One sample of the globular protein peroxidase is hydrolyzed by heating with 6 M HC1. A second sample is denatured by treatment with acetone. a) How does the peroxidase structure change during hydrolysis? Will this change the biological activity of peroxidase? b) How does the peroxidase structure change during denatur-ation? Will this change the biological activity of perox-idase? c) Are either of these processes likely to be reversible?
Enzyme kinetics
In biochemistry, enzymes are proteins that act as biological catalysts. Catalysis is the addition of a catalyst to a chemical reaction to speed up the pace of the reaction. Catalysis can be categorized as either homogeneous or heterogeneous, depending on whether the catalysts are distributed in the same phase as that of the reactants. Enzymes are an essential part of the cell because, without them, many organic processes would slow down and thus will affect the processes that are important for cell survival and sustenance.
Regulation of Enzymes
A substance that acts as a catalyst to regulate the reaction rate in the living organism's metabolic pathways without itself getting altered is an enzyme. Most of the biological reactions and metabolic pathways in the living systems are carried out by enzymes. They are specific for their works and work in particular conditions. It maintains the best possible rate of reaction in the most stable state. The enzymes have distinct properties as they can proceed with the reaction in any direction, their particular binding sites, pH specificity, temperature specificity required in very few amounts.
One sample of the globular protein peroxidase is hydrolyzed by heating with 6 M HC1.
A second sample is denatured by treatment
with acetone.
a)
How does the peroxidase structure change during hydrolysis?
Will this change the biological activity of peroxidase?
b)
How does the peroxidase structure change during denatur-ation? Will this change the biological activity of perox-idase?
c)
Are either of these processes likely to be reversible?
Denaturation is the process of loss of native conformation of the proteins.
The agents for denaturation are of two types:
Physical agents such as heat, UV, and X-rays.
The chemical agents bringing out denaturation are organic solvents like alcohol, ether, acids, and alkalies.
Denaturation may result in the loss of the secondary, tertiary, and quarternary structure of the protein.
Denaturation is responsible for the breaking of electrostatic interactions, H-bonds, van der Waals force of interactions, hydrophobic interactions, and disulfide bonds. It is not involved in the breaking of peptide bonds.
Protein hydrolysis can be made possible by chemical or enzymatic methods.
Enzymes used for hydrolysis are such as pepsin, chymotrypsin, trypsin, etc.
The process of chemical hydrolysis involves the treatment of peptides either with a strong acid or a strong base.
In acid hydrolysis, the peptide is heated with 6 M HCl at 110C for 24 hours.
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