Multiple Choice
1. C Bile emulsification is physical digestion. Bile salts are detergent-like molecules that break large fat globules into tiny droplets, increasing surface area for lipase action. No chemical bonds in fat molecules are broken by bile. Bile does not contain lipase (that is the pancreas) and its neutralising effect is from bicarbonate ions, not bile salts.
2. A Pancreatic lipase is the primary fat-digesting enzyme in the small intestine. Fat digestion only begins in the small intestine (after bile emulsification), so a lipase deficiency would manifest there. Fats would pass through undigested, causing fatty stools (steatorrhoea).
3. D Pepsinogen is secreted inactive to protect the gastric gland cells from self-digestion. The cells themselves are made of protein, if active pepsin were secreted directly, it could digest the cells that produce it. Activation only occurs in the stomach lumen (away from the cell) when HCl is present.
4. B Physical digestion increases surface area, which directly increases the rate of enzyme action. Enzymes can only act on substrate molecules they can access, an intact large food piece has a small surface area relative to its mass. Cutting it into smaller pieces exposes far more surface for simultaneous enzyme contact.
5. C Starch → maltose by salivary amylase (mouth) then pancreatic amylase (small intestine) → glucose + glucose by maltase (small intestine). Pepsin does not act on starch; amylase does not produce glucose directly; large intestine does not complete starch digestion.
Q6, Model Answer
In the mouth, protein is physically broken into smaller pieces by mastication (chewing) to increase surface area. No chemical digestion of protein occurs in the mouth, salivary amylase only acts on starch.
In the stomach (pH ~1.5–3.5), gastric glands secrete pepsinogen and hydrochloric acid (HCl). HCl activates pepsinogen to pepsin. Pepsin is a protease with an optimum pH of ~2, it cleaves peptide bonds within protein chains, producing shorter polypeptides.
In the small intestine (pH ~7.5, neutralised by NaHCO₃ from the pancreas), the pancreas secretes trypsin and chymotrypsin, which continue cleaving polypeptides into shorter peptide fragments. Pepsin is denatured at this pH and ceases to function.
Peptidases on the brush border of the intestinal epithelium cleave the remaining peptide bonds, producing individual amino acids, the final absorbable products.
Q7, Model Answer
The stomach must maintain pH ~2 for two reasons: first, this activates pepsinogen to active pepsin (pepsin has an optimum pH of ~2 and is only functional in strongly acidic conditions); second, the acidic environment kills most bacteria and pathogens present in ingested food.
A pH of 2 in the small intestine would be harmful because pancreatic enzymes (amylase, lipase, trypsin, chymotrypsin) have pH optima around 7–8 and would be denatured or strongly inhibited at pH 2. This would prevent digestion of carbohydrates, fats, and proteins in the small intestine. To prevent this, the pancreas secretes sodium bicarbonate into the duodenum, which neutralises the acidic chyme and raises pH to approximately 7.5 before pancreatic enzymes act.
Q8, Model Answer
Physical digestion breaks food into smaller pieces without altering the chemical structure of the molecules, no bonds are broken and no new products are formed. An example is bile emulsification in the small intestine: bile salts break large fat globules into tiny droplets, increasing the surface area of fat available for enzyme action, but the triglyceride molecules themselves are chemically unchanged.
Chemical digestion breaks covalent bonds within food molecules using enzymes via hydrolysis reactions, converting large insoluble polymers into small soluble monomers. An example is pepsin acting on proteins in the stomach (pH ~2): pepsin cleaves peptide bonds within protein chains, converting proteins into shorter polypeptides.
Physical digestion supports chemical digestion by increasing the surface area of food available for enzyme contact. Since enzyme reactions occur at the surface of substrate molecules, a smaller particle size means more substrate surface is simultaneously accessible, dramatically increasing the rate of chemical digestion. Without physical digestion, enzyme action would be limited to the outer surface of large food pieces, significantly slowing the overall process.