Chemistry NCERT Exemplar Solutions Class 12th Chapter Fourteen

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When an egg is cooked, the soluble globular protein albumin transforms into an insoluble fibrous protein. Bioactivity is lost throughout the denaturation process.

(ii) Albumin protein's secondary and tertiary structures are destroyed, but the primary structure (which contains the -amino acid sequence) is unaffected.

Although egg white is a fluid Ans, when it is cooked, the proteins get denatured and solidify as a result of coagulation.

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Enzyme active sites bind the substrate molecule in a favourable location so that the reagent may attack it effectively. At each site in an enzyme, there is a substrate binding site to which the substrate binds and the reaction then proceeds.

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Starch has α - glucose units, and cellulose has β−D− glucose units. In starch and glycogen, there is α−I glycosidic linkage, and in cellulose, there is glycosidic connection β - between glucose units.

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Two monosaccharide molecules are linked by an oxide bond generated by the loss of a water molecule. Glycosidic linkage is the joining of two monosaccharide units by an oxygen atom.

Disaccharides, trisaccharides, and polysaccharides all have glycosidic linkage.

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Nucleosides are linked to phosphoric acid at the 5′ position of the sugar moiety to produce a nucleotide. Furthermore, phosphodiester linkage between the 5′ and 3′ carbon atoms of pentose sugar bonds nucleotides (two molecules) together to generate dinucleotide. Phosphoric acid aids in the formation of this connection.

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Glucose reacts with hydroxylamine to form a monoxime, which is then combined with one molecule of hydrogen cyanide to form cyanohydrin. The reactions are shown in the table below.

It has a carbonyl group as a consequence, which can be an aldehyde or a ketone. Gluconic acid, a carboxylic acid containing six carbon atoms, is formed when glucose is gently oxidised with bromine water.

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Biocatalysts are enzymes that act as catalysts in biological reactions. They reduce the size of activation energy by finding a suitable path. Because the enzyme sucrase reduces the activation energy of sucrose hydrolysis from to, enzyme-catalyzed reactions occur at a much faster rate than traditionally catalysed ones. 

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Physical or chemical changes damage hydrogen bonding and other attractive factors. In addition, globules uncoil and the helix uncoils, resulting in a thread-like molecule. As a result, the biological activity of protein secondary and tertiary structures is lost entirely or partially. Protein denaturation is the term for this.

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Since both acidic (−COOH) and basic (−NH₂) groups present in amino acids, it act like salts rather than simple amines or carboxylic acids. In Ans, a −COOH a group can release a proton and an amine group can take a proton, resulting in the formation of a dipolar ion known as zwitterion.