydrolysis of food processing treatment effects the secondary structure by disrupting the hydrogen bonds between the amide groups

Teritary structure : It is also 3-dimensional structure of a complete protein chain. In this structure there are 4 types of bonds present between side chains :

a) hydrogen bonding

b) salt bridges

c) disulphide bonds

d) Non polar hydrophobic interactions

All these above bonds may get disrupted.

2) Mild heat denaturation of proteins improves the functional properties of a protein.

For example in case of mild heat degeneration of protein structures leads to unfolding of a protein to expose the hydrophobic groups and also cause irreversible aggregation.

This increases the hydrodynamic radius of a protein molecule which increases the viscosity of a solution.

Under mild pH denaturation some portion of a protein molecule were made susceptible to proteolysis.

Example : Ribonucleases

Whereas mild acid induced degeneration leads to surface hydrophobicity increased induced by deamidation without disrupting the peptide bonds.

Example : Soy protein under mild acid degeneration increases the functional properties of protein like solubility, emulsifying properties and foaming properties.

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