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ICAR AICE-JRF/SRF Biochemistry for Dairy Science: practice questions

ICAR AICE-JRF/SRF (PhD): Dairy Chemistry, Dairy Microbiology, Dairy Technology, Dairy Engineering · India · NTA for ICAR

Original practice questions written to the published syllabus · not past papers
10worked here, free
22written to this exam in this subject
10syllabus units

What this subject covers

Carbohydrates, proteins, lipids, enzymes and metabolism at the level a dairy chemist and microbiologist needs before studying milk itself.

In the exams: Background for ICAR AICE subject 34 Units 1–3 and GATE XL-Q/XL-U Section 1

Where the 22 questions fall

How our questions for ICAR AICE-JRF/SRF spread across the units of Biochemistry for Dairy Science. Difficulty: 0 easy, 0 medium, 22 hard.

Enzyme inhibition and regulation3
Glycolysis, TCA cycle and oxidative phosphorylation3
Lipid and amino acid metabolism3
Water, pH and buffers2
Amino acids, peptides and protein structure2
Lipid classes and fatty acids2
Enzymes: classification and Michaelis-Menten kinetics2
Nucleic acids and protein synthesis2
Vitamins as coenzymes and minerals2
Carbohydrate structure and reactions1

10 practice questions, worked

Choose an answer, then open the working. Each explanation says why the right answer is right and why the others are not.

1 · Water, pH and buffers · hard

Milk triacylglycerols separate as globules instead of dissolving in the serum mainly because of:

  1. Strong covalent links between fat molecules that form during milk secretion
  2. Electrostatic attraction between positively charged fat molecules
  3. The hydrophobic effect
  4. The high density of milk fat compared with the aqueous phase
Answer and working

C. The hydrophobic effect

Non-polar molecules cannot hydrogen-bond with water, so the system minimises contact by clustering them. Milk fat is less dense than serum, which is why cream rises, but density does not explain insolubility.

Further reading: Nelson and Cox, Lehninger Principles of Biochemistry

2 · Water, pH and buffers · hard

Why does the measured pH of milk differ when it is measured at 20 °C and at 60 °C?

  1. Lactose hydrolyses to glucose and galactose above 50 °C, releasing acid into the milk serum
  2. Glass pH electrodes stop responding to hydrogen ions once milk exceeds 40 °C
  3. Heat alters the ionisation of water and buffer salts and precipitates calcium phosphate
  4. Heating destroys the hydrogen ions present in milk serum, so pH always rises
Answer and working

C. Heat alters the ionisation of water and buffer salts and precipitates calcium phosphate

Kw and the dissociation constants of phosphates and other buffers change with temperature, and calcium phosphate precipitates on heating, releasing H⁺. Lactose does not hydrolyse on simple heating.

Further reading: Fox et al., Dairy Chemistry and Biochemistry

3 · Amino acids, peptides and protein structure · hard

When milk is heated above about 70 °C, β-lactoglobulin forms complexes with κ-casein. The key chemical reaction is:

  1. Thiol–disulfide exchange involving β-lactoglobulin's exposed free thiol
  2. Maillard condensation between lactose and the N-terminal amino group of κ-casein
  3. Hydrolysis of the Phe105–Met106 bond of κ-casein
  4. Phosphorylation of β-lactoglobulin by casein kinase in the serum
Answer and working

A. Thiol–disulfide exchange involving β-lactoglobulin's exposed free thiol

Unfolding exposes the free thiol (Cys121) of β-lactoglobulin, which attacks disulfides of κ-casein. Phe105–Met106 cleavage is the chymosin reaction.

Further reading: Fox et al., Dairy Chemistry and Biochemistry

4 · Amino acids, peptides and protein structure · hard

Which amino acid residue in the casein chains carries the phosphate groups that bind calcium phosphate in the micelle?

  1. Serine
  2. Lysine
  3. Methionine
  4. Proline
Answer and working

A. Serine

Caseins are phosphorylated on serine residues (phosphoserine), often in clusters, in the Golgi. These clusters bind calcium and colloidal calcium phosphate.

Further reading: Fox et al., Dairy Chemistry and Biochemistry

5 · Lipid classes and fatty acids · hard

The main conjugated linoleic acid isomer in milk fat, rumenic acid, is:

  1. trans-10, cis-12 18:2
  2. cis-9, cis-12 18:2
  3. trans-9, trans-12 18:2
  4. cis-9, trans-11 18:2
Answer and working

D. cis-9, trans-11 18:2

Rumenic acid (c9,t11) forms in the rumen and, mainly, in the mammary gland from vaccenic acid by Δ9-desaturase. trans-10, cis-12 is the isomer linked with milk fat depression; c9,c12 is ordinary linoleic acid.

Further reading: Fox et al., Dairy Chemistry and Biochemistry

6 · Lipid classes and fatty acids · hard

Hydrolytic rancidity in raw milk is promoted by agitation, foaming or homogenisation before pasteurisation because these:

  1. Introduce oxygen that oxidises unsaturated fatty acids by a free-radical chain
  2. Raise the temperature enough to activate copper-catalysed oxidation
  3. Damage the globule membrane, exposing the fat to lipoprotein lipase
  4. Destroy the lipase so that free fatty acids cannot be esterified again
Answer and working

C. Damage the globule membrane, exposing the fat to lipoprotein lipase

Native lipoprotein lipase is mostly bound to casein; membrane damage exposes the fat to it, releasing free fatty acids (rancid, soapy flavour). Oxygen and copper drive oxidative rancidity, a different process.

Further reading: Fox et al., Dairy Chemistry and Biochemistry

7 · Enzymes: classification and Michaelis-Menten kinetics · hard

Why does stored UHT milk sometimes gel or turn bitter although the UHT process killed all vegetative bacteria?

  1. Chymosin from the cow's udder is reactivated by cooling after the UHT treatment
  2. Lactic acid bacteria regrow from heat-resistant spores formed during UHT treatment
  3. Heat-stable psychrotroph proteases survive UHT and act during storage
  4. Alkaline phosphatase hydrolyses casein when the pack is stored warm for weeks
Answer and working

C. Heat-stable psychrotroph proteases survive UHT and act during storage

Proteases of Pseudomonas and related psychrotrophs can retain activity after UHT. Together with plasmin they hydrolyse casein, causing age gelation and bitterness.

Further reading: Fox et al., Dairy Chemistry and Biochemistry

8 · Glycolysis, TCA cycle and oxidative phosphorylation · hard

Using P/O ratios of 2.5 for NADH and 1.5 for FADH₂, how many ATP are obtained from the complete oxidation of one acetyl-CoA in the TCA cycle?

  1. 12
  2. 10
  3. 15
  4. 8
Answer and working

B. 10

3 NADH × 2.5 = 7.5; 1 FADH₂ × 1.5 = 1.5; 1 GTP = 1; total 10. The older ratios (3 and 2) give 12.

Further reading: Nelson and Cox, Lehninger Principles of Biochemistry

9 · Nucleic acids and protein synthesis · hard

In the mammary epithelial cell, the caseins are phosphorylated and assembled into micelles in the:

  1. Golgi apparatus and secretory vesicles
  2. Nucleus
  3. Mitochondria
  4. Cytosol, while translation on free ribosomes is still under way
Answer and working

A. Golgi apparatus and secretory vesicles

Secreted proteins pass from the rough ER to the Golgi, where casein kinase phosphorylates serines and micelles form with calcium phosphate.

Further reading: Fox et al., Dairy Chemistry and Biochemistry

10 · Vitamins as coenzymes and minerals · hard

Cobalamin (vitamin B12) is the coenzyme of methylmalonyl-CoA mutase. This enzyme is needed in the metabolism of:

  1. Glucose to pyruvate in glycolysis
  2. Propionyl-CoA from odd-chain fatty acids
  3. Acetyl-CoA to malonyl-CoA for fatty acid synthesis
  4. Ammonia to urea
Answer and working

B. Propionyl-CoA from odd-chain fatty acids

Propionyl-CoA is carboxylated to methylmalonyl-CoA and rearranged to succinyl-CoA by the B12 enzyme; in ruminants this is how propionate becomes glucose.

Further reading: Nelson and Cox, Lehninger Principles of Biochemistry

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Read the subject

Biochemistry for Dairy ScienceThe full study manual, free ICAR AICE-JRF/SRFFormat, sections and how it has changed

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